| 5hfn-pdb | HEADER HYDROLASE 07-JAN-16 5HFN
TITLE CRYSTAL STRUCTURE OF A LOOP TRUNCATION VARIANT OF THERMOTOGA MARITIMA
TITLE 2 ACETYL ESTERASE TM0077 (APO STRUCTURE) AT 2.75 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEPHALOSPORIN-C DEACETYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ACETYLXYLAN ESTERASE;
COMPND 5 EC: 3.1.1.41,3.1.1.72;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: THE CRYSTALLIZED CONSTRUCT IS A TRUNCATED MUTANT
COMPND 9 CONTAINING A DELETION OF RESIDUE NUMBERS 120-145 OF THE FULL LENGTH
COMPND 10 PROTEIN.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA (STRAIN ATCC 43589 / MSB8 /
SOURCE 3 DSM 3109 / JCM 10099);
SOURCE 4 ORGANISM_TAXID: 243274;
SOURCE 5 STRAIN: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
SOURCE 6 GENE: AXEA, TM_0077;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PMH1
KEYWDS HYDROLASE, CARBOHYDRATE METABOLISM, CEPHALOSPORIN C DEACETYLASE,
KEYWDS 2 ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MANOJ,M.K.SINGH
REVDAT 1 25-MAY-16 5HFN 0
JRNL AUTH M.K.SINGH,N.MANOJ
JRNL TITL AN EXTENDED LOOP IN CE7 CARBOHYDRATE ESTERASE FAMILY IS
JRNL TITL 2 DISPENSABLE FOR OLIGOMERIZATION BUT REQUIRED FOR ACTIVITY
JRNL TITL 3 AND THERMOSTABILITY
JRNL REF J.STRUCT.BIOL. V. 194 434 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 27085421
JRNL DOI 10.1016/J.JSB.2016.04.008
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 56965
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3028
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4168
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 237
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13206
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 1.43000
REMARK 3 B12 (A**2) : -0.22000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.312
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.250
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.666
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13636 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12720 ; 0.012 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18540 ; 1.816 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 29182 ; 1.677 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1670 ; 6.397 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 635 ;30.734 ;23.087
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2039 ;13.752 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;15.420 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1980 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15514 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3354 ; 0.011 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6704 ; 1.087 ; 1.916
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6703 ; 1.085 ; 1.915
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8351 ; 1.825 ; 2.865
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 15
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 323 B 4 323 32424 0.070 0.050
REMARK 3 2 A 3 323 C 3 323 32372 0.060 0.050
REMARK 3 3 A 2 322 D 2 322 32444 0.060 0.050
REMARK 3 4 A 2 323 E 2 323 33312 0.050 0.050
REMARK 3 5 A 4 322 F 4 322 32582 0.070 0.050
REMARK 3 6 B 4 322 C 4 322 32440 0.070 0.050
REMARK 3 7 B 4 322 D 4 322 32068 0.060 0.050
REMARK 3 8 B 4 322 E 4 322 32784 0.060 0.050
REMARK 3 9 B 4 323 F 4 323 32672 0.080 0.050
REMARK 3 10 C 4 322 D 4 322 32678 0.050 0.050
REMARK 3 11 C 4 323 E 4 323 32790 0.050 0.050
REMARK 3 12 C 4 323 F 4 323 33190 0.060 0.050
REMARK 3 13 D 2 322 E 2 322 32940 0.050 0.050
REMARK 3 14 D 4 322 F 4 322 32938 0.060 0.050
REMARK 3 15 E 4 323 F 4 323 33112 0.060 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5522 120.2026 47.1507
REMARK 3 T TENSOR
REMARK 3 T11: 0.2646 T22: 0.3301
REMARK 3 T33: 0.3776 T12: 0.0795
REMARK 3 T13: -0.0021 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 5.6376 L22: 1.7166
REMARK 3 L33: 1.8778 L12: 0.7138
REMARK 3 L13: 2.6642 L23: 0.1785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0334 S12: -1.0480 S13: 0.1890
REMARK 3 S21: 0.4013 S22: 0.0975 S23: -0.1040
REMARK 3 S31: -0.0728 S32: -0.5666 S33: -0.0641
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 179 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9091 111.3750 36.5525
REMARK 3 T TENSOR
REMARK 3 T11: 0.1239 T22: 0.2110
REMARK 3 T33: 0.3277 T12: 0.0312
REMARK 3 T13: -0.0424 T23: 0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 3.2191 L22: 1.1985
REMARK 3 L33: 2.1247 L12: -0.3430
REMARK 3 L13: -0.3878 L23: 0.0712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0650 S12: -0.0318 S13: -0.1067
REMARK 3 S21: -0.0089 S22: 0.1206 S23: 0.0966
REMARK 3 S31: 0.0791 S32: -0.1490 S33: -0.0557
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 158
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8362 67.5308 43.9186
REMARK 3 T TENSOR
REMARK 3 T11: 0.1460 T22: 0.2376
REMARK 3 T33: 0.6028 T12: 0.0032
REMARK 3 T13: -0.0132 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.3350 L22: 1.3203
REMARK 3 L33: 2.9788 L12: 0.2281
REMARK 3 L13: -0.5346 L23: 0.3018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0443 S12: 0.2050 S13: -0.1122
REMARK 3 S21: -0.0624 S22: -0.0479 S23: 0.3546
REMARK 3 S31: 0.2687 S32: 0.0876 S33: 0.0922
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 159 B 323
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3204 74.8580 35.1757
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.2783
REMARK 3 T33: 0.4562 T12: 0.0080
REMARK 3 T13: -0.1331 T23: 0.0814
REMARK 3 L TENSOR
REMARK 3 L11: 0.9562 L22: 2.7111
REMARK 3 L33: 2.0297 L12: -0.1383
REMARK 3 L13: -0.6355 L23: 0.3803
REMARK 3 S TENSOR
REMARK 3 S11: 0.1230 S12: 0.3612 S13: -0.0670
REMARK 3 S21: -0.3448 S22: -0.1446 S23: 0.3312
REMARK 3 S31: -0.1160 S32: -0.1712 S33: 0.0216
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 189
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8840 71.3182 14.5223
REMARK 3 T TENSOR
REMARK 3 T11: 0.4057 T22: 0.4874
REMARK 3 T33: 0.4562 T12: -0.1199
REMARK 3 T13: 0.1886 T23: -0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 1.5196 L22: 5.8177
REMARK 3 L33: 1.6353 L12: -0.2161
REMARK 3 L13: 0.0406 L23: -1.0369
REMARK 3 S TENSOR
REMARK 3 S11: -0.0588 S12: 0.3461 S13: 0.0167
REMARK 3 S21: -0.5706 S22: -0.0067 S23: -1.0690
REMARK 3 S31: -0.3156 S32: 0.4234 S33: 0.0656
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 190 C 323
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4838 80.7255 15.6555
REMARK 3 T TENSOR
REMARK 3 T11: 0.4236 T22: 0.3446
REMARK 3 T33: 0.2889 T12: -0.0355
REMARK 3 T13: 0.0139 T23: 0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 2.2913 L22: 4.0623
REMARK 3 L33: 0.7759 L12: 0.6695
REMARK 3 L13: 0.2528 L23: 0.4091
REMARK 3 S TENSOR
REMARK 3 S11: -0.0733 S12: 0.2949 S13: 0.2393
REMARK 3 S21: -0.6999 S22: 0.1777 S23: 0.0665
REMARK 3 S31: -0.2538 S32: 0.0958 S33: -0.1044
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -2 D 189
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6133 90.7205 69.8409
REMARK 3 T TENSOR
REMARK 3 T11: 0.5167 T22: 0.2017
REMARK 3 T33: 0.4302 T12: 0.0155
REMARK 3 T13: 0.1880 T23: -0.1226
REMARK 3 L TENSOR
REMARK 3 L11: 4.7424 L22: 2.0752
REMARK 3 L33: 2.3104 L12: 0.5939
REMARK 3 L13: 1.2781 L23: 0.1312
REMARK 3 S TENSOR
REMARK 3 S11: -0.0782 S12: -0.2976 S13: 0.6349
REMARK 3 S21: 0.3756 S22: -0.0032 S23: 0.4292
REMARK 3 S31: -0.6335 S32: -0.0983 S33: 0.0814
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 190 D 323
REMARK 3 ORIGIN FOR THE GROUP (A): 37.6525 85.3454 69.4939
REMARK 3 T TENSOR
REMARK 3 T11: 0.3580 T22: 0.2241
REMARK 3 T33: 0.2189 T12: 0.0061
REMARK 3 T13: 0.0124 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 3.6504 L22: 2.9702
REMARK 3 L33: 1.0985 L12: 0.9938
REMARK 3 L13: -0.1690 L23: 0.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.1946 S12: -0.4036 S13: 0.2254
REMARK 3 S21: 0.6196 S22: -0.0873 S23: -0.0291
REMARK 3 S31: -0.1723 S32: 0.2005 S33: -0.1073
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 2 E 189
REMARK 3 ORIGIN FOR THE GROUP (A): 51.1346 47.2624 36.7017
REMARK 3 T TENSOR
REMARK 3 T11: 0.1630 T22: 0.1335
REMARK 3 T33: 0.4208 T12: 0.0311
REMARK 3 T13: 0.0438 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 1.6842 L22: 2.5643
REMARK 3 L33: 3.0471 L12: 0.0289
REMARK 3 L13: -0.8085 L23: 1.1203
REMARK 3 S TENSOR
REMARK 3 S11: -0.1459 S12: 0.1257 S13: -0.1462
REMARK 3 S21: 0.0955 S22: 0.0368 S23: 0.0201
REMARK 3 S31: 0.0527 S32: -0.2212 S33: 0.1091
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 190 E 323
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7751 57.0540 48.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1767 T22: 0.1675
REMARK 3 T33: 0.3014 T12: 0.0560
REMARK 3 T13: -0.0573 T23: -0.0747
REMARK 3 L TENSOR
REMARK 3 L11: 2.1485 L22: 2.2013
REMARK 3 L33: 2.3263 L12: 0.2432
REMARK 3 L13: -0.7990 L23: 0.6123
REMARK 3 S TENSOR
REMARK 3 S11: -0.1254 S12: -0.1834 S13: -0.1013
REMARK 3 S21: 0.4034 S22: 0.1189 S23: -0.0650
REMARK 3 S31: 0.1328 S32: 0.0932 S33: 0.0065
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 4 F 218
REMARK 3 ORIGIN FOR THE GROUP (A): 78.0523 102.2749 43.9816
REMARK 3 T TENSOR
REMARK 3 T11: 0.1254 T22: 0.2253
REMARK 3 T33: 0.5696 T12: -0.0068
REMARK 3 T13: -0.0081 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 2.3431 L22: 4.7694
REMARK 3 L33: 0.9753 L12: -1.4854
REMARK 3 L13: 0.3397 L23: -0.7909
REMARK 3 S TENSOR
REMARK 3 S11: 0.1124 S12: 0.3969 S13: 0.2843
REMARK 3 S21: -0.3606 S22: -0.2175 S23: -0.6907
REMARK 3 S31: 0.0597 S32: 0.1763 S33: 0.1051
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 219 F 323
REMARK 3 ORIGIN FOR THE GROUP (A): 71.0864 90.6681 52.4644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1107 T22: 0.1388
REMARK 3 T33: 0.4059 T12: 0.0076
REMARK 3 T13: -0.0743 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 1.9885 L22: 3.0762
REMARK 3 L33: 2.0695 L12: -1.1477
REMARK 3 L13: -0.5056 L23: 0.4062
REMARK 3 S TENSOR
REMARK 3 S11: -0.1418 S12: 0.0323 S13: -0.1120
REMARK 3 S21: 0.3627 S22: 0.0173 S23: -0.1401
REMARK 3 S31: 0.1184 S32: -0.0529 S33: 0.1245
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5HFN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : DOUBLE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.30
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60062
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 52.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.90
REMARK 200 R MERGE FOR SHELL (I) : 1.17400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5FDF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION IS COMPOSED OF
REMARK 280 35%(V/V) PENTAERYTHRITOLPROPOXYLATE (5/4 PO/OH), 200MM POTASSIUM
REMARK 280 CHLORIDE, 50MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.03333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 110.06667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 110.06667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.03333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 91
REMARK 465 TYR A 92
REMARK 465 ASN A 93
REMARK 465 GLY A 94
REMARK 465 ARG A 118
REMARK 465 GLY A 119
REMARK 465 THR A 146
REMARK 465 ARG A 147
REMARK 465 GLY A 148
REMARK 465 ILE A 149
REMARK 465 LEU A 150
REMARK 465 ASP A 151
REMARK 465 PRO A 152
REMARK 465 ARG A 153
REMARK 465 THR A 154
REMARK 465 TYR A 155
REMARK 465 LYS A 324
REMARK 465 GLY A 325
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PHE B 3
REMARK 465 GLY B 91
REMARK 465 TYR B 92
REMARK 465 ASN B 93
REMARK 465 GLY B 94
REMARK 465 GLY B 95
REMARK 465 GLY B 119
REMARK 465 THR B 146
REMARK 465 ARG B 147
REMARK 465 GLY B 148
REMARK 465 ILE B 149
REMARK 465 LEU B 150
REMARK 465 ASP B 151
REMARK 465 PRO B 152
REMARK 465 ARG B 153
REMARK 465 THR B 154
REMARK 465 TYR B 155
REMARK 465 LYS B 324
REMARK 465 GLY B 325
REMARK 465 MET C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLY C 91
REMARK 465 TYR C 92
REMARK 465 ASN C 93
REMARK 465 GLY C 94
REMARK 465 GLY C 95
REMARK 465 GLY C 119
REMARK 465 THR C 146
REMARK 465 ARG C 147
REMARK 465 GLY C 148
REMARK 465 ILE C 149
REMARK 465 LEU C 150
REMARK 465 ASP C 151
REMARK 465 PRO C 152
REMARK 465 ARG C 153
REMARK 465 THR C 154
REMARK 465 TYR C 155
REMARK 465 LYS C 324
REMARK 465 GLY C 325
REMARK 465 MET D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 GLY D 91
REMARK 465 TYR D 92
REMARK 465 ASN D 93
REMARK 465 GLY D 94
REMARK 465 GLY D 95
REMARK 465 ARG D 118
REMARK 465 GLY D 119
REMARK 465 THR D 146
REMARK 465 ARG D 147
REMARK 465 GLY D 148
REMARK 465 ILE D 149
REMARK 465 LEU D 150
REMARK 465 ASP D 151
REMARK 465 PRO D 152
REMARK 465 ARG D 153
REMARK 465 THR D 154
REMARK 465 TYR D 155
REMARK 465 LYS D 324
REMARK 465 GLY D 325
REMARK 465 MET E -11
REMARK 465 GLY E -10
REMARK 465 SER E -9
REMARK 465 ASP E -8
REMARK 465 LYS E -7
REMARK 465 ILE E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 GLY E 91
REMARK 465 TYR E 92
REMARK 465 ASN E 93
REMARK 465 GLY E 94
REMARK 465 GLY E 95
REMARK 465 ARG E 118
REMARK 465 GLY E 119
REMARK 465 THR E 146
REMARK 465 ARG E 147
REMARK 465 GLY E 148
REMARK 465 ILE E 149
REMARK 465 LEU E 150
REMARK 465 ASP E 151
REMARK 465 PRO E 152
REMARK 465 ARG E 153
REMARK 465 THR E 154
REMARK 465 TYR E 155
REMARK 465 LYS E 324
REMARK 465 GLY E 325
REMARK 465 MET F -11
REMARK 465 GLY F -10
REMARK 465 SER F -9
REMARK 465 ASP F -8
REMARK 465 LYS F -7
REMARK 465 ILE F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 PHE F 3
REMARK 465 GLY F 91
REMARK 465 TYR F 92
REMARK 465 ASN F 93
REMARK 465 GLY F 94
REMARK 465 GLY F 119
REMARK 465 THR F 146
REMARK 465 ARG F 147
REMARK 465 GLY F 148
REMARK 465 ILE F 149
REMARK 465 LEU F 150
REMARK 465 ASP F 151
REMARK 465 PRO F 152
REMARK 465 ARG F 153
REMARK 465 THR F 154
REMARK 465 TYR F 155
REMARK 465 LYS F 324
REMARK 465 GLY F 325
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 3 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 9 CG CD OE1 OE2
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 26 CG CD OE1 OE2
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 PHE A 38 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 ARG A 65 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 ILE A 90 CG1 CG2 CD1
REMARK 470 ASP A 116 CG OD1 OD2
REMARK 470 THR A 117 OG1 CG2
REMARK 470 TYR A 156 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 159 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 189 CG CD OE1 NE2
REMARK 470 LYS A 202 CG CD CE NZ
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 TYR B 19 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 22 CG CD CE NZ
REMARK 470 GLU B 26 CG CD OE1 OE2
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 GLU B 48 CG CD OE1 OE2
REMARK 470 GLU B 79 CG CD OE1 OE2
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 ASP B 116 CG OD1 OD2
REMARK 470 THR B 117 OG1 CG2
REMARK 470 ARG B 118 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 159 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 189 CG CD OE1 NE2
REMARK 470 LYS B 202 CG CD CE NZ
REMARK 470 ARG B 218 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 244 CG CD OE1 OE2
REMARK 470 ARG B 248 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 263 CG CD CE NZ
REMARK 470 LYS B 320 CG CD CE NZ
REMARK 470 PHE C 3 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 9 CG CD OE1 OE2
REMARK 470 ARG C 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 TYR C 19 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 22 CG CD CE NZ
REMARK 470 GLU C 30 CG CD OE1 OE2
REMARK 470 GLU C 48 CG CD OE1 OE2
REMARK 470 GLU C 81 CG CD OE1 OE2
REMARK 470 LYS C 82 CG CD CE NZ
REMARK 470 ASP C 116 CG OD1 OD2
REMARK 470 THR C 117 OG1 CG2
REMARK 470 ARG C 158 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 159 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 202 CG CD CE NZ
REMARK 470 LYS C 203 CG CD CE NZ
REMARK 470 ARG C 218 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 244 CG CD OE1 OE2
REMARK 470 ARG C 248 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 263 CG CD CE NZ
REMARK 470 GLU C 323 CG CD OE1 OE2
REMARK 470 HIS D -2 CG ND1 CD2 CE1 NE2
REMARK 470 HIS D -1 CG ND1 CD2 CE1 NE2
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 TYR D 19 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 22 CG CD CE NZ
REMARK 470 GLU D 30 CG CD OE1 OE2
REMARK 470 LYS D 37 CG CD CE NZ
REMARK 470 ARG D 46 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 48 CG CD OE1 OE2
REMARK 470 ARG D 65 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 67 CG CD OE1 NE2
REMARK 470 GLU D 79 CG CD OE1 OE2
REMARK 470 GLU D 81 CG CD OE1 OE2
REMARK 470 LYS D 82 CG CD CE NZ
REMARK 470 ILE D 90 CG1 CG2 CD1
REMARK 470 ASP D 116 CG OD1 OD2
REMARK 470 ARG D 158 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 159 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 202 CG CD CE NZ
REMARK 470 ARG D 218 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 225 CG OD1 OD2
REMARK 470 GLU D 244 CG CD OE1 OE2
REMARK 470 ARG D 248 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 263 CG CD CE NZ
REMARK 470 ASN D 302 CG OD1 ND2
REMARK 470 GLU E 17 CG CD OE1 OE2
REMARK 470 TYR E 19 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS E 22 CG CD CE NZ
REMARK 470 LYS E 37 CG CD CE NZ
REMARK 470 GLU E 79 CG CD OE1 OE2
REMARK 470 GLU E 80 CG CD OE1 OE2
REMARK 470 ILE E 90 CG1 CG2 CD1
REMARK 470 ASP E 116 CG OD1 OD2
REMARK 470 THR E 117 OG1 CG2
REMARK 470 ARG E 159 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 202 CG CD CE NZ
REMARK 470 ARG E 218 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 237 CG CD CE NZ
REMARK 470 LYS E 263 CG CD CE NZ
REMARK 470 LYS E 320 CG CD CE NZ
REMARK 470 GLU F 9 CG CD OE1 OE2
REMARK 470 LYS F 22 CG CD CE NZ
REMARK 470 LYS F 37 CG CD CE NZ
REMARK 470 ARG F 46 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 48 CG CD OE1 OE2
REMARK 470 GLU F 81 CG CD OE1 OE2
REMARK 470 ARG F 158 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 202 CG CD CE NZ
REMARK 470 GLU F 244 CG CD OE1 OE2
REMARK 470 LYS F 263 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER B 188 CB SER B 188 OG -0.089
REMARK 500 SER C 188 CB SER C 188 OG -0.081
REMARK 500 GLU F 313 CD GLU F 313 OE2 -0.074
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 241 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 MET B 115 CB - CG - SD ANGL. DEV. = -18.4 DEGREES
REMARK 500 ASP B 241 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP C 241 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP D 241 CB - CG - OD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 MET E 47 CG - SD - CE ANGL. DEV. = 10.8 DEGREES
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG F 118 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG F 118 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 GLU F 180 CG - CD - OE1 ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG F 218 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 GLU F 231 OE1 - CD - OE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP F 241 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG F 248 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU F 313 CG - CD - OE1 ANGL. DEV. = 12.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 188 -120.87 57.06
REMARK 500 VAL A 211 51.32 34.78
REMARK 500 LEU A 214 34.97 73.08
REMARK 500 HIS A 239 67.27 -119.73
REMARK 500 ASN A 302 -144.90 -89.28
REMARK 500 SER B 188 -125.47 57.46
REMARK 500 VAL B 211 53.45 37.60
REMARK 500 LEU B 214 33.98 71.08
REMARK 500 ASN B 302 -144.10 -87.00
REMARK 500 SER C 188 -122.84 58.70
REMARK 500 VAL C 211 54.11 37.37
REMARK 500 LEU C 214 34.00 72.03
REMARK 500 HIS C 239 69.18 -117.54
REMARK 500 ASN C 302 -145.70 -88.32
REMARK 500 ALA D 2 -100.64 -130.24
REMARK 500 PHE D 4 -14.50 -140.57
REMARK 500 SER D 188 -121.59 55.94
REMARK 500 VAL D 211 54.88 36.03
REMARK 500 LEU D 214 36.17 70.44
REMARK 500 HIS D 239 68.67 -118.54
REMARK 500 ASN D 302 -143.98 -85.77
REMARK 500 SER E 188 -123.30 57.38
REMARK 500 VAL E 211 53.14 35.81
REMARK 500 HIS E 239 68.93 -119.62
REMARK 500 ASN E 302 -146.95 -88.16
REMARK 500 SER F 188 -124.92 56.80
REMARK 500 VAL F 211 56.48 36.09
REMARK 500 LEU F 214 33.85 70.93
REMARK 500 HIS F 239 67.16 -116.05
REMARK 500 ASN F 302 -141.85 -86.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FDF RELATED DB: PDB
REMARK 900 5FDF CONTAINS THE FULL LENGTH NATIVE PROTEIN IN A DIFFERENT CRYSTAL
REMARK 900 FORM (APO STRUCTURE)
REMARK 900 RELATED ID: 1VLQ RELATED DB: PDB
REMARK 900 1VLQ CONTAINS THE SAME FULL LENGTH SELENOMETHIONINE PROTEIN IN A
REMARK 900 DIFFERENT CRYSTAL FORM (APO STRUCTURE)
REMARK 900 RELATED ID: 3M81 RELATED DB: PDB
REMARK 900 3M81 CONTAINS THE SAME FULL LENGTH NATIVE PROTEIN IN A DIFFERENT
REMARK 900 CRYSTAL FORM (APO STRUCTURE)
REMARK 900 RELATED ID: 3M82 RELATED DB: PDB
REMARK 900 3M82 CONTAINS THE SAME FULL LENGTH NATIVE PROTEIN COMPLEXED WITH AS
REMARK 900 PMSF INHIBITOR
REMARK 900 RELATED ID: 3M83 RELATED DB: PDB
REMARK 900 3M83 CONTAINS THE SAME FULL LENGTH NATIVE PROTEIN COMPLEXED WITH
REMARK 900 PARAOXON INHIBITOR
DBREF 5HFN A 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5HFN B 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5HFN C 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5HFN D 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5HFN E 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5HFN F 1 325 UNP Q9WXT2 CAH_THEMA 1 325
SEQADV 5HFN MET A -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5HFN GLY A -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN SER A -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ASP A -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN LYS A -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ILE A -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS A -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS A -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS A -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS A -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS A -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS A 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN A UNP Q9WXT2 GLN 120 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLY 121 DELETION
SEQADV 5HFN A UNP Q9WXT2 SER 122 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLY 123 DELETION
SEQADV 5HFN A UNP Q9WXT2 TRP 124 DELETION
SEQADV 5HFN A UNP Q9WXT2 LEU 125 DELETION
SEQADV 5HFN A UNP Q9WXT2 LYS 126 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLY 127 DELETION
SEQADV 5HFN A UNP Q9WXT2 ASP 128 DELETION
SEQADV 5HFN A UNP Q9WXT2 THR 129 DELETION
SEQADV 5HFN A UNP Q9WXT2 PRO 130 DELETION
SEQADV 5HFN A UNP Q9WXT2 ASP 131 DELETION
SEQADV 5HFN A UNP Q9WXT2 TYR 132 DELETION
SEQADV 5HFN A UNP Q9WXT2 PRO 133 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLU 134 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLY 135 DELETION
SEQADV 5HFN A UNP Q9WXT2 PRO 136 DELETION
SEQADV 5HFN A UNP Q9WXT2 VAL 137 DELETION
SEQADV 5HFN A UNP Q9WXT2 ASP 138 DELETION
SEQADV 5HFN A UNP Q9WXT2 PRO 139 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLN 140 DELETION
SEQADV 5HFN A UNP Q9WXT2 TYR 141 DELETION
SEQADV 5HFN A UNP Q9WXT2 PRO 142 DELETION
SEQADV 5HFN A UNP Q9WXT2 GLY 143 DELETION
SEQADV 5HFN A UNP Q9WXT2 PHE 144 DELETION
SEQADV 5HFN A UNP Q9WXT2 MET 145 DELETION
SEQADV 5HFN MET B -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5HFN GLY B -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN SER B -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ASP B -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN LYS B -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ILE B -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS B -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS B -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS B -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS B -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS B -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS B 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN B UNP Q9WXT2 GLN 120 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLY 121 DELETION
SEQADV 5HFN B UNP Q9WXT2 SER 122 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLY 123 DELETION
SEQADV 5HFN B UNP Q9WXT2 TRP 124 DELETION
SEQADV 5HFN B UNP Q9WXT2 LEU 125 DELETION
SEQADV 5HFN B UNP Q9WXT2 LYS 126 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLY 127 DELETION
SEQADV 5HFN B UNP Q9WXT2 ASP 128 DELETION
SEQADV 5HFN B UNP Q9WXT2 THR 129 DELETION
SEQADV 5HFN B UNP Q9WXT2 PRO 130 DELETION
SEQADV 5HFN B UNP Q9WXT2 ASP 131 DELETION
SEQADV 5HFN B UNP Q9WXT2 TYR 132 DELETION
SEQADV 5HFN B UNP Q9WXT2 PRO 133 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLU 134 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLY 135 DELETION
SEQADV 5HFN B UNP Q9WXT2 PRO 136 DELETION
SEQADV 5HFN B UNP Q9WXT2 VAL 137 DELETION
SEQADV 5HFN B UNP Q9WXT2 ASP 138 DELETION
SEQADV 5HFN B UNP Q9WXT2 PRO 139 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLN 140 DELETION
SEQADV 5HFN B UNP Q9WXT2 TYR 141 DELETION
SEQADV 5HFN B UNP Q9WXT2 PRO 142 DELETION
SEQADV 5HFN B UNP Q9WXT2 GLY 143 DELETION
SEQADV 5HFN B UNP Q9WXT2 PHE 144 DELETION
SEQADV 5HFN B UNP Q9WXT2 MET 145 DELETION
SEQADV 5HFN MET C -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5HFN GLY C -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN SER C -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ASP C -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN LYS C -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ILE C -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS C -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS C -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS C -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS C -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS C -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS C 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN C UNP Q9WXT2 GLN 120 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLY 121 DELETION
SEQADV 5HFN C UNP Q9WXT2 SER 122 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLY 123 DELETION
SEQADV 5HFN C UNP Q9WXT2 TRP 124 DELETION
SEQADV 5HFN C UNP Q9WXT2 LEU 125 DELETION
SEQADV 5HFN C UNP Q9WXT2 LYS 126 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLY 127 DELETION
SEQADV 5HFN C UNP Q9WXT2 ASP 128 DELETION
SEQADV 5HFN C UNP Q9WXT2 THR 129 DELETION
SEQADV 5HFN C UNP Q9WXT2 PRO 130 DELETION
SEQADV 5HFN C UNP Q9WXT2 ASP 131 DELETION
SEQADV 5HFN C UNP Q9WXT2 TYR 132 DELETION
SEQADV 5HFN C UNP Q9WXT2 PRO 133 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLU 134 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLY 135 DELETION
SEQADV 5HFN C UNP Q9WXT2 PRO 136 DELETION
SEQADV 5HFN C UNP Q9WXT2 VAL 137 DELETION
SEQADV 5HFN C UNP Q9WXT2 ASP 138 DELETION
SEQADV 5HFN C UNP Q9WXT2 PRO 139 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLN 140 DELETION
SEQADV 5HFN C UNP Q9WXT2 TYR 141 DELETION
SEQADV 5HFN C UNP Q9WXT2 PRO 142 DELETION
SEQADV 5HFN C UNP Q9WXT2 GLY 143 DELETION
SEQADV 5HFN C UNP Q9WXT2 PHE 144 DELETION
SEQADV 5HFN C UNP Q9WXT2 MET 145 DELETION
SEQADV 5HFN MET D -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5HFN GLY D -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN SER D -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ASP D -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN LYS D -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ILE D -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS D -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS D -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS D -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS D -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS D -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS D 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN D UNP Q9WXT2 GLN 120 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLY 121 DELETION
SEQADV 5HFN D UNP Q9WXT2 SER 122 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLY 123 DELETION
SEQADV 5HFN D UNP Q9WXT2 TRP 124 DELETION
SEQADV 5HFN D UNP Q9WXT2 LEU 125 DELETION
SEQADV 5HFN D UNP Q9WXT2 LYS 126 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLY 127 DELETION
SEQADV 5HFN D UNP Q9WXT2 ASP 128 DELETION
SEQADV 5HFN D UNP Q9WXT2 THR 129 DELETION
SEQADV 5HFN D UNP Q9WXT2 PRO 130 DELETION
SEQADV 5HFN D UNP Q9WXT2 ASP 131 DELETION
SEQADV 5HFN D UNP Q9WXT2 TYR 132 DELETION
SEQADV 5HFN D UNP Q9WXT2 PRO 133 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLU 134 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLY 135 DELETION
SEQADV 5HFN D UNP Q9WXT2 PRO 136 DELETION
SEQADV 5HFN D UNP Q9WXT2 VAL 137 DELETION
SEQADV 5HFN D UNP Q9WXT2 ASP 138 DELETION
SEQADV 5HFN D UNP Q9WXT2 PRO 139 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLN 140 DELETION
SEQADV 5HFN D UNP Q9WXT2 TYR 141 DELETION
SEQADV 5HFN D UNP Q9WXT2 PRO 142 DELETION
SEQADV 5HFN D UNP Q9WXT2 GLY 143 DELETION
SEQADV 5HFN D UNP Q9WXT2 PHE 144 DELETION
SEQADV 5HFN D UNP Q9WXT2 MET 145 DELETION
SEQADV 5HFN MET E -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5HFN GLY E -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN SER E -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ASP E -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN LYS E -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ILE E -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS E -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS E -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS E -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS E -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS E -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS E 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN E UNP Q9WXT2 GLN 120 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLY 121 DELETION
SEQADV 5HFN E UNP Q9WXT2 SER 122 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLY 123 DELETION
SEQADV 5HFN E UNP Q9WXT2 TRP 124 DELETION
SEQADV 5HFN E UNP Q9WXT2 LEU 125 DELETION
SEQADV 5HFN E UNP Q9WXT2 LYS 126 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLY 127 DELETION
SEQADV 5HFN E UNP Q9WXT2 ASP 128 DELETION
SEQADV 5HFN E UNP Q9WXT2 THR 129 DELETION
SEQADV 5HFN E UNP Q9WXT2 PRO 130 DELETION
SEQADV 5HFN E UNP Q9WXT2 ASP 131 DELETION
SEQADV 5HFN E UNP Q9WXT2 TYR 132 DELETION
SEQADV 5HFN E UNP Q9WXT2 PRO 133 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLU 134 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLY 135 DELETION
SEQADV 5HFN E UNP Q9WXT2 PRO 136 DELETION
SEQADV 5HFN E UNP Q9WXT2 VAL 137 DELETION
SEQADV 5HFN E UNP Q9WXT2 ASP 138 DELETION
SEQADV 5HFN E UNP Q9WXT2 PRO 139 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLN 140 DELETION
SEQADV 5HFN E UNP Q9WXT2 TYR 141 DELETION
SEQADV 5HFN E UNP Q9WXT2 PRO 142 DELETION
SEQADV 5HFN E UNP Q9WXT2 GLY 143 DELETION
SEQADV 5HFN E UNP Q9WXT2 PHE 144 DELETION
SEQADV 5HFN E UNP Q9WXT2 MET 145 DELETION
SEQADV 5HFN MET F -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5HFN GLY F -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN SER F -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ASP F -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN LYS F -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN ILE F -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS F -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS F -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS F -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS F -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS F -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN HIS F 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5HFN F UNP Q9WXT2 GLN 120 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLY 121 DELETION
SEQADV 5HFN F UNP Q9WXT2 SER 122 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLY 123 DELETION
SEQADV 5HFN F UNP Q9WXT2 TRP 124 DELETION
SEQADV 5HFN F UNP Q9WXT2 LEU 125 DELETION
SEQADV 5HFN F UNP Q9WXT2 LYS 126 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLY 127 DELETION
SEQADV 5HFN F UNP Q9WXT2 ASP 128 DELETION
SEQADV 5HFN F UNP Q9WXT2 THR 129 DELETION
SEQADV 5HFN F UNP Q9WXT2 PRO 130 DELETION
SEQADV 5HFN F UNP Q9WXT2 ASP 131 DELETION
SEQADV 5HFN F UNP Q9WXT2 TYR 132 DELETION
SEQADV 5HFN F UNP Q9WXT2 PRO 133 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLU 134 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLY 135 DELETION
SEQADV 5HFN F UNP Q9WXT2 PRO 136 DELETION
SEQADV 5HFN F UNP Q9WXT2 VAL 137 DELETION
SEQADV 5HFN F UNP Q9WXT2 ASP 138 DELETION
SEQADV 5HFN F UNP Q9WXT2 PRO 139 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLN 140 DELETION
SEQADV 5HFN F UNP Q9WXT2 TYR 141 DELETION
SEQADV 5HFN F UNP Q9WXT2 PRO 142 DELETION
SEQADV 5HFN F UNP Q9WXT2 GLY 143 DELETION
SEQADV 5HFN F UNP Q9WXT2 PHE 144 DELETION
SEQADV 5HFN F UNP Q9WXT2 MET 145 DELETION
SEQRES 1 A 311 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 311 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 A 311 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 A 311 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 A 311 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 A 311 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 A 311 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 A 311 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 A 311 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 A 311 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 A 311 GLY THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 12 A 311 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 13 A 311 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 14 A 311 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 15 A 311 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 16 A 311 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 17 A 311 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 18 A 311 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 19 A 311 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 20 A 311 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 21 A 311 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 22 A 311 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 23 A 311 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 24 A 311 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 B 311 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 311 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 B 311 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 B 311 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 B 311 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 B 311 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 B 311 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 B 311 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 B 311 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 B 311 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 B 311 GLY THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 12 B 311 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 13 B 311 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 14 B 311 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 15 B 311 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 16 B 311 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 17 B 311 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 18 B 311 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 19 B 311 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 20 B 311 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 21 B 311 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 22 B 311 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 23 B 311 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 24 B 311 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 C 311 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 C 311 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 C 311 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 C 311 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 C 311 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 C 311 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 C 311 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 C 311 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 C 311 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 C 311 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 C 311 GLY THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 12 C 311 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 13 C 311 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 14 C 311 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 15 C 311 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 16 C 311 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 17 C 311 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 18 C 311 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 19 C 311 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 20 C 311 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 21 C 311 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 22 C 311 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 23 C 311 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 24 C 311 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 D 311 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 D 311 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 D 311 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 D 311 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 D 311 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 D 311 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 D 311 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 D 311 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 D 311 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 D 311 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 D 311 GLY THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 12 D 311 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 13 D 311 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 14 D 311 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 15 D 311 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 16 D 311 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 17 D 311 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 18 D 311 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 19 D 311 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 20 D 311 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 21 D 311 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 22 D 311 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 23 D 311 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 24 D 311 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 E 311 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 E 311 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 E 311 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 E 311 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 E 311 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 E 311 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 E 311 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 E 311 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 E 311 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 E 311 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 E 311 GLY THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 12 E 311 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 13 E 311 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 14 E 311 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 15 E 311 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 16 E 311 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 17 E 311 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 18 E 311 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 19 E 311 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 20 E 311 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 21 E 311 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 22 E 311 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 23 E 311 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 24 E 311 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 F 311 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 F 311 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 F 311 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 F 311 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 F 311 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 F 311 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 F 311 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 F 311 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 F 311 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 F 311 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 F 311 GLY THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 12 F 311 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 13 F 311 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 14 F 311 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 15 F 311 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 16 F 311 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 17 F 311 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 18 F 311 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 19 F 311 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 20 F 311 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 21 F 311 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 22 F 311 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 23 F 311 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 24 F 311 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
FORMUL 7 HOH *85(H2 O)
HELIX 1 AA1 PRO A 7 LYS A 12 1 6
HELIX 2 AA2 ASP A 23 LYS A 37 1 15
HELIX 3 AA3 TYR A 64 GLY A 66 5 3
HELIX 4 AA4 PHE A 98 TRP A 102 5 5
HELIX 5 AA5 LEU A 103 MET A 108 1 6
HELIX 6 AA6 TYR A 157 SER A 173 1 17
HELIX 7 AA7 SER A 188 SER A 201 1 14
HELIX 8 AA8 HIS A 216 VAL A 224 1 9
HELIX 9 AA9 TYR A 229 HIS A 239 1 11
HELIX 10 AB1 LYS A 242 TYR A 252 1 11
HELIX 11 AB2 ASP A 254 ALA A 260 1 7
HELIX 12 AB3 PRO A 278 TYR A 289 1 12
HELIX 13 AB4 GLY A 306 PHE A 322 1 17
HELIX 14 AB5 PRO B 7 TYR B 14 1 8
HELIX 15 AB6 ASP B 23 LYS B 37 1 15
HELIX 16 AB7 TYR B 64 GLY B 66 5 3
HELIX 17 AB8 PHE B 98 TRP B 102 5 5
HELIX 18 AB9 LEU B 103 MET B 108 1 6
HELIX 19 AC1 TYR B 157 SER B 173 1 17
HELIX 20 AC2 SER B 188 SER B 201 1 14
HELIX 21 AC3 HIS B 216 VAL B 224 1 9
HELIX 22 AC4 TYR B 229 HIS B 239 1 11
HELIX 23 AC5 LYS B 242 TYR B 252 1 11
HELIX 24 AC6 ASP B 254 ALA B 260 1 7
HELIX 25 AC7 PRO B 278 TYR B 289 1 12
HELIX 26 AC8 GLY B 306 PHE B 322 1 17
HELIX 27 AC9 PRO C 7 LYS C 13 1 7
HELIX 28 AD1 ASP C 23 LYS C 37 1 15
HELIX 29 AD2 TYR C 64 GLY C 66 5 3
HELIX 30 AD3 PHE C 98 TRP C 102 5 5
HELIX 31 AD4 LEU C 103 MET C 108 1 6
HELIX 32 AD5 TYR C 157 SER C 173 1 17
HELIX 33 AD6 SER C 188 SER C 201 1 14
HELIX 34 AD7 HIS C 216 VAL C 224 1 9
HELIX 35 AD8 TYR C 229 HIS C 239 1 11
HELIX 36 AD9 LYS C 242 TYR C 252 1 11
HELIX 37 AE1 ASP C 254 ALA C 260 1 7
HELIX 38 AE2 PRO C 278 TYR C 289 1 12
HELIX 39 AE3 GLY C 306 PHE C 322 1 17
HELIX 40 AE4 PRO D 7 LYS D 13 1 7
HELIX 41 AE5 ASP D 23 LYS D 37 1 15
HELIX 42 AE6 TYR D 64 GLY D 66 5 3
HELIX 43 AE7 PHE D 98 TRP D 102 5 5
HELIX 44 AE8 LEU D 103 MET D 108 1 6
HELIX 45 AE9 TYR D 157 SER D 173 1 17
HELIX 46 AF1 SER D 188 SER D 201 1 14
HELIX 47 AF2 HIS D 216 VAL D 224 1 9
HELIX 48 AF3 TYR D 229 HIS D 239 1 11
HELIX 49 AF4 LYS D 242 TYR D 252 1 11
HELIX 50 AF5 ASP D 254 ALA D 260 1 7
HELIX 51 AF6 PRO D 278 TYR D 289 1 12
HELIX 52 AF7 GLY D 306 GLU D 323 1 18
HELIX 53 AF8 PRO E 7 LYS E 13 1 7
HELIX 54 AF9 ASP E 23 LYS E 37 1 15
HELIX 55 AG1 TYR E 64 GLY E 66 5 3
HELIX 56 AG2 PHE E 98 TRP E 102 5 5
HELIX 57 AG3 LEU E 103 MET E 108 1 6
HELIX 58 AG4 TYR E 157 SER E 173 1 17
HELIX 59 AG5 SER E 188 SER E 201 1 14
HELIX 60 AG6 HIS E 216 VAL E 224 1 9
HELIX 61 AG7 TYR E 229 HIS E 239 1 11
HELIX 62 AG8 LYS E 242 TYR E 252 1 11
HELIX 63 AG9 ASP E 254 ALA E 260 1 7
HELIX 64 AH1 PRO E 278 TYR E 289 1 12
HELIX 65 AH2 GLY E 306 PHE E 322 1 17
HELIX 66 AH3 PRO F 7 LYS F 13 1 7
HELIX 67 AH4 ASP F 23 LYS F 37 1 15
HELIX 68 AH5 TYR F 64 GLY F 66 5 3
HELIX 69 AH6 PHE F 98 TRP F 102 5 5
HELIX 70 AH7 LEU F 103 MET F 108 1 6
HELIX 71 AH8 TYR F 157 SER F 173 1 17
HELIX 72 AH9 SER F 188 SER F 201 1 14
HELIX 73 AI1 HIS F 216 VAL F 224 1 9
HELIX 74 AI2 TYR F 229 HIS F 239 1 11
HELIX 75 AI3 LYS F 242 TYR F 252 1 11
HELIX 76 AI4 ASP F 254 ALA F 260 1 7
HELIX 77 AI5 PRO F 278 TYR F 289 1 12
HELIX 78 AI6 GLY F 306 PHE F 322 1 17
SHEET 1 AA1 9 VAL A 43 ARG A 46 0
SHEET 2 AA1 9 VAL A 54 SER A 62 -1 O ASP A 58 N GLU A 45
SHEET 3 AA1 9 ARG A 68 PRO A 76 -1 O GLY A 71 N VAL A 59
SHEET 4 AA1 9 ILE A 111 MET A 115 -1 O CYS A 112 N LEU A 74
SHEET 5 AA1 9 LEU A 83 TYR A 89 1 N VAL A 86 O ILE A 111
SHEET 6 AA1 9 VAL A 177 GLY A 187 1 O VAL A 183 N CYS A 85
SHEET 7 AA1 9 ALA A 206 ASP A 210 1 O ALA A 206 N ILE A 184
SHEET 8 AA1 9 ALA A 266 GLY A 271 1 O LEU A 267 N LEU A 207
SHEET 9 AA1 9 LYS A 293 TYR A 298 1 O TYR A 298 N VAL A 270
SHEET 1 AA2 9 VAL B 43 ARG B 46 0
SHEET 2 AA2 9 VAL B 54 SER B 62 -1 O ASP B 58 N GLU B 45
SHEET 3 AA2 9 ARG B 68 PRO B 76 -1 O LEU B 73 N TYR B 57
SHEET 4 AA2 9 ILE B 111 ASP B 116 -1 O CYS B 112 N LEU B 74
SHEET 5 AA2 9 LEU B 83 ILE B 90 1 N VAL B 86 O ILE B 111
SHEET 6 AA2 9 VAL B 177 GLY B 187 1 O VAL B 183 N CYS B 85
SHEET 7 AA2 9 ALA B 206 ASP B 210 1 O ALA B 206 N ILE B 184
SHEET 8 AA2 9 ALA B 266 GLY B 271 1 O LEU B 267 N LEU B 207
SHEET 9 AA2 9 LYS B 293 TYR B 298 1 O TYR B 298 N VAL B 270
SHEET 1 AA3 9 VAL C 43 ARG C 46 0
SHEET 2 AA3 9 VAL C 54 SER C 62 -1 O ASP C 58 N GLU C 45
SHEET 3 AA3 9 ARG C 68 PRO C 76 -1 O GLY C 71 N VAL C 59
SHEET 4 AA3 9 ILE C 111 MET C 115 -1 O CYS C 112 N LEU C 74
SHEET 5 AA3 9 LEU C 83 TYR C 89 1 N VAL C 86 O ILE C 111
SHEET 6 AA3 9 VAL C 177 GLY C 187 1 O VAL C 183 N CYS C 85
SHEET 7 AA3 9 ALA C 206 ASP C 210 1 O ALA C 206 N ILE C 184
SHEET 8 AA3 9 ALA C 266 GLY C 271 1 O LEU C 267 N LEU C 207
SHEET 9 AA3 9 LYS C 293 TYR C 298 1 O GLU C 294 N PHE C 268
SHEET 1 AA4 9 VAL D 43 ARG D 46 0
SHEET 2 AA4 9 VAL D 54 SER D 62 -1 O ASP D 58 N GLU D 45
SHEET 3 AA4 9 ARG D 68 PRO D 76 -1 O GLY D 71 N VAL D 59
SHEET 4 AA4 9 ILE D 111 MET D 115 -1 O VAL D 114 N TRP D 72
SHEET 5 AA4 9 LEU D 83 TYR D 89 1 N VAL D 86 O ILE D 111
SHEET 6 AA4 9 VAL D 177 GLY D 187 1 O VAL D 183 N CYS D 85
SHEET 7 AA4 9 ALA D 206 ASP D 210 1 O ALA D 206 N ILE D 184
SHEET 8 AA4 9 ALA D 266 GLY D 271 1 O LEU D 267 N LEU D 207
SHEET 9 AA4 9 LYS D 293 TYR D 298 1 O GLU D 294 N PHE D 268
SHEET 1 AA5 9 VAL E 43 ARG E 46 0
SHEET 2 AA5 9 VAL E 54 SER E 62 -1 O ASP E 58 N GLU E 45
SHEET 3 AA5 9 ARG E 68 PRO E 76 -1 O GLY E 71 N VAL E 59
SHEET 4 AA5 9 ILE E 111 MET E 115 -1 O CYS E 112 N LEU E 74
SHEET 5 AA5 9 LEU E 83 TYR E 89 1 N VAL E 86 O ILE E 111
SHEET 6 AA5 9 VAL E 177 GLY E 187 1 O VAL E 183 N CYS E 85
SHEET 7 AA5 9 ALA E 206 ASP E 210 1 O ALA E 206 N ILE E 184
SHEET 8 AA5 9 ALA E 266 GLY E 271 1 O LEU E 267 N LEU E 207
SHEET 9 AA5 9 LYS E 293 TYR E 298 1 O GLU E 294 N PHE E 268
SHEET 1 AA6 9 VAL F 43 ARG F 46 0
SHEET 2 AA6 9 VAL F 54 SER F 62 -1 O ASP F 58 N GLU F 45
SHEET 3 AA6 9 ARG F 68 PRO F 76 -1 O GLY F 71 N VAL F 59
SHEET 4 AA6 9 ILE F 111 MET F 115 -1 O CYS F 112 N LEU F 74
SHEET 5 AA6 9 LEU F 83 TYR F 89 1 N VAL F 86 O ILE F 111
SHEET 6 AA6 9 VAL F 177 GLY F 187 1 O VAL F 183 N CYS F 85
SHEET 7 AA6 9 ALA F 206 ASP F 210 1 O ALA F 206 N ILE F 184
SHEET 8 AA6 9 ALA F 266 GLY F 271 1 O LEU F 267 N LEU F 207
SHEET 9 AA6 9 LYS F 293 TYR F 298 1 O GLU F 294 N PHE F 268
CISPEP 1 HIS A 227 PRO A 228 0 8.02
CISPEP 2 HIS B 227 PRO B 228 0 1.80
CISPEP 3 HIS B 227 PRO B 228 0 3.73
CISPEP 4 HIS C 227 PRO C 228 0 6.25
CISPEP 5 HIS C 227 PRO C 228 0 8.55
CISPEP 6 HIS D 227 PRO D 228 0 5.17
CISPEP 7 HIS D 227 PRO D 228 0 6.55
CISPEP 8 HIS E 227 PRO E 228 0 4.05
CISPEP 9 HIS E 227 PRO E 228 0 6.33
CISPEP 10 HIS F 227 PRO F 228 0 2.78
CISPEP 11 HIS F 227 PRO F 228 0 5.42
CRYST1 155.080 155.080 165.100 90.00 90.00 120.00 P 31 2 1 36
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006448 0.003723 0.000000 0.00000
SCALE2 0.000000 0.007446 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006057 0.00000
TER 2188 GLU A 323
TER 4385 GLU B 323
TER 6581 GLU C 323
TER 8783 GLU D 323
TER 11006 GLU E 323
TER 13247 GLU F 323
MASTER 914 0 0 78 54 0 0 613291 6 0 144
END
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