| 6igp-pdb | HEADER HYDROLASE 25-SEP-18 6IGP
TITLE CRYSTAL STRUCTURE OF S9 PEPTIDASE (INACTIVE STATE)FROM DEINOCOCCUS
TITLE 2 RADIODURANS R1 IN P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PEPTIDE HYDROLASE, PUTATIVE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS STR. R1;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1;
SOURCE 5 GENE: DR_0165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PST50TR
KEYWDS SERINE PEPTIDASE, MEROPS S9, POP FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.YADAV,V.D.GOYAL,A.KUMAR,R.D.MAKDE
REVDAT 1 14-NOV-18 6IGP 0
JRNL AUTH P.YADAV,V.D.GOYAL,N.K.GAUR,A.KUMAR,S.M.GOKHALE,S.N.JAMDAR,
JRNL AUTH 2 R.D.MAKDE
JRNL TITL CRYSTAL STRUCTURE OF INACTIVE STATE OF S9 PEPTIDASE FROM
JRNL TITL 2 DEINOCOCCUS RADIODURANS R1 IN TRIS-CL CONDITION
JRNL TITL 3 (CONDITION-2)
JRNL REF J.BIOL.CHEM. 2018
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 119705
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5987
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 48.7533 - 7.4488 0.98 3979 214 0.1891 0.2078
REMARK 3 2 7.4488 - 5.9156 1.00 3922 187 0.1928 0.1989
REMARK 3 3 5.9156 - 5.1688 1.00 3857 211 0.1625 0.1811
REMARK 3 4 5.1688 - 4.6966 1.00 3825 225 0.1423 0.1756
REMARK 3 5 4.6966 - 4.3602 1.00 3793 236 0.1420 0.1634
REMARK 3 6 4.3602 - 4.1033 1.00 3798 226 0.1489 0.1975
REMARK 3 7 4.1033 - 3.8979 1.00 3789 218 0.1620 0.1957
REMARK 3 8 3.8979 - 3.7283 1.00 3778 218 0.1682 0.2064
REMARK 3 9 3.7283 - 3.5848 1.00 3800 215 0.1736 0.1766
REMARK 3 10 3.5848 - 3.4611 1.00 3767 206 0.1897 0.2337
REMARK 3 11 3.4611 - 3.3529 1.00 3812 170 0.1944 0.1950
REMARK 3 12 3.3529 - 3.2571 1.00 3769 214 0.1926 0.2224
REMARK 3 13 3.2571 - 3.1714 1.00 3781 193 0.1892 0.2113
REMARK 3 14 3.1714 - 3.0940 1.00 3785 203 0.1900 0.2298
REMARK 3 15 3.0940 - 3.0237 1.00 3784 190 0.1894 0.2354
REMARK 3 16 3.0237 - 2.9594 1.00 3785 185 0.1989 0.2494
REMARK 3 17 2.9594 - 2.9002 1.00 3752 201 0.2030 0.2763
REMARK 3 18 2.9002 - 2.8454 1.00 3806 191 0.2160 0.2588
REMARK 3 19 2.8454 - 2.7946 1.00 3780 168 0.2187 0.2463
REMARK 3 20 2.7946 - 2.7473 1.00 3786 190 0.2160 0.2547
REMARK 3 21 2.7473 - 2.7030 1.00 3760 193 0.2084 0.2672
REMARK 3 22 2.7030 - 2.6614 1.00 3748 170 0.2125 0.2639
REMARK 3 23 2.6614 - 2.6222 1.00 3801 198 0.2114 0.2677
REMARK 3 24 2.6222 - 2.5853 1.00 3767 193 0.2093 0.2559
REMARK 3 25 2.5853 - 2.5504 1.00 3701 205 0.2152 0.2759
REMARK 3 26 2.5504 - 2.5172 1.00 3772 200 0.2102 0.2650
REMARK 3 27 2.5172 - 2.4858 1.00 3752 208 0.2153 0.2735
REMARK 3 28 2.4858 - 2.4558 1.00 3762 177 0.2115 0.2374
REMARK 3 29 2.4558 - 2.4273 1.00 3767 186 0.2182 0.2544
REMARK 3 30 2.4273 - 2.4000 1.00 3740 196 0.2236 0.2475
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) : 24.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
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 : 0.006 18487
REMARK 3 ANGLE : 0.877 25230
REMARK 3 CHIRALITY : 0.056 2664
REMARK 3 PLANARITY : 0.006 3332
REMARK 3 DIHEDRAL : 3.698 10580
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 9:655)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4065 -24.8558 -8.9453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.1410
REMARK 3 T33: 0.1187 T12: 0.0118
REMARK 3 T13: 0.0086 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.3619 L22: 0.6445
REMARK 3 L33: 0.3888 L12: -0.0503
REMARK 3 L13: 0.1533 L23: -0.1196
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: 0.0506 S13: -0.0977
REMARK 3 S21: -0.0686 S22: 0.0101 S23: 0.0121
REMARK 3 S31: -0.0298 S32: -0.0381 S33: -0.0182
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 7:655)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5763 -25.8130 -88.4090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1887 T22: 0.1754
REMARK 3 T33: 0.1468 T12: 0.0097
REMARK 3 T13: -0.0050 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 1.2601 L22: 0.5447
REMARK 3 L33: 0.3065 L12: 0.1502
REMARK 3 L13: -0.1214 L23: -0.0173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0204 S12: -0.1918 S13: -0.1228
REMARK 3 S21: 0.1294 S22: -0.0022 S23: 0.0395
REMARK 3 S31: -0.0128 S32: 0.0210 S33: 0.0153
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESSEQ 7:655)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2117 -18.7866 -67.0637
REMARK 3 T TENSOR
REMARK 3 T11: 0.2186 T22: 0.1564
REMARK 3 T33: 0.2636 T12: -0.0141
REMARK 3 T13: 0.0113 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.7675 L22: 0.4103
REMARK 3 L33: 1.3223 L12: 0.1071
REMARK 3 L13: 0.0695 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0211 S12: -0.1426 S13: -0.0353
REMARK 3 S21: 0.1430 S22: -0.0543 S23: 0.0670
REMARK 3 S31: 0.1226 S32: -0.0710 S33: 0.0820
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESSEQ 7:655)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5417 -18.8175 -29.9233
REMARK 3 T TENSOR
REMARK 3 T11: 0.2595 T22: 0.3747
REMARK 3 T33: 0.1969 T12: 0.0765
REMARK 3 T13: 0.0320 T23: 0.1042
REMARK 3 L TENSOR
REMARK 3 L11: 0.9992 L22: 0.6449
REMARK 3 L33: 1.1245 L12: -0.2982
REMARK 3 L13: -0.0719 L23: -0.0228
REMARK 3 S TENSOR
REMARK 3 S11: 0.1495 S12: 0.4381 S13: 0.1474
REMARK 3 S21: -0.2369 S22: -0.1611 S23: -0.1128
REMARK 3 S31: 0.1104 S32: 0.0394 S33: 0.0182
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 6IGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0-5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : RRCAT INDUS-2
REMARK 200 BEAMLINE : PX-BL21
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97947
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119902
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.15600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 0.86500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
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: 5YZM
REMARK 200
REMARK 200 REMARK: PLATE LIKE CRYSTALS (~100 MICRONS)
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-CL PH 8.5, 200MM AMMONIUM
REMARK 280 -CITRATE, 10MM CALCIUM CHLORIDE, 14 % PEG 3350, PH 5.31,
REMARK 280 MICROBATCH, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 59.92850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.48650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.24600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.48650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.92850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.24600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 THR A 6
REMARK 465 PRO A 7
REMARK 465 ALA A 8
REMARK 465 SER A 40
REMARK 465 GLU A 41
REMARK 465 GLU A 42
REMARK 465 ASP A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 LYS A 46
REMARK 465 PRO A 47
REMARK 465 ASP A 48
REMARK 465 LYS A 49
REMARK 465 ASP A 50
REMARK 465 PHE A 51
REMARK 465 ALA A 52
REMARK 465 ARG A 53
REMARK 465 GLY A 99
REMARK 465 GLU A 100
REMARK 465 ALA A 143
REMARK 465 ASP A 144
REMARK 465 THR A 145
REMARK 465 GLU A 146
REMARK 465 ASP A 147
REMARK 465 LYS A 148
REMARK 465 ARG A 149
REMARK 465 ASP A 150
REMARK 465 GLU A 151
REMARK 465 ARG A 152
REMARK 465 GLY A 153
REMARK 465 GLU A 154
REMARK 465 ALA A 155
REMARK 465 ARG A 156
REMARK 465 VAL A 157
REMARK 465 LEU A 158
REMARK 465 THR A 159
REMARK 465 ARG A 160
REMARK 465 PRO A 161
REMARK 465 VAL A 162
REMARK 465 TYR A 163
REMARK 465 ARG A 164
REMARK 465 ALA A 165
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 ALA A 168
REMARK 465 ASP A 169
REMARK 465 TRP A 170
REMARK 465 LEU A 171
REMARK 465 PRO A 172
REMARK 465 GLU A 173
REMARK 465 ARG A 174
REMARK 465 ALA A 236
REMARK 465 ASP A 237
REMARK 465 ALA A 238
REMARK 465 PRO A 239
REMARK 465 ALA A 240
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 THR B 6
REMARK 465 SER B 40
REMARK 465 GLU B 41
REMARK 465 GLU B 42
REMARK 465 ASP B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 LYS B 46
REMARK 465 PRO B 47
REMARK 465 ASP B 48
REMARK 465 LYS B 49
REMARK 465 ASP B 50
REMARK 465 PHE B 51
REMARK 465 ALA B 52
REMARK 465 ARG B 53
REMARK 465 GLY B 99
REMARK 465 GLU B 100
REMARK 465 VAL B 101
REMARK 465 ALA B 143
REMARK 465 ASP B 144
REMARK 465 THR B 145
REMARK 465 GLU B 146
REMARK 465 ASP B 147
REMARK 465 LYS B 148
REMARK 465 ARG B 149
REMARK 465 ASP B 150
REMARK 465 GLU B 151
REMARK 465 ARG B 152
REMARK 465 GLY B 153
REMARK 465 GLU B 154
REMARK 465 ALA B 155
REMARK 465 ARG B 156
REMARK 465 VAL B 157
REMARK 465 LEU B 158
REMARK 465 THR B 159
REMARK 465 ARG B 160
REMARK 465 PRO B 161
REMARK 465 VAL B 162
REMARK 465 TYR B 163
REMARK 465 ARG B 164
REMARK 465 ALA B 165
REMARK 465 ASN B 166
REMARK 465 GLY B 167
REMARK 465 ALA B 168
REMARK 465 ASP B 169
REMARK 465 TRP B 170
REMARK 465 LEU B 171
REMARK 465 PRO B 172
REMARK 465 GLU B 173
REMARK 465 ARG B 174
REMARK 465 GLU B 216
REMARK 465 ASP B 217
REMARK 465 GLU B 218
REMARK 465 TRP B 219
REMARK 465 GLN B 220
REMARK 465 ALA B 221
REMARK 465 SER B 222
REMARK 465 GLN B 223
REMARK 465 ALA B 236
REMARK 465 ASP B 237
REMARK 465 ALA B 238
REMARK 465 PRO B 239
REMARK 465 ALA B 240
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 ASN C 3
REMARK 465 SER C 4
REMARK 465 GLU C 5
REMARK 465 THR C 6
REMARK 465 SER C 40
REMARK 465 GLU C 41
REMARK 465 GLU C 42
REMARK 465 ASP C 43
REMARK 465 PRO C 44
REMARK 465 ALA C 45
REMARK 465 LYS C 46
REMARK 465 PRO C 47
REMARK 465 ASP C 48
REMARK 465 LYS C 49
REMARK 465 ASP C 50
REMARK 465 PHE C 51
REMARK 465 ALA C 52
REMARK 465 ALA C 98
REMARK 465 GLY C 99
REMARK 465 GLU C 100
REMARK 465 VAL C 101
REMARK 465 LYS C 102
REMARK 465 HIS C 120
REMARK 465 PHE C 121
REMARK 465 LYS C 122
REMARK 465 THR C 142
REMARK 465 ALA C 143
REMARK 465 ASP C 144
REMARK 465 THR C 145
REMARK 465 GLU C 146
REMARK 465 ASP C 147
REMARK 465 LYS C 148
REMARK 465 ARG C 149
REMARK 465 ASP C 150
REMARK 465 GLU C 151
REMARK 465 ARG C 152
REMARK 465 GLY C 153
REMARK 465 GLU C 154
REMARK 465 ALA C 155
REMARK 465 ARG C 156
REMARK 465 VAL C 157
REMARK 465 LEU C 158
REMARK 465 THR C 159
REMARK 465 ARG C 160
REMARK 465 PRO C 161
REMARK 465 VAL C 162
REMARK 465 TYR C 163
REMARK 465 ARG C 164
REMARK 465 ALA C 165
REMARK 465 ASN C 166
REMARK 465 GLY C 167
REMARK 465 ALA C 168
REMARK 465 ASP C 169
REMARK 465 TRP C 170
REMARK 465 LEU C 171
REMARK 465 PRO C 172
REMARK 465 GLU C 173
REMARK 465 ARG C 174
REMARK 465 PRO C 175
REMARK 465 GLU C 216
REMARK 465 ASP C 217
REMARK 465 GLU C 218
REMARK 465 TRP C 219
REMARK 465 GLN C 220
REMARK 465 ALA C 221
REMARK 465 SER C 222
REMARK 465 ALA C 236
REMARK 465 ASP C 237
REMARK 465 ALA C 238
REMARK 465 PRO C 239
REMARK 465 ALA C 240
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 ASN D 2
REMARK 465 ASN D 3
REMARK 465 SER D 4
REMARK 465 GLU D 5
REMARK 465 THR D 6
REMARK 465 SER D 40
REMARK 465 GLU D 41
REMARK 465 GLU D 42
REMARK 465 ASP D 43
REMARK 465 PRO D 44
REMARK 465 ALA D 45
REMARK 465 LYS D 46
REMARK 465 PRO D 47
REMARK 465 ASP D 48
REMARK 465 LYS D 49
REMARK 465 ASP D 50
REMARK 465 PHE D 51
REMARK 465 ALA D 52
REMARK 465 ARG D 53
REMARK 465 ALA D 98
REMARK 465 GLY D 99
REMARK 465 GLU D 100
REMARK 465 VAL D 101
REMARK 465 LYS D 102
REMARK 465 LYS D 122
REMARK 465 ASN D 123
REMARK 465 GLY D 124
REMARK 465 VAL D 125
REMARK 465 THR D 142
REMARK 465 ALA D 143
REMARK 465 ASP D 144
REMARK 465 THR D 145
REMARK 465 GLU D 146
REMARK 465 ASP D 147
REMARK 465 LYS D 148
REMARK 465 ARG D 149
REMARK 465 ASP D 150
REMARK 465 GLU D 151
REMARK 465 ARG D 152
REMARK 465 GLY D 153
REMARK 465 GLU D 154
REMARK 465 ALA D 155
REMARK 465 ARG D 156
REMARK 465 VAL D 157
REMARK 465 LEU D 158
REMARK 465 THR D 159
REMARK 465 ARG D 160
REMARK 465 PRO D 161
REMARK 465 VAL D 162
REMARK 465 TYR D 163
REMARK 465 ARG D 164
REMARK 465 ALA D 165
REMARK 465 ASN D 166
REMARK 465 GLY D 167
REMARK 465 ALA D 168
REMARK 465 ASP D 169
REMARK 465 TRP D 170
REMARK 465 LEU D 171
REMARK 465 PRO D 172
REMARK 465 GLU D 173
REMARK 465 ARG D 174
REMARK 465 PRO D 175
REMARK 465 GLU D 216
REMARK 465 ASP D 217
REMARK 465 GLU D 218
REMARK 465 TRP D 219
REMARK 465 GLN D 220
REMARK 465 ALA D 221
REMARK 465 SER D 222
REMARK 465 ALA D 236
REMARK 465 ASP D 237
REMARK 465 ALA D 238
REMARK 465 PRO D 239
REMARK 465 ALA D 240
REMARK 465 ALA D 241
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 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 LYS A 187 CD CE NZ
REMARK 470 TRP A 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 224 CZ3 CH2
REMARK 470 LYS A 273 CG CD CE NZ
REMARK 470 GLU A 421 CG CD OE1 OE2
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 ARG A 566 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 586 CG CD CE NZ
REMARK 470 GLU B 75 CG CD OE1 OE2
REMARK 470 ARG B 78 CD NE CZ NH1 NH2
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 ARG B 135 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 GLU B 195 CG CD OE1 OE2
REMARK 470 TRP B 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 224 CZ3 CH2
REMARK 470 GLN B 243 CG CD OE1 NE2
REMARK 470 PRO B 270 CG CD
REMARK 470 LYS B 273 CG CD CE NZ
REMARK 470 GLU B 277 CG CD OE1 OE2
REMARK 470 LYS B 347 CE NZ
REMARK 470 GLU B 412 CG CD OE1 OE2
REMARK 470 GLU B 421 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 LYS B 507 CG CD CE NZ
REMARK 470 ARG B 554 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 566 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 633 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 30 CD CE NZ
REMARK 470 ARG C 53 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 69 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 75 CG CD OE1 OE2
REMARK 470 ARG C 78 NE CZ NH1 NH2
REMARK 470 LEU C 107 CG CD1 CD2
REMARK 470 ARG C 116 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 117 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 123 CG OD1 ND2
REMARK 470 VAL C 125 CG1 CG2
REMARK 470 ARG C 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 184 CG CD OE1 OE2
REMARK 470 LYS C 187 CG CD CE NZ
REMARK 470 ARG C 189 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 ILE C 196 CG1 CG2 CD1
REMARK 470 ARG C 208 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 223 CG CD OE1 NE2
REMARK 470 ARG C 225 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 243 CG CD OE1 NE2
REMARK 470 LYS C 244 CG CD CE NZ
REMARK 470 LEU C 245 CG CD1 CD2
REMARK 470 ASP C 247 CG OD1 OD2
REMARK 470 GLN C 262 CG CD OE1 NE2
REMARK 470 LYS C 273 CG CD CE NZ
REMARK 470 ASN C 275 CG OD1 ND2
REMARK 470 ASN C 286 CG OD1 ND2
REMARK 470 ARG C 290 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 347 CE NZ
REMARK 470 GLU C 364 CD OE1 OE2
REMARK 470 ARG C 376 NE CZ NH1 NH2
REMARK 470 GLU C 400 CG CD OE1 OE2
REMARK 470 GLU C 421 CG CD OE1 OE2
REMARK 470 ARG C 554 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 12 CG OD1 OD2
REMARK 470 LYS D 30 CD CE NZ
REMARK 470 ARG D 57 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 64 CG CD OE1 OE2
REMARK 470 ARG D 69 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 75 CG CD OE1 OE2
REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2
REMARK 470 SER D 97 OG
REMARK 470 GLU D 114 CG CD OE1 OE2
REMARK 470 ARG D 116 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 117 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 120 CG ND1 CD2 CE1 NE2
REMARK 470 PHE D 121 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 135 CG CD NE CZ NH1 NH2
REMARK 470 THR D 141 OG1 CG2
REMARK 470 TRP D 179 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 179 CZ3 CH2
REMARK 470 VAL D 183 CG1 CG2
REMARK 470 GLU D 184 CG CD OE1 OE2
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 LEU D 188 CG CD1 CD2
REMARK 470 ARG D 189 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 190 CG CD OE1 OE2
REMARK 470 GLU D 195 CG CD OE1 OE2
REMARK 470 ILE D 196 CG1 CG2 CD1
REMARK 470 ARG D 208 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 223 CG CD OE1 NE2
REMARK 470 TRP D 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 224 CZ3 CH2
REMARK 470 GLN D 243 CG CD OE1 NE2
REMARK 470 LEU D 245 CG CD1 CD2
REMARK 470 ASN D 275 CG OD1 ND2
REMARK 470 ASN D 286 CG OD1 ND2
REMARK 470 ARG D 290 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 347 CE NZ
REMARK 470 ARG D 399 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 421 CG CD OE1 OE2
REMARK 470 GLU D 423 CG CD OE1 OE2
REMARK 470 LYS D 425 CG CD CE NZ
REMARK 470 ARG D 636 CG CD NE CZ NH1 NH2
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 VAL D 118 CG1 - CB - CG2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 VAL D 304 CG1 - CB - CG2 ANGL. DEV. = -12.3 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 ALA A 103 85.81 -155.49
REMARK 500 SER A 250 -165.69 -166.60
REMARK 500 ASP A 293 53.53 -96.49
REMARK 500 ARG A 480 45.15 -152.50
REMARK 500 THR A 483 -97.79 -102.69
REMARK 500 SER A 514 -119.92 62.80
REMARK 500 ALA B 103 93.71 -160.59
REMARK 500 SER B 250 -169.34 -167.80
REMARK 500 ASP B 293 51.68 -94.24
REMARK 500 ARG B 480 46.59 -154.41
REMARK 500 THR B 483 -96.63 -103.23
REMARK 500 SER B 514 -117.39 64.42
REMARK 500 SER C 250 -168.53 -167.57
REMARK 500 ASP C 293 56.33 -94.78
REMARK 500 ARG C 480 46.58 -153.68
REMARK 500 THR C 483 -97.15 -102.55
REMARK 500 SER C 514 -120.63 62.39
REMARK 500 SER D 250 -169.99 -167.53
REMARK 500 ASP D 293 54.41 -93.03
REMARK 500 ASP D 350 89.44 -157.40
REMARK 500 ARG D 480 46.55 -154.84
REMARK 500 THR D 483 -97.61 -102.64
REMARK 500 SER D 514 -118.95 63.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1079 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH C1015 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH C1016 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH D 890 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH D 891 DISTANCE = 6.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YZM RELATED DB: PDB
REMARK 900 5YZM CONTAINS THE SAME PROTEIN IN DIFFERENT CRYSTALLIZATION
REMARK 900 CONDITION
DBREF 6IGP A 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IGP B 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IGP C 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IGP D 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
SEQADV 6IGP GLY A 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP SER A 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP GLY B 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP SER B 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP GLY C 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP SER C 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP GLY D 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGP SER D 1 UNP Q9RXY9 EXPRESSION TAG
SEQRES 1 A 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 A 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 A 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 A 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 A 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 A 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 A 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 A 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 A 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 A 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 A 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 A 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 A 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 A 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 A 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 A 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 A 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 A 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 A 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 A 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 A 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 A 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 A 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 A 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 A 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 A 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 A 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 A 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 A 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 A 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 A 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 A 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 A 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 A 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 A 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 A 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 A 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 A 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 A 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 A 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 A 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 A 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 A 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 A 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 A 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 A 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 A 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 A 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 A 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 A 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 A 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 B 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 B 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 B 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 B 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 B 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 B 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 B 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 B 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 B 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 B 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 B 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 B 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 B 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 B 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 B 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 B 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 B 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 B 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 B 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 B 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 B 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 B 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 B 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 B 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 B 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 B 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 B 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 B 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 B 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 B 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 B 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 B 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 B 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 B 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 B 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 B 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 B 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 B 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 B 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 B 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 B 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 B 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 B 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 B 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 B 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 B 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 B 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 B 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 B 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 B 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 B 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 C 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 C 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 C 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 C 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 C 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 C 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 C 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 C 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 C 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 C 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 C 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 C 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 C 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 C 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 C 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 C 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 C 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 C 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 C 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 C 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 C 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 C 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 C 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 C 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 C 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 C 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 C 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 C 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 C 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 C 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 C 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 C 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 C 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 C 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 C 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 C 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 C 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 C 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 C 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 C 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 C 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 C 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 C 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 C 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 C 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 C 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 C 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 C 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 C 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 C 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 C 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 D 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 D 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 D 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 D 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 D 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 D 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 D 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 D 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 D 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 D 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 D 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 D 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 D 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 D 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 D 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 D 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 D 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 D 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 D 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 D 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 D 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 D 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 D 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 D 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 D 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 D 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 D 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 D 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 D 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 D 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 D 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 D 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 D 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 D 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 D 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 D 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 D 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 D 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 D 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 D 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 D 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 D 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 D 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 D 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 D 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 D 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 D 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 D 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 D 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 D 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 D 656 TRP LEU GLU ARG TRP LEU
HET GOL A 701 6
HET GOL B 701 6
HET GOL C 701 6
HET GOL C 702 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *960(H2 O)
HELIX 1 AA1 GLY A 10 LEU A 17 5 8
HELIX 2 AA2 ASP A 217 SER A 222 1 6
HELIX 3 AA3 LEU A 390 PHE A 394 5 5
HELIX 4 AA4 THR A 445 ARG A 454 1 10
HELIX 5 AA5 GLY A 470 ALA A 476 1 7
HELIX 6 AA6 THR A 483 VAL A 500 1 18
HELIX 7 AA7 SER A 514 GLY A 525 1 12
HELIX 8 AA8 ASN A 541 SER A 549 1 9
HELIX 9 AA9 ILE A 551 GLY A 561 1 11
HELIX 10 AB1 ARG A 566 LEU A 576 1 11
HELIX 11 AB2 SER A 577 VAL A 585 5 9
HELIX 12 AB3 VAL A 602 HIS A 615 1 14
HELIX 13 AB4 HIS A 629 GLY A 635 1 7
HELIX 14 AB5 PRO A 637 LEU A 655 1 19
HELIX 15 AB6 GLY B 10 LEU B 17 5 8
HELIX 16 AB7 LEU B 390 PHE B 394 5 5
HELIX 17 AB8 THR B 445 ARG B 454 1 10
HELIX 18 AB9 GLY B 470 ALA B 476 1 7
HELIX 19 AC1 THR B 483 VAL B 500 1 18
HELIX 20 AC2 SER B 514 GLY B 525 1 12
HELIX 21 AC3 ASN B 541 SER B 549 1 9
HELIX 22 AC4 ILE B 551 GLY B 561 1 11
HELIX 23 AC5 ARG B 566 LEU B 576 1 11
HELIX 24 AC6 SER B 577 VAL B 585 5 9
HELIX 25 AC7 VAL B 602 HIS B 615 1 14
HELIX 26 AC8 HIS B 629 GLY B 635 1 7
HELIX 27 AC9 PRO B 637 LEU B 655 1 19
HELIX 28 AD1 GLY C 10 LEU C 17 5 8
HELIX 29 AD2 LEU C 390 PHE C 394 5 5
HELIX 30 AD3 THR C 445 ARG C 454 1 10
HELIX 31 AD4 GLY C 470 ALA C 476 1 7
HELIX 32 AD5 THR C 483 VAL C 500 1 18
HELIX 33 AD6 SER C 514 GLY C 525 1 12
HELIX 34 AD7 ASN C 541 SER C 549 1 9
HELIX 35 AD8 ILE C 551 GLY C 561 1 11
HELIX 36 AD9 ARG C 566 LEU C 576 1 11
HELIX 37 AE1 SER C 577 VAL C 585 5 9
HELIX 38 AE2 VAL C 602 HIS C 615 1 14
HELIX 39 AE3 HIS C 629 GLY C 635 1 7
HELIX 40 AE4 PRO C 637 LEU C 655 1 19
HELIX 41 AE5 GLY D 10 LEU D 17 5 8
HELIX 42 AE6 LEU D 390 PHE D 394 5 5
HELIX 43 AE7 THR D 445 ARG D 454 1 10
HELIX 44 AE8 GLY D 470 ALA D 476 1 7
HELIX 45 AE9 THR D 483 VAL D 500 1 18
HELIX 46 AF1 SER D 514 GLY D 525 1 12
HELIX 47 AF2 ASN D 541 SER D 549 1 9
HELIX 48 AF3 ILE D 551 GLY D 561 1 11
HELIX 49 AF4 ARG D 566 LEU D 576 1 11
HELIX 50 AF5 SER D 577 VAL D 585 5 9
HELIX 51 AF6 VAL D 602 HIS D 615 1 14
HELIX 52 AF7 HIS D 629 GLY D 635 1 7
HELIX 53 AF8 PRO D 637 LEU D 655 1 19
SHEET 1 AA1 4 PHE A 19 VAL A 25 0
SHEET 2 AA1 4 VAL A 32 GLN A 38 -1 O ALA A 33 N GLN A 24
SHEET 3 AA1 4 ARG A 57 SER A 63 -1 O TRP A 61 N PHE A 34
SHEET 4 AA1 4 ARG A 69 PRO A 70 -1 O ARG A 69 N LEU A 62
SHEET 1 AA2 4 GLY A 79 TRP A 85 0
SHEET 2 AA2 4 ASN A 91 SER A 97 -1 O ALA A 93 N ARG A 84
SHEET 3 AA2 4 ALA A 104 PRO A 109 -1 O MET A 106 N PHE A 94
SHEET 4 AA2 4 ARG A 116 ARG A 117 -1 O ARG A 116 N LEU A 107
SHEET 1 AA3 4 VAL A 125 TRP A 130 0
SHEET 2 AA3 4 PHE A 136 THR A 141 -1 O ALA A 138 N GLN A 129
SHEET 3 AA3 4 ALA A 177 ASP A 182 -1 O TRP A 179 N PHE A 139
SHEET 4 AA3 4 LYS A 187 TYR A 192 -1 O LYS A 187 N ASP A 182
SHEET 1 AA4 7 LEU A 201 TRP A 203 0
SHEET 2 AA4 7 GLY A 209 GLN A 214 -1 O LEU A 211 N SER A 202
SHEET 3 AA4 7 GLN A 226 PRO A 232 -1 O TYR A 229 N ILE A 212
SHEET 4 AA4 7 GLN A 243 PRO A 257 -1 O GLN A 243 N ASP A 230
SHEET 5 AA4 7 PHE A 264 ARG A 269 -1 O ILE A 267 N HIS A 253
SHEET 6 AA4 7 HIS A 280 GLU A 285 -1 O ILE A 284 N PHE A 264
SHEET 7 AA4 7 GLN A 288 ARG A 291 -1 O ARG A 290 N LEU A 283
SHEET 1 AA5 4 ARG A 318 TRP A 319 0
SHEET 2 AA5 4 THR A 324 VAL A 331 -1 O LEU A 326 N ARG A 318
SHEET 3 AA5 4 SER A 334 HIS A 341 -1 O ALA A 340 N LEU A 325
SHEET 4 AA5 4 GLY A 344 ASP A 350 -1 O ASP A 350 N LEU A 337
SHEET 1 AA6 4 GLY A 355 ALA A 362 0
SHEET 2 AA6 4 VAL A 367 SER A 373 -1 O GLU A 372 N VAL A 356
SHEET 3 AA6 4 GLU A 379 LEU A 382 -1 O GLU A 381 N LEU A 369
SHEET 4 AA6 4 GLN A 385 ARG A 386 -1 O GLN A 385 N LEU A 382
SHEET 1 AA7 8 GLN A 402 THR A 408 0
SHEET 2 AA7 8 GLY A 411 LEU A 418 -1 O GLY A 413 N PHE A 406
SHEET 3 AA7 8 GLY A 457 SER A 461 -1 O TYR A 460 N TRP A 416
SHEET 4 AA7 8 VAL A 426 ILE A 432 1 N LEU A 429 O CYS A 459
SHEET 5 AA7 8 LEU A 503 GLY A 513 1 O ALA A 509 N LEU A 430
SHEET 6 AA7 8 ALA A 532 ASP A 536 1 O ASP A 536 N GLY A 512
SHEET 7 AA7 8 THR A 589 SER A 594 1 O LEU A 590 N THR A 535
SHEET 8 AA7 8 VAL A 619 PHE A 624 1 O ARG A 620 N ILE A 591
SHEET 1 AA8 4 PHE B 19 VAL B 25 0
SHEET 2 AA8 4 VAL B 32 GLN B 38 -1 O ALA B 33 N GLN B 24
SHEET 3 AA8 4 ARG B 57 SER B 63 -1 O ARG B 57 N GLN B 38
SHEET 4 AA8 4 ARG B 69 PRO B 70 -1 O ARG B 69 N LEU B 62
SHEET 1 AA9 4 GLY B 79 TRP B 85 0
SHEET 2 AA9 4 ASN B 91 SER B 97 -1 O ALA B 93 N ARG B 84
SHEET 3 AA9 4 ALA B 104 PRO B 109 -1 O MET B 106 N PHE B 94
SHEET 4 AA9 4 ARG B 116 ARG B 117 -1 O ARG B 116 N LEU B 107
SHEET 1 AB1 4 VAL B 125 TRP B 130 0
SHEET 2 AB1 4 PHE B 136 THR B 141 -1 O ALA B 138 N GLN B 129
SHEET 3 AB1 4 ALA B 177 ASP B 182 -1 O TRP B 179 N PHE B 139
SHEET 4 AB1 4 LYS B 187 TYR B 192 -1 O TYR B 192 N LEU B 178
SHEET 1 AB2 4 LEU B 201 TRP B 203 0
SHEET 2 AB2 4 GLY B 209 GLN B 214 -1 O LEU B 211 N SER B 202
SHEET 3 AB2 4 GLN B 226 PRO B 232 -1 O TYR B 229 N ILE B 212
SHEET 4 AB2 4 GLN B 243 SER B 250 -1 O GLN B 243 N ASP B 230
SHEET 1 AB3 4 ALA B 252 PRO B 257 0
SHEET 2 AB3 4 PHE B 264 GLY B 268 -1 O ILE B 267 N HIS B 253
SHEET 3 AB3 4 HIS B 280 GLU B 285 -1 O ILE B 284 N PHE B 264
SHEET 4 AB3 4 GLN B 288 ARG B 291 -1 O ARG B 290 N LEU B 283
SHEET 1 AB4 4 ARG B 318 ASP B 321 0
SHEET 2 AB4 4 THR B 324 VAL B 331 -1 O LEU B 326 N ARG B 318
SHEET 3 AB4 4 SER B 334 HIS B 341 -1 O PHE B 338 N PHE B 327
SHEET 4 AB4 4 VAL B 346 ASP B 350 -1 O ASP B 350 N LEU B 337
SHEET 1 AB5 4 GLY B 355 ALA B 362 0
SHEET 2 AB5 4 VAL B 367 SER B 373 -1 O GLU B 372 N VAL B 356
SHEET 3 AB5 4 ARG B 376 LEU B 382 -1 O GLU B 381 N LEU B 369
SHEET 4 AB5 4 GLN B 385 ARG B 386 -1 O GLN B 385 N LEU B 382
SHEET 1 AB6 8 GLN B 402 THR B 408 0
SHEET 2 AB6 8 GLY B 411 LEU B 418 -1 O GLY B 413 N PHE B 406
SHEET 3 AB6 8 GLY B 457 SER B 461 -1 O TYR B 460 N TRP B 416
SHEET 4 AB6 8 VAL B 426 ILE B 432 1 N PRO B 427 O GLY B 457
SHEET 5 AB6 8 LEU B 503 GLY B 513 1 O ALA B 509 N LEU B 430
SHEET 6 AB6 8 ALA B 532 ASP B 536 1 O ASP B 536 N GLY B 512
SHEET 7 AB6 8 THR B 589 SER B 594 1 O LEU B 590 N THR B 535
SHEET 8 AB6 8 VAL B 619 PHE B 624 1 O ARG B 620 N ILE B 591
SHEET 1 AB7 4 PHE C 19 VAL C 25 0
SHEET 2 AB7 4 VAL C 32 GLN C 38 -1 O ALA C 33 N GLN C 24
SHEET 3 AB7 4 ARG C 57 SER C 63 -1 O TRP C 61 N PHE C 34
SHEET 4 AB7 4 ARG C 69 PRO C 70 -1 O ARG C 69 N LEU C 62
SHEET 1 AB8 4 GLY C 79 TRP C 85 0
SHEET 2 AB8 4 ASN C 91 SER C 97 -1 O ALA C 93 N ARG C 84
SHEET 3 AB8 4 ALA C 104 PRO C 109 -1 O MET C 106 N PHE C 94
SHEET 4 AB8 4 ARG C 116 ARG C 117 -1 O ARG C 116 N LEU C 107
SHEET 1 AB9 4 SER C 126 TRP C 130 0
SHEET 2 AB9 4 PHE C 136 THR C 140 -1 O ALA C 138 N GLN C 129
SHEET 3 AB9 4 LEU C 178 ASP C 182 -1 O TRP C 179 N PHE C 139
SHEET 4 AB9 4 LYS C 187 TYR C 192 -1 O TYR C 192 N LEU C 178
SHEET 1 AC1 4 LEU C 201 TRP C 203 0
SHEET 2 AC1 4 GLY C 209 GLN C 214 -1 O LEU C 211 N SER C 202
SHEET 3 AC1 4 GLN C 226 PRO C 232 -1 O TYR C 229 N ILE C 212
SHEET 4 AC1 4 GLN C 243 SER C 250 -1 O GLN C 243 N ASP C 230
SHEET 1 AC2 4 ALA C 252 PRO C 257 0
SHEET 2 AC2 4 PHE C 264 GLY C 268 -1 O ILE C 267 N HIS C 253
SHEET 3 AC2 4 HIS C 280 GLU C 285 -1 O ILE C 284 N PHE C 264
SHEET 4 AC2 4 GLN C 288 ARG C 291 -1 O ARG C 290 N LEU C 283
SHEET 1 AC3 4 ARG C 318 TRP C 319 0
SHEET 2 AC3 4 THR C 324 VAL C 331 -1 O LEU C 326 N ARG C 318
SHEET 3 AC3 4 SER C 334 HIS C 341 -1 O PHE C 338 N PHE C 327
SHEET 4 AC3 4 LYS C 347 ASP C 350 -1 O ASP C 350 N LEU C 337
SHEET 1 AC4 4 GLY C 355 ALA C 362 0
SHEET 2 AC4 4 VAL C 367 SER C 373 -1 O GLU C 372 N VAL C 356
SHEET 3 AC4 4 GLU C 379 LEU C 382 -1 O GLU C 381 N LEU C 369
SHEET 4 AC4 4 GLN C 385 ARG C 386 -1 O GLN C 385 N LEU C 382
SHEET 1 AC5 8 GLN C 402 THR C 408 0
SHEET 2 AC5 8 GLY C 411 LEU C 418 -1 O GLY C 413 N PHE C 406
SHEET 3 AC5 8 GLY C 457 SER C 461 -1 O TYR C 460 N TRP C 416
SHEET 4 AC5 8 VAL C 426 ILE C 432 1 N PRO C 427 O GLY C 457
SHEET 5 AC5 8 LEU C 503 GLY C 513 1 O ALA C 509 N LEU C 430
SHEET 6 AC5 8 ALA C 532 ASP C 536 1 O ASP C 536 N GLY C 512
SHEET 7 AC5 8 THR C 589 SER C 594 1 O LEU C 590 N THR C 535
SHEET 8 AC5 8 VAL C 619 PHE C 624 1 O ARG C 620 N ILE C 591
SHEET 1 AC6 4 PHE D 19 VAL D 25 0
SHEET 2 AC6 4 VAL D 32 GLN D 38 -1 O ALA D 33 N GLN D 24
SHEET 3 AC6 4 ARG D 57 SER D 63 -1 O ARG D 57 N GLN D 38
SHEET 4 AC6 4 ARG D 69 PRO D 70 -1 O ARG D 69 N LEU D 62
SHEET 1 AC7 4 GLY D 79 TRP D 85 0
SHEET 2 AC7 4 ASN D 91 SER D 97 -1 O ALA D 93 N ARG D 84
SHEET 3 AC7 4 ALA D 104 PRO D 109 -1 O MET D 106 N PHE D 94
SHEET 4 AC7 4 ARG D 116 ARG D 117 -1 O ARG D 116 N LEU D 107
SHEET 1 AC8 4 GLN D 129 TRP D 130 0
SHEET 2 AC8 4 PHE D 136 THR D 140 -1 O ALA D 138 N GLN D 129
SHEET 3 AC8 4 LEU D 178 ASP D 182 -1 O TRP D 179 N PHE D 139
SHEET 4 AC8 4 LYS D 187 TYR D 192 -1 O TYR D 192 N LEU D 178
SHEET 1 AC9 4 LEU D 201 TRP D 203 0
SHEET 2 AC9 4 GLY D 209 GLN D 214 -1 O LEU D 211 N SER D 202
SHEET 3 AC9 4 GLN D 226 PRO D 232 -1 O TYR D 229 N ILE D 212
SHEET 4 AC9 4 GLN D 243 SER D 250 -1 O GLN D 243 N ASP D 230
SHEET 1 AD1 4 ALA D 252 PRO D 257 0
SHEET 2 AD1 4 PHE D 264 GLY D 268 -1 O ILE D 267 N HIS D 253
SHEET 3 AD1 4 HIS D 280 GLU D 285 -1 O ILE D 284 N PHE D 264
SHEET 4 AD1 4 GLN D 288 ARG D 291 -1 O ARG D 290 N LEU D 283
SHEET 1 AD2 4 ARG D 318 TRP D 319 0
SHEET 2 AD2 4 THR D 324 VAL D 331 -1 O LEU D 326 N ARG D 318
SHEET 3 AD2 4 SER D 334 HIS D 341 -1 O PHE D 338 N PHE D 327
SHEET 4 AD2 4 VAL D 346 ASP D 350 -1 O LYS D 347 N THR D 339
SHEET 1 AD3 4 GLY D 355 ALA D 362 0
SHEET 2 AD3 4 VAL D 367 SER D 373 -1 O GLU D 372 N VAL D 356
SHEET 3 AD3 4 ARG D 376 LEU D 382 -1 O GLU D 381 N LEU D 369
SHEET 4 AD3 4 GLN D 385 ARG D 386 -1 O GLN D 385 N LEU D 382
SHEET 1 AD4 8 GLN D 402 THR D 408 0
SHEET 2 AD4 8 GLY D 411 LEU D 418 -1 O GLY D 413 N PHE D 406
SHEET 3 AD4 8 GLY D 457 SER D 461 -1 O TYR D 460 N TRP D 416
SHEET 4 AD4 8 VAL D 426 ILE D 432 1 N PRO D 427 O GLY D 457
SHEET 5 AD4 8 LEU D 503 GLY D 513 1 O ASP D 504 N VAL D 426
SHEET 6 AD4 8 ALA D 532 ASP D 536 1 O ASP D 536 N GLY D 512
SHEET 7 AD4 8 THR D 589 SER D 594 1 O LEU D 590 N THR D 535
SHEET 8 AD4 8 VAL D 619 PHE D 624 1 O ARG D 620 N ILE D 591
CISPEP 1 GLY A 435 PRO A 436 0 10.41
CISPEP 2 GLY B 435 PRO B 436 0 9.65
CISPEP 3 GLY C 435 PRO C 436 0 8.59
CISPEP 4 GLY D 435 PRO D 436 0 8.76
SITE 1 AC1 7 ALA A 374 GLY A 443 PHE A 444 THR A 445
SITE 2 AC1 7 PHE A 448 GLN A 449 TYR A 460
SITE 1 AC2 2 ARG B 537 HIS B 629
SITE 1 AC3 6 ARG B 399 GLU B 400 VAL B 417 LEU B 419
SITE 2 AC3 6 GLU C 409 ARG C 480
SITE 1 AC4 1 HIS C 298
CRYST1 119.857 130.492 194.973 90.00 90.00 90.00 P 21 21 21 16
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 0.008343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005129 0.00000
TER 4613 LEU A 655
TER 9124 LEU B 655
TER 13548 LEU C 655
TER 17930 LEU D 655
MASTER 785 0 4 53 143 0 6 618910 4 24 204
END
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