| 6cqw-pdb | HEADER HYDROLASE 16-MAR-18 6CQW
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH VX(-) AND HI-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BESTER,M.A.GUELTA,S.D.PEGAN,J.J.HEIGHT
REVDAT 1 05-DEC-18 6CQW 0
JRNL AUTH S.M.BESTER,M.A.GUELTA,J.CHEUNG,M.D.WINEMILLER,S.Y.BAE,
JRNL AUTH 2 J.MYSLINSKI,S.D.PEGAN,J.J.HEIGHT
JRNL TITL STRUCTURAL INSIGHTS OF STEREOSPECIFIC INHIBITION OF HUMAN
JRNL TITL 2 ACETYLCHOLINESTERASE BY VX AND SUBSEQUENT REACTIVATION BY
JRNL TITL 3 HI-6.
JRNL REF CHEM. RES. TOXICOL. 2018
JRNL REFN ISSN 1520-5010
JRNL PMID 30462502
JRNL DOI 10.1021/ACS.CHEMRESTOX.8B00294
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 95442
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4748
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.6799 - 7.0643 0.99 3291 173 0.1737 0.1859
REMARK 3 2 7.0643 - 5.6122 1.00 3182 156 0.1771 0.2053
REMARK 3 3 5.6122 - 4.9042 1.00 3120 146 0.1512 0.1664
REMARK 3 4 4.9042 - 4.4565 0.99 3097 145 0.1254 0.1541
REMARK 3 5 4.4565 - 4.1374 1.00 3070 163 0.1331 0.1520
REMARK 3 6 4.1374 - 3.8937 1.00 3017 179 0.1363 0.1555
REMARK 3 7 3.8937 - 3.6989 1.00 3061 172 0.1460 0.1676
REMARK 3 8 3.6989 - 3.5380 1.00 3055 140 0.1673 0.1912
REMARK 3 9 3.5380 - 3.4018 1.00 3023 189 0.1708 0.1949
REMARK 3 10 3.4018 - 3.2845 1.00 3016 162 0.1750 0.2015
REMARK 3 11 3.2845 - 3.1819 1.00 3013 159 0.1827 0.2074
REMARK 3 12 3.1819 - 3.0909 1.00 3043 166 0.1835 0.2312
REMARK 3 13 3.0909 - 3.0096 1.00 2993 183 0.1815 0.2057
REMARK 3 14 3.0096 - 2.9362 1.00 3029 153 0.1860 0.2505
REMARK 3 15 2.9362 - 2.8695 1.00 2981 205 0.1970 0.2308
REMARK 3 16 2.8695 - 2.8084 1.00 3003 179 0.2024 0.2239
REMARK 3 17 2.8084 - 2.7522 1.00 2997 142 0.1971 0.2548
REMARK 3 18 2.7522 - 2.7003 1.00 3034 153 0.1998 0.2550
REMARK 3 19 2.7003 - 2.6521 1.00 3025 163 0.1951 0.2319
REMARK 3 20 2.6521 - 2.6072 1.00 3013 148 0.2028 0.2427
REMARK 3 21 2.6072 - 2.5651 1.00 2980 152 0.1995 0.2405
REMARK 3 22 2.5651 - 2.5257 1.00 3014 158 0.2057 0.2412
REMARK 3 23 2.5257 - 2.4885 1.00 3032 141 0.2035 0.2409
REMARK 3 24 2.4885 - 2.4535 1.00 3020 139 0.2106 0.2274
REMARK 3 25 2.4535 - 2.4203 1.00 2975 181 0.2137 0.2641
REMARK 3 26 2.4203 - 2.3889 1.00 2980 146 0.2244 0.2611
REMARK 3 27 2.3889 - 2.3590 1.00 3045 142 0.2320 0.3068
REMARK 3 28 2.3590 - 2.3306 1.00 2945 154 0.2410 0.2708
REMARK 3 29 2.3306 - 2.3035 0.97 2991 130 0.2496 0.2877
REMARK 3 30 2.3035 - 2.2776 0.89 2649 129 0.2775 0.3747
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 8839
REMARK 3 ANGLE : 0.721 12108
REMARK 3 CHIRALITY : 0.046 1302
REMARK 3 PLANARITY : 0.006 1592
REMARK 3 DIHEDRAL : 14.381 5177
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:32)
REMARK 3 ORIGIN FOR THE GROUP (A): 71.9801 40.4330 45.5772
REMARK 3 T TENSOR
REMARK 3 T11: 0.6348 T22: 0.5669
REMARK 3 T33: 0.4408 T12: -0.0925
REMARK 3 T13: -0.1278 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 4.6656 L22: 4.4463
REMARK 3 L33: 7.0157 L12: -1.3039
REMARK 3 L13: -3.8883 L23: 2.4520
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -0.5229 S13: 0.3504
REMARK 3 S21: 0.5124 S22: 0.0943 S23: -0.5908
REMARK 3 S31: -0.4982 S32: 0.7845 S33: -0.1042
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 33:490)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1776 29.0222 26.0515
REMARK 3 T TENSOR
REMARK 3 T11: 0.3093 T22: 0.3357
REMARK 3 T33: 0.3043 T12: 0.0235
REMARK 3 T13: -0.0323 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.3319 L22: 1.0002
REMARK 3 L33: 2.7973 L12: 0.1108
REMARK 3 L13: 0.7997 L23: 0.2653
REMARK 3 S TENSOR
REMARK 3 S11: -0.0555 S12: -0.1017 S13: -0.0648
REMARK 3 S21: 0.0018 S22: 0.0313 S23: 0.0070
REMARK 3 S31: -0.2281 S32: -0.1195 S33: 0.0201
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 491:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2456 36.7949 6.3767
REMARK 3 T TENSOR
REMARK 3 T11: 0.5802 T22: 0.4293
REMARK 3 T33: 0.2923 T12: -0.0475
REMARK 3 T13: -0.0643 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 3.8590 L22: 2.4300
REMARK 3 L33: 2.8775 L12: -0.6181
REMARK 3 L13: -0.1607 L23: 0.1293
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: 0.3325 S13: 0.2893
REMARK 3 S21: -0.0600 S22: -0.0621 S23: -0.0302
REMARK 3 S31: -0.6580 S32: 0.1317 S33: 0.1121
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 4:257)
REMARK 3 ORIGIN FOR THE GROUP (A): 108.0105 32.8187 40.0778
REMARK 3 T TENSOR
REMARK 3 T11: 0.2860 T22: 0.3490
REMARK 3 T33: 0.3240 T12: -0.1090
REMARK 3 T13: -0.0083 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.3462 L22: 1.3520
REMARK 3 L33: 2.2052 L12: -0.3658
REMARK 3 L13: -0.1019 L23: -0.2156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0794 S12: -0.1170 S13: -0.0605
REMARK 3 S21: 0.1976 S22: -0.0839 S23: -0.0214
REMARK 3 S31: 0.0357 S32: 0.2195 S33: -0.0018
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 258:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 107.7185 45.9915 23.0955
REMARK 3 T TENSOR
REMARK 3 T11: 0.3325 T22: 0.4087
REMARK 3 T33: 0.3360 T12: -0.0815
REMARK 3 T13: -0.0111 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 0.8841 L22: 0.9465
REMARK 3 L33: 2.1161 L12: 0.0177
REMARK 3 L13: -0.0053 L23: -0.2645
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: 0.1629 S13: 0.0524
REMARK 3 S21: -0.0459 S22: -0.1089 S23: -0.0806
REMARK 3 S31: -0.2420 S32: 0.2112 S33: 0.0666
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6CQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233252.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.278
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : 0.04600
REMARK 200 FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.42700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 TO 21% PEG 3350, 0.17 - 0.2M
REMARK 280 POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K, TEMPERATURE 295.0K
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 108.20367
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 216.40733
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 216.40733
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 108.20367
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 52.51500
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -90.95865
REMARK 350 BIOMT3 2 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 GLY A 2
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 THR B 543
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY B 135 O HOH B 701 2.02
REMARK 500 O ASN A 482 O ASP A 488 2.03
REMARK 500 OE1 GLU A 285 O HOH A 701 2.06
REMARK 500 CD PRO A 492 O HOH A 703 2.07
REMARK 500 O HOH B 851 O HOH B 988 2.08
REMARK 500 O4 NAG A 604 O HOH A 702 2.11
REMARK 500 O HOH A 891 O HOH A 990 2.11
REMARK 500 O HOH B 722 O HOH B 953 2.11
REMARK 500 O HOH B 949 O HOH B 953 2.12
REMARK 500 N VAL B 139 O HOH B 701 2.13
REMARK 500 OE1 GLU B 81 O HOH B 702 2.14
REMARK 500 O HOH B 1006 O HOH B 1038 2.15
REMARK 500 O HOH B 775 O HOH B 988 2.16
REMARK 500 O HOH B 762 O HOH B 1027 2.16
REMARK 500 N PRO A 492 O HOH A 703 2.19
REMARK 500 CA SER A 110 O HOH A 705 2.19
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 GLU A 468 CA - C - O ANGL. DEV. = 13.4 DEGREES
REMARK 500 GLU A 468 CA - C - O ANGL. DEV. = 16.7 DEGREES
REMARK 500 GLU A 468 CA - C - N ANGL. DEV. = -15.2 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 PHE A 47 -8.57 74.23
REMARK 500 ASN A 170 19.62 58.94
REMARK 500 SER A 203 -121.29 56.56
REMARK 500 ASP A 306 -78.22 -94.20
REMARK 500 VAL A 407 -63.87 -122.87
REMARK 500 ASN A 464 52.03 -95.10
REMARK 500 PHE B 47 -6.83 73.80
REMARK 500 ALA B 62 50.40 -113.03
REMARK 500 SER B 203 -122.53 57.41
REMARK 500 ASP B 306 -80.89 -99.24
REMARK 500 VAL B 407 -60.97 -127.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 601 through NAG A 603 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800 to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800 601 through NAG B 603 bound to ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VX B 605 and SER B
REMARK 800 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6CQX RELATED DB: PDB
REMARK 900 RELATED ID: 6CQY RELATED DB: PDB
REMARK 900 RELATED ID: 6CQZ RELATED DB: PDB
REMARK 900 RELATED ID: 6CQT RELATED DB: PDB
REMARK 900 RELATED ID: 6CQU RELATED DB: PDB
REMARK 900 RELATED ID: 6CQV RELATED DB: PDB
DBREF 6CQW A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6CQW B 2 543 UNP P22303 ACES_HUMAN 33 574
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 B 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 B 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 B 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 B 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 B 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 B 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 B 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 B 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 B 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 B 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 B 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 B 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 B 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 B 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 B 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 B 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 B 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 B 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 B 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 B 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 B 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 B 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 B 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 B 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 B 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 B 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 B 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 B 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 B 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 B 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 B 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 B 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 B 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 B 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 B 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 B 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 B 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 B 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 B 542 PHE LEU PRO LYS LEU LEU SER ALA THR
HET FUC A 601 10
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET VX A 606 6
HET HI6 A 607 21
HET FUC B 601 10
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET VX B 605 6
HET HI6 B 606 21
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM
HETSYN HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-
HETSYN 2 HI6 PYRIDINIUM DIMETHYLETHER
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 6 VX 2(C3 H9 O3 P)
FORMUL 7 HI6 2(C14 H16 N4 O3 2+)
FORMUL 12 HOH *665(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 SER A 215 1 13
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 MET A 241 VAL A 255 1 15
HELIX 12 AB3 ASN A 265 THR A 275 1 11
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 ARG A 485 1 20
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 ALA A 542 1 9
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 GLY B 240 VAL B 255 1 16
HELIX 38 AE2 ASN B 265 THR B 275 1 11
HELIX 39 AE3 PRO B 277 GLU B 285 1 9
HELIX 40 AE4 TRP B 286 LEU B 289 5 4
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 TYR B 382 1 12
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 PHE B 535 SER B 541 1 7
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 THR A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 2 VAL A 239 GLY A 240 0
SHEET 2 AA4 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA5 3 LEU B 9 VAL B 12 0
SHEET 2 AA5 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA5 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA611 ILE B 20 LEU B 22 0
SHEET 2 AA611 VAL B 29 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA611 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA611 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA611 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA611 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA611 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 AA611 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA611 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA611 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA611 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA7 2 VAL B 68 CYS B 69 0
SHEET 2 AA7 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
LINK OG SER A 203 P1 VX A 606 1555 1555 1.40
LINK ND2 ASN A 265 C1 NAG A 604 1555 1555 1.44
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.37
LINK ND2 ASN A 464 C1 NAG A 605 1555 1555 1.44
LINK OG SER B 203 P1 VX B 605 1555 1555 1.40
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.57
LINK ND2 ASN B 464 C1 NAG B 604 1555 1555 1.45
LINK C1 FUC A 601 O6 NAG A 602 1555 1555 1.44
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.44
LINK C1 FUC B 601 O6 NAG B 602 1555 1555 1.43
LINK O4 NAG B 602 C1 NAG B 603 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 3.65
CISPEP 2 CYS A 257 PRO A 258 0 -5.79
CISPEP 3 TYR B 105 PRO B 106 0 -1.53
CISPEP 4 PRO B 258 PRO B 259 0 12.00
CISPEP 5 ALA B 497 PRO B 498 0 -1.97
SITE 1 AC1 9 GLY A 121 GLY A 122 SER A 203 ALA A 204
SITE 2 AC1 9 PHE A 295 PHE A 297 PHE A 338 HIS A 447
SITE 3 AC1 9 HOH A 825
SITE 1 AC2 14 TYR A 72 ASP A 74 TYR A 124 VAL A 282
SITE 2 AC2 14 GLU A 285 TRP A 286 VAL A 294 PHE A 295
SITE 3 AC2 14 TYR A 337 TYR A 341 HOH A 717 HOH A 749
SITE 4 AC2 14 HOH A 781 HOH A 790
SITE 1 AC3 12 TYR B 72 ASP B 74 TYR B 124 VAL B 282
SITE 2 AC3 12 GLU B 285 TRP B 286 VAL B 294 PHE B 295
SITE 3 AC3 12 TYR B 337 PHE B 338 TYR B 341 HOH B 850
SITE 1 AC4 5 ASN A 265 THR A 267 GLU A 268 HOH A 702
SITE 2 AC4 5 HOH A 885
SITE 1 AC5 7 ALA A 343 PRO A 344 GLY A 345 PHE A 346
SITE 2 AC5 7 SER A 347 ASN A 350 HOH A 836
SITE 1 AC6 2 SER A 462 ASN A 464
SITE 1 AC7 3 PRO B 344 GLY B 345 ASN B 350
SITE 1 AC8 3 ASN B 464 HOH B 731 HOH B 849
SITE 1 AC9 13 GLY B 121 GLY B 122 GLU B 202 ALA B 204
SITE 2 AC9 13 GLY B 205 ALA B 206 ALA B 207 GLN B 228
SITE 3 AC9 13 SER B 229 PHE B 295 PHE B 297 PHE B 338
SITE 4 AC9 13 HIS B 447
CRYST1 105.030 105.030 324.611 90.00 90.00 120.00 P 31 2 1 12
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 0.009521 0.005497 0.000000 0.00000
SCALE2 0.000000 0.010994 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003081 0.00000
TER 4201 ALA A 542
TER 8366 ALA B 542
MASTER 461 0 13 52 34 0 21 6 9106 2 191 84
END
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