HEADER IMMUNE SYSTEM 11-FEB-14 4ORG
TITLE CRYSTAL STRUCTURE OF HUMAN FAB CAP256-VRC26.04, A POTENT V1V2-DIRECTED
TITLE 2 HIV-1 NEUTRALIZING ANTIBODY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAP256-VRC26.04 LIGHT CHAIN;
COMPND 3 CHAIN: L, B, D, F;
COMPND 4 FRAGMENT: FAB;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CAP256-VRC26.04 HEAVY CHAIN;
COMPND 8 CHAIN: H, A, C, E;
COMPND 9 FRAGMENT: FAB;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVRC8400;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PVRC8400
KEYWDS FAB, HIV-1, V1V2, CAP256, VRC26, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GORMAN,N.A.DORIA-ROSE,C.A.SCHRAMM,P.L.MOORE,J.R.MASCOLA,L.SHAPIRO,
AUTHOR 2 L.MORRIS,P.D.KWONG
REVDAT 5 06-DEC-23 4ORG 1 REMARK
REVDAT 4 20-SEP-23 4ORG 1 LINK
REVDAT 3 14-MAY-14 4ORG 1 JRNL
REVDAT 2 02-APR-14 4ORG 1 JRNL
REVDAT 1 26-FEB-14 4ORG 0
JRNL AUTH N.A.DORIA-ROSE,C.A.SCHRAMM,J.GORMAN,P.L.MOORE,J.N.BHIMAN,
JRNL AUTH 2 B.J.DEKOSKY,M.J.ERNANDES,I.S.GEORGIEV,H.J.KIM,M.PANCERA,
JRNL AUTH 3 R.P.STAUPE,H.R.ALTAE-TRAN,R.T.BAILER,E.T.CROOKS,A.CUPO,
JRNL AUTH 4 A.DRUZ,N.J.GARRETT,K.H.HOI,R.KONG,M.K.LOUDER,N.S.LONGO,
JRNL AUTH 5 K.MCKEE,M.NONYANE,S.O'DELL,R.S.ROARK,R.S.RUDICELL,
JRNL AUTH 6 S.D.SCHMIDT,D.J.SHEWARD,C.SOTO,C.K.WIBMER,Y.YANG,Z.ZHANG,
JRNL AUTH 7 NISC COMPARATIVE SEQUENCING,J.C.MULLIKIN,J.M.BINLEY,
JRNL AUTH 8 R.W.SANDERS,I.A.WILSON,J.P.MOORE,A.B.WARD,G.GEORGIOU,
JRNL AUTH 9 C.WILLIAMSON,S.S.ABDOOL KARIM,L.MORRIS,P.D.KWONG,L.SHAPIRO,
JRNL AUTH10 J.R.MASCOLA
JRNL TITL DEVELOPMENTAL PATHWAY FOR POTENT V1V2-DIRECTED
JRNL TITL 2 HIV-NEUTRALIZING ANTIBODIES.
JRNL REF NATURE V. 509 55 2014
JRNL REFN ISSN 0028-0836
JRNL PMID 24590074
JRNL DOI 10.1038/NATURE13036
REMARK 2
REMARK 2 RESOLUTION. 3.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 36066
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.275
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1808
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 35.6314 - 7.3189 0.84 2401 126 0.2127 0.2102
REMARK 3 2 7.3189 - 5.8175 0.98 2783 149 0.2544 0.2553
REMARK 3 3 5.8175 - 5.0845 0.98 2806 146 0.2488 0.2496
REMARK 3 4 5.0845 - 4.6207 0.98 2765 143 0.2322 0.2356
REMARK 3 5 4.6207 - 4.2901 0.97 2752 149 0.2455 0.2418
REMARK 3 6 4.2901 - 4.0375 0.98 2775 143 0.2686 0.3209
REMARK 3 7 4.0375 - 3.8356 0.98 2809 156 0.2954 0.3204
REMARK 3 8 3.8356 - 3.6688 0.98 2768 138 0.3043 0.3201
REMARK 3 9 3.6688 - 3.5277 0.97 2782 144 0.3196 0.3456
REMARK 3 10 3.5277 - 3.4060 0.96 2681 151 0.3264 0.3450
REMARK 3 11 3.4060 - 3.2996 0.92 2661 139 0.3526 0.3759
REMARK 3 12 3.2996 - 3.2054 0.87 2458 128 0.3614 0.4062
REMARK 3 13 3.2054 - 3.1210 0.64 1817 96 0.3884 0.4286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.180
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 : 0.003 13741
REMARK 3 ANGLE : 0.726 18695
REMARK 3 CHIRALITY : 0.027 2107
REMARK 3 PLANARITY : 0.004 2384
REMARK 3 DIHEDRAL : 10.624 4870
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN L AND ( RESID 3 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7915 -31.4154 -10.6714
REMARK 3 T TENSOR
REMARK 3 T11: 0.4831 T22: 0.5086
REMARK 3 T33: 0.3543 T12: -0.0200
REMARK 3 T13: -0.0705 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.0186 L22: -0.0005
REMARK 3 L33: 0.0303 L12: 0.0126
REMARK 3 L13: 0.0064 L23: 0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.1202 S12: 0.0785 S13: 0.0796
REMARK 3 S21: -0.0221 S22: 0.0990 S23: -0.0128
REMARK 3 S31: -0.1808 S32: 0.0817 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN L AND ( RESID 110 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7690 -44.8590 -34.7613
REMARK 3 T TENSOR
REMARK 3 T11: -0.1706 T22: -0.0258
REMARK 3 T33: 0.1268 T12: -0.2301
REMARK 3 T13: 0.0036 T23: 0.1523
REMARK 3 L TENSOR
REMARK 3 L11: 0.0481 L22: -0.0170
REMARK 3 L33: -0.0094 L12: 0.0151
REMARK 3 L13: 0.0126 L23: 0.0518
REMARK 3 S TENSOR
REMARK 3 S11: -0.0863 S12: 0.0474 S13: 0.0992
REMARK 3 S21: -0.1183 S22: -0.0875 S23: 0.0621
REMARK 3 S31: -0.0246 S32: -0.0390 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN H AND ( RESID 2 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1032 -24.0975 -3.5649
REMARK 3 T TENSOR
REMARK 3 T11: 0.4608 T22: 0.2351
REMARK 3 T33: 0.3783 T12: 0.0432
REMARK 3 T13: -0.0488 T23: -0.0977
REMARK 3 L TENSOR
REMARK 3 L11: 0.0324 L22: 0.0112
REMARK 3 L33: 0.0196 L12: -0.0255
REMARK 3 L13: 0.0087 L23: -0.0029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: 0.2177 S13: 0.0905
REMARK 3 S21: 0.0877 S22: -0.0285 S23: 0.0354
REMARK 3 S31: -0.1672 S32: -0.1039 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN H AND ( RESID 114 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1830 -57.8542 -33.6246
REMARK 3 T TENSOR
REMARK 3 T11: 0.2012 T22: 0.1448
REMARK 3 T33: 0.2998 T12: -0.4216
REMARK 3 T13: 0.0753 T23: -0.1884
REMARK 3 L TENSOR
REMARK 3 L11: 0.0241 L22: 0.0039
REMARK 3 L33: -0.0089 L12: -0.0028
REMARK 3 L13: 0.0065 L23: 0.0030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: -0.1722 S13: -0.1882
REMARK 3 S21: 0.0307 S22: -0.1082 S23: -0.0026
REMARK 3 S31: 0.0870 S32: 0.0888 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND ( RESID 3 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3494 -39.3780 38.0137
REMARK 3 T TENSOR
REMARK 3 T11: 0.3864 T22: 0.2873
REMARK 3 T33: 0.3558 T12: -0.0176
REMARK 3 T13: -0.0382 T23: -0.0949
REMARK 3 L TENSOR
REMARK 3 L11: 0.0275 L22: 0.0081
REMARK 3 L33: 0.0242 L12: 0.0071
REMARK 3 L13: 0.0059 L23: 0.0176
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: 0.0511 S13: 0.0942
REMARK 3 S21: -0.0173 S22: -0.0143 S23: -0.0878
REMARK 3 S31: -0.1395 S32: 0.0741 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND ( RESID 110 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2047 -52.5004 13.8046
REMARK 3 T TENSOR
REMARK 3 T11: 0.0265 T22: 0.5650
REMARK 3 T33: 0.3255 T12: 0.2224
REMARK 3 T13: 0.1483 T23: -0.2050
REMARK 3 L TENSOR
REMARK 3 L11: 0.0323 L22: 0.0096
REMARK 3 L33: 0.0194 L12: 0.0285
REMARK 3 L13: 0.0012 L23: 0.0358
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0021 S13: 0.1183
REMARK 3 S21: -0.0955 S22: 0.1196 S23: 0.0542
REMARK 3 S31: -0.0087 S32: 0.0277 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND ( RESID 2 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5652 -32.6694 44.2912
REMARK 3 T TENSOR
REMARK 3 T11: 0.3165 T22: 0.4986
REMARK 3 T33: 0.2963 T12: 0.0750
REMARK 3 T13: -0.0402 T23: -0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 0.0138 L22: 0.0001
REMARK 3 L33: 0.0322 L12: 0.0086
REMARK 3 L13: 0.0008 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: 0.1037 S13: -0.0397
REMARK 3 S21: 0.0832 S22: -0.0407 S23: 0.0371
REMARK 3 S31: -0.2128 S32: -0.1169 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND ( RESID 114 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4767 -65.5184 14.7968
REMARK 3 T TENSOR
REMARK 3 T11: -0.3629 T22: 0.0741
REMARK 3 T33: 0.1361 T12: 0.4298
REMARK 3 T13: -0.1860 T23: 0.1901
REMARK 3 L TENSOR
REMARK 3 L11: 0.0127 L22: 0.0056
REMARK 3 L33: -0.0095 L12: 0.0009
REMARK 3 L13: 0.0094 L23: -0.0148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0201 S12: -0.0511 S13: -0.0035
REMARK 3 S21: -0.0233 S22: -0.0581 S23: -0.0060
REMARK 3 S31: 0.2283 S32: -0.1059 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN D AND ( RESID 3 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3497 6.2218 -14.7783
REMARK 3 T TENSOR
REMARK 3 T11: 0.5568 T22: 0.4180
REMARK 3 T33: 0.4400 T12: -0.1719
REMARK 3 T13: 0.1250 T23: -0.1163
REMARK 3 L TENSOR
REMARK 3 L11: 0.0337 L22: 0.0143
REMARK 3 L33: 0.0202 L12: -0.0045
REMARK 3 L13: 0.0057 L23: 0.0157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: 0.0258 S13: -0.0607
REMARK 3 S21: -0.0114 S22: 0.0280 S23: 0.0228
REMARK 3 S31: 0.0633 S32: 0.0851 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN D AND ( RESID 110 THROUGH 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3915 17.7075 10.8622
REMARK 3 T TENSOR
REMARK 3 T11: 0.1156 T22: 0.3364
REMARK 3 T33: 0.3627 T12: -0.0772
REMARK 3 T13: 0.1559 T23: -0.2087
REMARK 3 L TENSOR
REMARK 3 L11: 0.0472 L22: -0.0007
REMARK 3 L33: 0.0083 L12: 0.0079
REMARK 3 L13: 0.0044 L23: 0.0394
REMARK 3 S TENSOR
REMARK 3 S11: -0.0508 S12: -0.0217 S13: -0.0402
REMARK 3 S21: 0.0581 S22: 0.0453 S23: 0.0257
REMARK 3 S31: -0.0339 S32: 0.0772 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND ( RESID 2 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8885 -3.2839 -19.5180
REMARK 3 T TENSOR
REMARK 3 T11: 0.4139 T22: 0.3401
REMARK 3 T33: 0.4128 T12: -0.0794
REMARK 3 T13: -0.0260 T23: -0.1428
REMARK 3 L TENSOR
REMARK 3 L11: 0.0312 L22: 0.0027
REMARK 3 L33: 0.0197 L12: 0.0020
REMARK 3 L13: 0.0204 L23: 0.0056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0478 S12: -0.0238 S13: 0.0547
REMARK 3 S21: 0.0045 S22: -0.0641 S23: 0.1003
REMARK 3 S31: 0.0144 S32: -0.1167 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C AND ( RESID 114 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1578 30.1847 9.9456
REMARK 3 T TENSOR
REMARK 3 T11: -0.5135 T22: -0.0631
REMARK 3 T33: 0.2297 T12: -0.3735
REMARK 3 T13: 0.2898 T23: 0.1486
REMARK 3 L TENSOR
REMARK 3 L11: 0.0050 L22: -0.0107
REMARK 3 L33: -0.0002 L12: 0.0008
REMARK 3 L13: 0.0010 L23: -0.0106
REMARK 3 S TENSOR
REMARK 3 S11: 0.0523 S12: 0.1480 S13: 0.0278
REMARK 3 S21: -0.0990 S22: -0.0104 S23: 0.0348
REMARK 3 S31: -0.0108 S32: 0.0304 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN F AND ( RESID 3 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9200 -1.3406 33.8668
REMARK 3 T TENSOR
REMARK 3 T11: 0.2931 T22: 0.2367
REMARK 3 T33: 0.3212 T12: 0.0527
REMARK 3 T13: -0.0583 T23: 0.1107
REMARK 3 L TENSOR
REMARK 3 L11: 0.0292 L22: 0.0084
REMARK 3 L33: 0.0266 L12: -0.0151
REMARK 3 L13: 0.0294 L23: 0.0022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0250 S12: 0.0368 S13: 0.0456
REMARK 3 S21: -0.0745 S22: 0.0534 S23: -0.0271
REMARK 3 S31: 0.0902 S32: 0.0786 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN F AND ( RESID 110 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8215 10.2165 59.6768
REMARK 3 T TENSOR
REMARK 3 T11: 0.1501 T22: 0.1461
REMARK 3 T33: 0.1276 T12: 0.0357
REMARK 3 T13: -0.0044 T23: 0.2574
REMARK 3 L TENSOR
REMARK 3 L11: 0.0414 L22: 0.0102
REMARK 3 L33: 0.0083 L12: -0.0201
REMARK 3 L13: 0.0063 L23: 0.0158
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0892 S13: -0.1068
REMARK 3 S21: 0.1426 S22: 0.1524 S23: 0.0213
REMARK 3 S31: 0.0081 S32: -0.0750 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN E AND ( RESID 2 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5994 -11.1334 29.1049
REMARK 3 T TENSOR
REMARK 3 T11: 0.3965 T22: 0.3729
REMARK 3 T33: 0.4356 T12: 0.0099
REMARK 3 T13: 0.0892 T23: -0.1368
REMARK 3 L TENSOR
REMARK 3 L11: 0.0375 L22: 0.0139
REMARK 3 L33: -0.0107 L12: 0.0181
REMARK 3 L13: -0.0007 L23: 0.0122
REMARK 3 S TENSOR
REMARK 3 S11: -0.0561 S12: -0.0907 S13: -0.1058
REMARK 3 S21: 0.0119 S22: -0.0865 S23: 0.2168
REMARK 3 S31: -0.0372 S32: 0.0267 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN E AND ( RESID 114 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1492 22.5461 58.3491
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.3671
REMARK 3 T33: 0.2820 T12: -0.0083
REMARK 3 T13: -0.0812 T23: -0.0834
REMARK 3 L TENSOR
REMARK 3 L11: 0.0174 L22: -0.0076
REMARK 3 L33: 0.0145 L12: -0.0120
REMARK 3 L13: -0.0010 L23: 0.0117
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: 0.1223 S13: 0.2502
REMARK 3 S21: -0.1807 S22: -0.0267 S23: -0.0950
REMARK 3 S31: -0.1371 S32: 0.0747 S33: 0.0000
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 4ORG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
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 : DOUBLE CRYSTAL SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36109
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.121
REMARK 200 RESOLUTION RANGE LOW (A) : 97.204
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.840
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: PDB ENTRY 4OCW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, 25% ISOPROPANOL, 0.1 M
REMARK 280 TRIS, PH 8.0, CRYOPROTECTANT: 20% ETHYLENE GLYCOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H
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
REMARK 350 BIOMOLECULE: 2
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: 3350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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
REMARK 350 BIOMOLECULE: 3
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: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C
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
REMARK 350 BIOMOLECULE: 4
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: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, E
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 PRO L 2
REMARK 465 THR L 209
REMARK 465 GLU L 210
REMARK 465 CYS L 211
REMARK 465 SER L 212
REMARK 465 GLU H 1
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 GLY H 133
REMARK 465 LYS H 214
REMARK 465 SER H 215
REMARK 465 CYS H 216
REMARK 465 ASP H 217
REMARK 465 LYS H 218
REMARK 465 GLY H 219
REMARK 465 LEU H 220
REMARK 465 GLU H 221
REMARK 465 VAL H 222
REMARK 465 LEU H 223
REMARK 465 PHE H 224
REMARK 465 GLN H 225
REMARK 465 PRO B 2
REMARK 465 ALA B 92
REMARK 465 ALA B 93
REMARK 465 SER B 94
REMARK 465 THR B 209
REMARK 465 GLU B 210
REMARK 465 CYS B 211
REMARK 465 SER B 212
REMARK 465 GLU A 1
REMARK 465 ASP A 100G
REMARK 465 TYS A 100H
REMARK 465 TYS A 100I
REMARK 465 ASP A 100J
REMARK 465 PHE A 100K
REMARK 465 GLY A 100L
REMARK 465 LYS A 100M
REMARK 465 GLN A 100N
REMARK 465 SER A 130
REMARK 465 THR A 131
REMARK 465 SER A 132
REMARK 465 LYS A 214
REMARK 465 SER A 215
REMARK 465 CYS A 216
REMARK 465 ASP A 217
REMARK 465 LYS A 218
REMARK 465 GLY A 219
REMARK 465 LEU A 220
REMARK 465 GLU A 221
REMARK 465 VAL A 222
REMARK 465 LEU A 223
REMARK 465 PHE A 224
REMARK 465 GLN A 225
REMARK 465 PRO D 2
REMARK 465 THR D 95A
REMARK 465 SER D 95B
REMARK 465 ALA D 95C
REMARK 465 ARG D 95D
REMARK 465 GLU D 210
REMARK 465 CYS D 211
REMARK 465 SER D 212
REMARK 465 GLU C 1
REMARK 465 ASP C 100J
REMARK 465 PHE C 100K
REMARK 465 GLY C 100L
REMARK 465 LYS C 100M
REMARK 465 GLN C 100N
REMARK 465 LYS C 129
REMARK 465 SER C 130
REMARK 465 THR C 131
REMARK 465 CYS C 216
REMARK 465 ASP C 217
REMARK 465 LYS C 218
REMARK 465 GLY C 219
REMARK 465 LEU C 220
REMARK 465 GLU C 221
REMARK 465 VAL C 222
REMARK 465 LEU C 223
REMARK 465 PHE C 224
REMARK 465 GLN C 225
REMARK 465 PRO F 2
REMARK 465 THR F 95A
REMARK 465 SER F 95B
REMARK 465 ALA F 95C
REMARK 465 ARG F 95D
REMARK 465 CYS F 211
REMARK 465 SER F 212
REMARK 465 GLU E 1
REMARK 465 TYS E 100I
REMARK 465 ASP E 100J
REMARK 465 PHE E 100K
REMARK 465 GLY E 100L
REMARK 465 LYS E 100M
REMARK 465 GLN E 100N
REMARK 465 LYS E 129
REMARK 465 SER E 130
REMARK 465 THR E 131
REMARK 465 SER E 132
REMARK 465 CYS E 216
REMARK 465 ASP E 217
REMARK 465 LYS E 218
REMARK 465 GLY E 219
REMARK 465 LEU E 220
REMARK 465 GLU E 221
REMARK 465 VAL E 222
REMARK 465 LEU E 223
REMARK 465 PHE E 224
REMARK 465 GLN E 225
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 ASP H 100G CG OD1 OD2
REMARK 470 TYS H 100H CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYS H 100H S O1 O2 O3
REMARK 470 TYS H 100I CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYS H 100I S O1 O2 O3
REMARK 470 ASP H 100J CG OD1 OD2
REMARK 470 LYS A 129 CG CD CE NZ
REMARK 470 TYS C 100H CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYS C 100H S O1 O2 O3
REMARK 470 TYS C 100I CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYS C 100I S O1 O2 O3
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 ILE L 28 -62.87 -138.89
REMARK 500 THR L 51 -54.46 68.63
REMARK 500 SER L 67 -159.61 -143.31
REMARK 500 THR L 76 -79.60 -71.74
REMARK 500 GLU L 83 104.09 -54.46
REMARK 500 TRP L 91 89.67 -150.83
REMARK 500 ALA L 92 164.34 173.89
REMARK 500 THR L 95A -152.86 -142.85
REMARK 500 ARG L 96 -167.53 -74.33
REMARK 500 VAL L 97 -47.84 -137.83
REMARK 500 THR L 102 106.32 -160.02
REMARK 500 THR L 145 87.72 -155.39
REMARK 500 SER L 152 -53.92 68.77
REMARK 500 VAL H 48 -66.30 -93.03
REMARK 500 ASP H 100G -49.94 -131.96
REMARK 500 TYS H 100I -63.43 -91.21
REMARK 500 ASP H 100J 25.94 143.68
REMARK 500 PHE H 100K 66.65 64.76
REMARK 500 GLN H 100N -119.74 -141.74
REMARK 500 PRO H 123 -178.23 -69.06
REMARK 500 THR H 135 60.08 -168.00
REMARK 500 ASP H 144 72.62 46.64
REMARK 500 PHE H 146 142.47 -173.23
REMARK 500 SER H 161 143.85 161.98
REMARK 500 THR H 191 -66.82 -97.93
REMARK 500 ILE B 28 -56.25 -142.97
REMARK 500 LEU B 47 -62.25 -90.15
REMARK 500 THR B 51 -55.86 67.74
REMARK 500 THR B 95A 58.57 -144.28
REMARK 500 SER B 95B 17.12 59.28
REMARK 500 SER B 152 -49.80 68.73
REMARK 500 HIS B 197 105.15 -168.49
REMARK 500 GLU B 198 74.75 54.62
REMARK 500 SER A 28 93.76 -69.09
REMARK 500 VAL A 48 -70.11 -88.53
REMARK 500 ARG A 66 -43.35 -131.40
REMARK 500 GLU A 100C 111.85 -165.92
REMARK 500 ALA A 114 -174.22 -66.07
REMARK 500 SER A 128 40.98 -162.51
REMARK 500 ASP A 144 98.34 34.56
REMARK 500 HIS A 200 79.50 -100.03
REMARK 500 GLN D 17 -176.07 -68.84
REMARK 500 ILE D 28 -45.26 -132.50
REMARK 500 PRO D 44 -177.11 -68.41
REMARK 500 THR D 51 -57.18 64.54
REMARK 500 ALA D 93 -71.34 -63.14
REMARK 500 SER D 106A -61.10 -150.22
REMARK 500 PRO D 141 36.77 -93.71
REMARK 500 SER D 152 -43.42 69.17
REMARK 500 LYS D 156 14.81 -151.29
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OCW RELATED DB: PDB
REMARK 900 V1V2 ANTIBODY FROM THE SAME LINEAGE
REMARK 900 RELATED ID: 4ODH RELATED DB: PDB
REMARK 900 V1V2 ANTIBODY FROM THE SAME LINEAGE
REMARK 900 RELATED ID: 4OCR RELATED DB: PDB
REMARK 900 V1V2 ANTIBODY FROM THE SAME LINEAGE
REMARK 900 RELATED ID: 4OD1 RELATED DB: PDB
REMARK 900 V1V2 ANTIBODY FROM THE SAME LINEAGE
REMARK 900 RELATED ID: 4OD3 RELATED DB: PDB
REMARK 900 V1V2 ANTIBODY FROM THE SAME LINEAGE
REMARK 900 RELATED ID: 4OCS RELATED DB: PDB
REMARK 900 V1V2 ANTIBODY FROM THE SAME LINEAGE
DBREF 4ORG H 1 225 PDB 4ORG 4ORG 1 225
DBREF 4ORG A 1 225 PDB 4ORG 4ORG 1 225
DBREF 4ORG C 1 225 PDB 4ORG 4ORG 1 225
DBREF 4ORG E 1 225 PDB 4ORG 4ORG 1 225
DBREF 4ORG L 2 212 PDB 4ORG 4ORG 2 212
DBREF 4ORG B 2 212 PDB 4ORG 4ORG 2 212
DBREF 4ORG D 2 212 PDB 4ORG 4ORG 2 212
DBREF 4ORG F 2 212 PDB 4ORG 4ORG 2 212
SEQRES 1 L 216 PRO VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA PRO
SEQRES 2 L 216 GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER SER
SEQRES 3 L 216 ASN ILE GLY ASN ASN PHE VAL SER TRP TYR GLN GLN ARG
SEQRES 4 L 216 PRO GLY THR ALA PRO SER LEU LEU ILE TYR GLU THR ASN
SEQRES 5 L 216 LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER
SEQRES 6 L 216 LYS SER ALA THR SER ALA THR LEU ALA ILE THR GLY LEU
SEQRES 7 L 216 GLN THR GLY ASP GLU ALA ASP TYR TYR CYS ALA THR TRP
SEQRES 8 L 216 ALA ALA SER LEU THR SER ALA ARG VAL PHE GLY THR GLY
SEQRES 9 L 216 THR LYS VAL ILE VAL SER GLY GLN PRO LYS ALA ASN PRO
SEQRES 10 L 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER
SEQRES 1 H 256 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 H 256 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLN
SEQRES 3 H 256 PHE SER PHE ASN ARG TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 H 256 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER
SEQRES 5 H 256 TYR ASP GLY THR ASP LYS TYR HIS ALA ASP LYS VAL TRP
SEQRES 6 H 256 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 H 256 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 256 ALA LEU TYR TYR CYS ALA LYS ASP LEU ARG GLU ASP GLU
SEQRES 9 H 256 CYS GLU GLU TRP TRP SER ASP TYS TYS ASP PHE GLY LYS
SEQRES 10 H 256 GLN LEU PRO CYS ARG LYS SER ARG GLY VAL ALA GLY ILE
SEQRES 11 H 256 PHE ASP LYS TRP GLY GLN GLY THR MET VAL ILE VAL SER
SEQRES 12 H 256 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA
SEQRES 13 H 256 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 14 H 256 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 15 H 256 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 16 H 256 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 17 H 256 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 18 H 256 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 19 H 256 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS
SEQRES 20 H 256 ASP LYS GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 B 216 PRO VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA PRO
SEQRES 2 B 216 GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER SER
SEQRES 3 B 216 ASN ILE GLY ASN ASN PHE VAL SER TRP TYR GLN GLN ARG
SEQRES 4 B 216 PRO GLY THR ALA PRO SER LEU LEU ILE TYR GLU THR ASN
SEQRES 5 B 216 LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER
SEQRES 6 B 216 LYS SER ALA THR SER ALA THR LEU ALA ILE THR GLY LEU
SEQRES 7 B 216 GLN THR GLY ASP GLU ALA ASP TYR TYR CYS ALA THR TRP
SEQRES 8 B 216 ALA ALA SER LEU THR SER ALA ARG VAL PHE GLY THR GLY
SEQRES 9 B 216 THR LYS VAL ILE VAL SER GLY GLN PRO LYS ALA ASN PRO
SEQRES 10 B 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 B 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 B 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 B 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 B 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 B 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 B 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 B 216 THR VAL ALA PRO THR GLU CYS SER
SEQRES 1 A 256 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 A 256 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLN
SEQRES 3 A 256 PHE SER PHE ASN ARG TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 A 256 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER
SEQRES 5 A 256 TYR ASP GLY THR ASP LYS TYR HIS ALA ASP LYS VAL TRP
SEQRES 6 A 256 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 A 256 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 A 256 ALA LEU TYR TYR CYS ALA LYS ASP LEU ARG GLU ASP GLU
SEQRES 9 A 256 CYS GLU GLU TRP TRP SER ASP TYS TYS ASP PHE GLY LYS
SEQRES 10 A 256 GLN LEU PRO CYS ARG LYS SER ARG GLY VAL ALA GLY ILE
SEQRES 11 A 256 PHE ASP LYS TRP GLY GLN GLY THR MET VAL ILE VAL SER
SEQRES 12 A 256 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA
SEQRES 13 A 256 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 14 A 256 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 15 A 256 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 16 A 256 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 17 A 256 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 18 A 256 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 19 A 256 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS
SEQRES 20 A 256 ASP LYS GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 D 216 PRO VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA PRO
SEQRES 2 D 216 GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER SER
SEQRES 3 D 216 ASN ILE GLY ASN ASN PHE VAL SER TRP TYR GLN GLN ARG
SEQRES 4 D 216 PRO GLY THR ALA PRO SER LEU LEU ILE TYR GLU THR ASN
SEQRES 5 D 216 LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER
SEQRES 6 D 216 LYS SER ALA THR SER ALA THR LEU ALA ILE THR GLY LEU
SEQRES 7 D 216 GLN THR GLY ASP GLU ALA ASP TYR TYR CYS ALA THR TRP
SEQRES 8 D 216 ALA ALA SER LEU THR SER ALA ARG VAL PHE GLY THR GLY
SEQRES 9 D 216 THR LYS VAL ILE VAL SER GLY GLN PRO LYS ALA ASN PRO
SEQRES 10 D 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 D 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 D 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 D 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 D 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 D 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 D 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 D 216 THR VAL ALA PRO THR GLU CYS SER
SEQRES 1 C 256 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 C 256 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLN
SEQRES 3 C 256 PHE SER PHE ASN ARG TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 C 256 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER
SEQRES 5 C 256 TYR ASP GLY THR ASP LYS TYR HIS ALA ASP LYS VAL TRP
SEQRES 6 C 256 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 C 256 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 C 256 ALA LEU TYR TYR CYS ALA LYS ASP LEU ARG GLU ASP GLU
SEQRES 9 C 256 CYS GLU GLU TRP TRP SER ASP TYS TYS ASP PHE GLY LYS
SEQRES 10 C 256 GLN LEU PRO CYS ARG LYS SER ARG GLY VAL ALA GLY ILE
SEQRES 11 C 256 PHE ASP LYS TRP GLY GLN GLY THR MET VAL ILE VAL SER
SEQRES 12 C 256 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA
SEQRES 13 C 256 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 14 C 256 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 15 C 256 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 16 C 256 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 17 C 256 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 18 C 256 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 19 C 256 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS
SEQRES 20 C 256 ASP LYS GLY LEU GLU VAL LEU PHE GLN
SEQRES 1 F 216 PRO VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA PRO
SEQRES 2 F 216 GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER SER
SEQRES 3 F 216 ASN ILE GLY ASN ASN PHE VAL SER TRP TYR GLN GLN ARG
SEQRES 4 F 216 PRO GLY THR ALA PRO SER LEU LEU ILE TYR GLU THR ASN
SEQRES 5 F 216 LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER
SEQRES 6 F 216 LYS SER ALA THR SER ALA THR LEU ALA ILE THR GLY LEU
SEQRES 7 F 216 GLN THR GLY ASP GLU ALA ASP TYR TYR CYS ALA THR TRP
SEQRES 8 F 216 ALA ALA SER LEU THR SER ALA ARG VAL PHE GLY THR GLY
SEQRES 9 F 216 THR LYS VAL ILE VAL SER GLY GLN PRO LYS ALA ASN PRO
SEQRES 10 F 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 F 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 F 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 F 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 F 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 F 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 F 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 F 216 THR VAL ALA PRO THR GLU CYS SER
SEQRES 1 E 256 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 E 256 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLN
SEQRES 3 E 256 PHE SER PHE ASN ARG TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 E 256 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER
SEQRES 5 E 256 TYR ASP GLY THR ASP LYS TYR HIS ALA ASP LYS VAL TRP
SEQRES 6 E 256 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 E 256 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 E 256 ALA LEU TYR TYR CYS ALA LYS ASP LEU ARG GLU ASP GLU
SEQRES 9 E 256 CYS GLU GLU TRP TRP SER ASP TYS TYS ASP PHE GLY LYS
SEQRES 10 E 256 GLN LEU PRO CYS ARG LYS SER ARG GLY VAL ALA GLY ILE
SEQRES 11 E 256 PHE ASP LYS TRP GLY GLN GLY THR MET VAL ILE VAL SER
SEQRES 12 E 256 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA
SEQRES 13 E 256 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 14 E 256 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 15 E 256 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 16 E 256 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 17 E 256 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 18 E 256 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 19 E 256 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS
SEQRES 20 E 256 ASP LYS GLY LEU GLU VAL LEU PHE GLN
MODRES 4ORG TYS H 100H TYR O-SULFO-L-TYROSINE
MODRES 4ORG TYS H 100I TYR O-SULFO-L-TYROSINE
MODRES 4ORG TYS C 100H TYR O-SULFO-L-TYROSINE
MODRES 4ORG TYS C 100I TYR O-SULFO-L-TYROSINE
MODRES 4ORG TYS E 100H TYR O-SULFO-L-TYROSINE
HET TYS H 100H 7
HET TYS H 100I 7
HET TYS C 100H 7
HET TYS C 100I 7
HET TYS E 100H 24
HETNAM TYS O-SULFO-L-TYROSINE
FORMUL 2 TYS 5(C9 H11 N O6 S)
HELIX 1 1 SER L 26 ILE L 28 5 5
HELIX 2 2 SER L 121 ALA L 127 1 7
HELIX 3 3 THR L 181 LYS L 186 1 6
HELIX 4 4 SER H 28 ASN H 30 5 3
HELIX 5 5 ASP H 61 TRP H 64 5 4
HELIX 6 6 ARG H 83 THR H 87 5 5
HELIX 7 7 PRO H 185 LEU H 189 5 5
HELIX 8 8 LYS H 201 ASN H 204 5 4
HELIX 9 9 SER B 26 ILE B 28 5 5
HELIX 10 10 SER B 121 GLN B 126 1 6
HELIX 11 11 THR B 181 LYS B 186 1 6
HELIX 12 12 SER A 28 ASN A 30 5 3
HELIX 13 13 ASP A 61 TRP A 64 5 4
HELIX 14 14 PRO A 185 LEU A 189 5 5
HELIX 15 15 LYS A 201 ASN A 204 5 4
HELIX 16 16 SER D 27 ASN D 30 1 6
HELIX 17 17 GLN D 79 GLU D 83 5 5
HELIX 18 18 SER D 121 GLN D 126 1 6
HELIX 19 19 THR D 181 HIS D 188 1 8
HELIX 20 20 SER C 28 TYR C 32 5 5
HELIX 21 21 ARG C 83 THR C 87 5 5
HELIX 22 22 SER C 187 LEU C 189 5 3
HELIX 23 23 LYS C 201 ASN C 204 5 4
HELIX 24 24 SER F 27 ASN F 30 1 6
HELIX 25 25 GLN F 79 GLU F 83 5 5
HELIX 26 26 SER F 121 ALA F 127 1 7
HELIX 27 27 THR F 181 LYS F 186 1 6
HELIX 28 28 SER E 28 TYR E 32 5 5
HELIX 29 29 ARG E 83 THR E 87 5 5
HELIX 30 30 PRO E 185 LEU E 189 5 5
HELIX 31 31 LYS E 201 ASN E 204 5 4
SHEET 1 A 5 SER L 9 ALA L 13 0
SHEET 2 A 5 LYS L 103 VAL L 106 1 O LYS L 103 N VAL L 11
SHEET 3 A 5 ALA L 84 ALA L 89 -1 N ALA L 84 O VAL L 104
SHEET 4 A 5 SER L 34 GLN L 38 -1 N SER L 34 O ALA L 89
SHEET 5 A 5 SER L 45 ILE L 48 -1 O ILE L 48 N TRP L 35
SHEET 1 B 2 VAL L 19 SER L 24 0
SHEET 2 B 2 SER L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 1 C 4 THR L 114 PHE L 118 0
SHEET 2 C 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116
SHEET 3 C 4 TYR L 172 LEU L 180 -1 O TYR L 172 N PHE L 139
SHEET 4 C 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177
SHEET 1 D 4 THR L 114 PHE L 118 0
SHEET 2 D 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116
SHEET 3 D 4 TYR L 172 LEU L 180 -1 O TYR L 172 N PHE L 139
SHEET 4 D 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173
SHEET 1 E 4 SER L 153 PRO L 154 0
SHEET 2 E 4 VAL L 146 ALA L 150 -1 N ALA L 150 O SER L 153
SHEET 3 E 4 TYR L 191 THR L 196 -1 O GLN L 194 N ALA L 147
SHEET 4 E 4 THR L 201 VAL L 206 -1 O LYS L 204 N CYS L 193
SHEET 1 F 4 GLN H 3 SER H 7 0
SHEET 2 F 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7
SHEET 3 F 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18
SHEET 4 F 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 G 6 GLY H 10 VAL H 11 0
SHEET 2 G 6 THR H 107 ILE H 110 1 O ILE H 110 N GLY H 10
SHEET 3 G 6 ALA H 88 GLU H 98 -1 N TYR H 90 O THR H 107
SHEET 4 G 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 G 6 GLU H 46 ILE H 51 -1 O VAL H 48 N TRP H 36
SHEET 6 G 6 LYS H 57 HIS H 59 -1 O TYR H 58 N ALA H 50
SHEET 1 H 4 GLY H 10 VAL H 11 0
SHEET 2 H 4 THR H 107 ILE H 110 1 O ILE H 110 N GLY H 10
SHEET 3 H 4 ALA H 88 GLU H 98 -1 N TYR H 90 O THR H 107
SHEET 4 H 4 PHE H 101 TRP H 103 -1 O LYS H 102 N LYS H 94
SHEET 1 I 4 SER H 120 PHE H 122 0
SHEET 2 I 4 ALA H 137 TYR H 145 -1 O LYS H 143 N SER H 120
SHEET 3 I 4 TYR H 176 THR H 183 -1 O VAL H 182 N LEU H 138
SHEET 4 I 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 J 3 THR H 151 TRP H 154 0
SHEET 2 J 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 J 3 THR H 205 VAL H 211 -1 O LYS H 209 N CYS H 196
SHEET 1 K 5 SER B 9 ALA B 13 0
SHEET 2 K 5 THR B 102 VAL B 106 1 O ILE B 105 N VAL B 11
SHEET 3 K 5 ALA B 84 ALA B 89 -1 N TYR B 86 O THR B 102
SHEET 4 K 5 SER B 34 GLN B 38 -1 N GLN B 38 O ASP B 85
SHEET 5 K 5 SER B 45 ILE B 48 -1 O LEU B 47 N TRP B 35
SHEET 1 L 3 VAL B 19 SER B 22 0
SHEET 2 L 3 THR B 72 ILE B 75 -1 O LEU B 73 N ILE B 21
SHEET 3 L 3 PHE B 62 GLY B 64 -1 N SER B 63 O ALA B 74
SHEET 1 M 4 THR B 116 PHE B 118 0
SHEET 2 M 4 ALA B 130 PHE B 139 -1 O LEU B 135 N THR B 116
SHEET 3 M 4 TYR B 172 LEU B 180 -1 O TYR B 172 N PHE B 139
SHEET 4 M 4 VAL B 159 THR B 161 -1 N GLU B 160 O TYR B 177
SHEET 1 N 4 THR B 116 PHE B 118 0
SHEET 2 N 4 ALA B 130 PHE B 139 -1 O LEU B 135 N THR B 116
SHEET 3 N 4 TYR B 172 LEU B 180 -1 O TYR B 172 N PHE B 139
SHEET 4 N 4 SER B 165 LYS B 166 -1 N SER B 165 O ALA B 173
SHEET 1 O 4 SER B 153 VAL B 155 0
SHEET 2 O 4 THR B 145 ALA B 150 -1 N ALA B 150 O SER B 153
SHEET 3 O 4 TYR B 191 HIS B 197 -1 O SER B 192 N LYS B 149
SHEET 4 O 4 SER B 200 VAL B 206 -1 O LYS B 204 N CYS B 193
SHEET 1 P 4 GLN A 3 SER A 7 0
SHEET 2 P 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5
SHEET 3 P 4 THR A 77 MET A 82 -1 O LEU A 78 N CYS A 22
SHEET 4 P 4 PHE A 67 ASP A 72 -1 N SER A 70 O TYR A 79
SHEET 1 Q 6 GLY A 10 VAL A 12 0
SHEET 2 Q 6 THR A 107 VAL A 111 1 O ILE A 110 N VAL A 12
SHEET 3 Q 6 ALA A 88 GLU A 98 -1 N ALA A 88 O VAL A 109
SHEET 4 Q 6 TYR A 32 GLN A 39 -1 N VAL A 37 O TYR A 91
SHEET 5 Q 6 LEU A 45 ILE A 51 -1 O VAL A 48 N TRP A 36
SHEET 6 Q 6 LYS A 57 HIS A 59 -1 O TYR A 58 N ALA A 50
SHEET 1 R 4 GLY A 10 VAL A 12 0
SHEET 2 R 4 THR A 107 VAL A 111 1 O ILE A 110 N VAL A 12
SHEET 3 R 4 ALA A 88 GLU A 98 -1 N ALA A 88 O VAL A 109
SHEET 4 R 4 PHE A 101 TRP A 103 -1 O LYS A 102 N LYS A 94
SHEET 1 S 4 SER A 120 SER A 127 0
SHEET 2 S 4 ALA A 137 TYR A 145 -1 O GLY A 139 N LEU A 124
SHEET 3 S 4 TYR A 176 VAL A 182 -1 O VAL A 182 N LEU A 138
SHEET 4 S 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181
SHEET 1 T 4 SER A 120 SER A 127 0
SHEET 2 T 4 ALA A 137 TYR A 145 -1 O GLY A 139 N LEU A 124
SHEET 3 T 4 TYR A 176 VAL A 182 -1 O VAL A 182 N LEU A 138
SHEET 4 T 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177
SHEET 1 U 2 TYR A 194 HIS A 200 0
SHEET 2 U 2 THR A 205 VAL A 211 -1 O VAL A 207 N VAL A 198
SHEET 1 V 5 SER D 9 ALA D 13 0
SHEET 2 V 5 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11
SHEET 3 V 5 ASP D 85 ALA D 89 -1 N TYR D 86 O THR D 102
SHEET 4 V 5 SER D 34 GLN D 38 -1 N GLN D 38 O ASP D 85
SHEET 5 V 5 LEU D 46 ILE D 48 -1 O LEU D 47 N TRP D 35
SHEET 1 W 3 LYS D 18 SER D 24 0
SHEET 2 W 3 SER D 70 THR D 76 -1 O LEU D 73 N ILE D 21
SHEET 3 W 3 PHE D 62 GLY D 64 -1 N SER D 63 O ALA D 74
SHEET 1 X 4 THR D 114 PHE D 118 0
SHEET 2 X 4 ALA D 130 PHE D 139 -1 O LEU D 135 N THR D 116
SHEET 3 X 4 TYR D 172 LEU D 180 -1 O ALA D 174 N ILE D 136
SHEET 4 X 4 VAL D 159 THR D 161 -1 N GLU D 160 O TYR D 177
SHEET 1 Y 4 THR D 114 PHE D 118 0
SHEET 2 Y 4 ALA D 130 PHE D 139 -1 O LEU D 135 N THR D 116
SHEET 3 Y 4 TYR D 172 LEU D 180 -1 O ALA D 174 N ILE D 136
SHEET 4 Y 4 SER D 165 LYS D 166 -1 N SER D 165 O ALA D 173
SHEET 1 Z 4 SER D 153 PRO D 154 0
SHEET 2 Z 4 THR D 145 ALA D 150 -1 N ALA D 150 O SER D 153
SHEET 3 Z 4 TYR D 191 HIS D 197 -1 O SER D 192 N LYS D 149
SHEET 4 Z 4 SER D 200 VAL D 206 -1 O LYS D 204 N CYS D 193
SHEET 1 AA 4 GLN C 3 SER C 7 0
SHEET 2 AA 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5
SHEET 3 AA 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18
SHEET 4 AA 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79
SHEET 1 AB 5 LYS C 57 HIS C 59 0
SHEET 2 AB 5 GLU C 46 ILE C 51 -1 N ALA C 50 O TYR C 58
SHEET 3 AB 5 MET C 34 GLN C 39 -1 N MET C 34 O ILE C 51
SHEET 4 AB 5 ALA C 88 ASP C 95 -1 O TYR C 91 N VAL C 37
SHEET 5 AB 5 PHE C 101 TRP C 103 -1 O LYS C 102 N LYS C 94
SHEET 1 AC 5 LYS C 57 HIS C 59 0
SHEET 2 AC 5 GLU C 46 ILE C 51 -1 N ALA C 50 O TYR C 58
SHEET 3 AC 5 MET C 34 GLN C 39 -1 N MET C 34 O ILE C 51
SHEET 4 AC 5 ALA C 88 ASP C 95 -1 O TYR C 91 N VAL C 37
SHEET 5 AC 5 THR C 107 VAL C 109 -1 O VAL C 109 N ALA C 88
SHEET 1 AD 4 VAL C 121 LEU C 124 0
SHEET 2 AD 4 THR C 135 VAL C 142 -1 O GLY C 139 N LEU C 124
SHEET 3 AD 4 SER C 179 PRO C 185 -1 O VAL C 182 N LEU C 138
SHEET 4 AD 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181
SHEET 1 AE 2 TYR C 194 HIS C 200 0
SHEET 2 AE 2 THR C 205 VAL C 211 -1 O THR C 205 N HIS C 200
SHEET 1 AF 2 SER F 9 ALA F 13 0
SHEET 2 AF 2 LYS F 103 VAL F 106 1 O LYS F 103 N VAL F 11
SHEET 1 AG 3 VAL F 19 SER F 22 0
SHEET 2 AG 3 THR F 72 ILE F 75 -1 O LEU F 73 N ILE F 21
SHEET 3 AG 3 PHE F 62 GLY F 64 -1 N SER F 63 O ALA F 74
SHEET 1 AH 3 PRO F 44 ILE F 48 0
SHEET 2 AH 3 SER F 34 GLN F 38 -1 N GLN F 37 O SER F 45
SHEET 3 AH 3 ASP F 85 ALA F 89 -1 O ASP F 85 N GLN F 38
SHEET 1 AI 4 THR F 114 PHE F 118 0
SHEET 2 AI 4 ALA F 130 PHE F 139 -1 O VAL F 133 N PHE F 118
SHEET 3 AI 4 TYR F 172 LEU F 180 -1 O TYR F 172 N PHE F 139
SHEET 4 AI 4 VAL F 159 THR F 161 -1 N GLU F 160 O TYR F 177
SHEET 1 AJ 4 THR F 114 PHE F 118 0
SHEET 2 AJ 4 ALA F 130 PHE F 139 -1 O VAL F 133 N PHE F 118
SHEET 3 AJ 4 TYR F 172 LEU F 180 -1 O TYR F 172 N PHE F 139
SHEET 4 AJ 4 SER F 165 LYS F 166 -1 N SER F 165 O ALA F 173
SHEET 1 AK 4 SER F 153 VAL F 155 0
SHEET 2 AK 4 THR F 145 ALA F 150 -1 N TRP F 148 O VAL F 155
SHEET 3 AK 4 TYR F 191 HIS F 197 -1 O GLN F 194 N ALA F 147
SHEET 4 AK 4 SER F 200 VAL F 206 -1 O SER F 200 N HIS F 197
SHEET 1 AL 4 GLN E 3 SER E 7 0
SHEET 2 AL 4 SER E 17 SER E 25 -1 O ALA E 23 N VAL E 5
SHEET 3 AL 4 THR E 77 ASN E 82A-1 O MET E 82 N LEU E 18
SHEET 4 AL 4 THR E 68 ASP E 72 -1 N SER E 70 O TYR E 79
SHEET 1 AM 5 LYS E 57 HIS E 59 0
SHEET 2 AM 5 GLU E 46 ILE E 51 -1 N ALA E 50 O TYR E 58
SHEET 3 AM 5 MET E 34 GLN E 39 -1 N TRP E 36 O VAL E 48
SHEET 4 AM 5 ALA E 88 ASP E 95 -1 O TYR E 91 N VAL E 37
SHEET 5 AM 5 PHE E 101 TRP E 103 -1 O LYS E 102 N LYS E 94
SHEET 1 AN 5 LYS E 57 HIS E 59 0
SHEET 2 AN 5 GLU E 46 ILE E 51 -1 N ALA E 50 O TYR E 58
SHEET 3 AN 5 MET E 34 GLN E 39 -1 N TRP E 36 O VAL E 48
SHEET 4 AN 5 ALA E 88 ASP E 95 -1 O TYR E 91 N VAL E 37
SHEET 5 AN 5 THR E 107 VAL E 109 -1 O VAL E 109 N ALA E 88
SHEET 1 AO 2 CYS E 100A TRP E 100D 0
SHEET 2 AO 2 CYS E 100Q SER E 100T-1 O ARG E 100R N GLU E 100C
SHEET 1 AP 4 SER E 120 LEU E 124 0
SHEET 2 AP 4 LEU E 138 TYR E 145 -1 O LEU E 141 N PHE E 122
SHEET 3 AP 4 TYR E 176 VAL E 182 -1 O VAL E 182 N LEU E 138
SHEET 4 AP 4 VAL E 163 LEU E 170 -1 N HIS E 164 O VAL E 181
SHEET 1 AQ 3 THR E 151 TRP E 154 0
SHEET 2 AQ 3 TYR E 194 HIS E 200 -1 O ASN E 197 N SER E 153
SHEET 3 AQ 3 THR E 205 VAL E 211 -1 O VAL E 211 N TYR E 194
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 2 CYS L 134 CYS L 193 1555 1555 2.03
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 4 CYS H 100A CYS H 100Q 1555 1555 2.04
SSBOND 5 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 6 CYS B 23 CYS B 88 1555 1555 2.03
SSBOND 7 CYS B 134 CYS B 193 1555 1555 2.03
SSBOND 8 CYS A 22 CYS A 92 1555 1555 2.03
SSBOND 9 CYS A 100A CYS A 100Q 1555 1555 2.03
SSBOND 10 CYS A 140 CYS A 196 1555 1555 2.03
SSBOND 11 CYS D 23 CYS D 88 1555 1555 2.03
SSBOND 12 CYS D 134 CYS D 193 1555 1555 2.03
SSBOND 13 CYS C 22 CYS C 92 1555 1555 2.03
SSBOND 14 CYS C 100A CYS C 100Q 1555 1555 2.03
SSBOND 15 CYS C 140 CYS C 196 1555 1555 2.03
SSBOND 16 CYS F 23 CYS F 88 1555 1555 2.03
SSBOND 17 CYS F 134 CYS F 193 1555 1555 2.03
SSBOND 18 CYS E 22 CYS E 92 1555 1555 2.03
SSBOND 19 CYS E 100A CYS E 100Q 1555 1555 2.04
SSBOND 20 CYS E 140 CYS E 196 1555 1555 2.03
LINK C ASP H 100G N TYS H 100H 1555 1555 1.33
LINK C TYS H 100H N TYS H 100I 1555 1555 1.33
LINK C TYS H 100I N ASP H 100J 1555 1555 1.33
LINK C ASP C 100G N TYS C 100H 1555 1555 1.33
LINK C TYS C 100H N TYS C 100I 1555 1555 1.33
LINK C ASP E 100G N TYS E 100H 1555 1555 1.33
CISPEP 1 ALA L 92 ALA L 93 0 2.87
CISPEP 2 ALA L 93 SER L 94 0 1.15
CISPEP 3 TYR L 140 PRO L 141 0 4.59
CISPEP 4 PRO H 41 GLY H 42 0 -2.51
CISPEP 5 TYS H 100H TYS H 100I 0 3.69
CISPEP 6 PHE H 100K GLY H 100L 0 -7.24
CISPEP 7 LYS H 100M GLN H 100N 0 -2.91
CISPEP 8 THR H 135 ALA H 136 0 3.49
CISPEP 9 PHE H 146 PRO H 147 0 -9.66
CISPEP 10 GLU H 148 PRO H 149 0 2.49
CISPEP 11 THR B 100 GLY B 101 0 -1.67
CISPEP 12 TYR B 140 PRO B 141 0 5.06
CISPEP 13 PRO A 41 GLY A 42 0 -1.03
CISPEP 14 ALA A 125 PRO A 126 0 -19.86
CISPEP 15 PHE A 146 PRO A 147 0 -2.47
CISPEP 16 GLU A 148 PRO A 149 0 2.42
CISPEP 17 SER A 161 GLY A 162 0 1.41
CISPEP 18 THR D 100 GLY D 101 0 -3.24
CISPEP 19 TYR D 140 PRO D 141 0 0.91
CISPEP 20 PRO C 41 GLY C 42 0 -3.45
CISPEP 21 PHE C 146 PRO C 147 0 -11.01
CISPEP 22 GLU C 148 PRO C 149 0 1.61
CISPEP 23 TYR F 140 PRO F 141 0 1.35
CISPEP 24 PRO E 41 GLY E 42 0 -2.45
CISPEP 25 ALA E 125 PRO E 126 0 -17.04
CISPEP 26 PHE E 146 PRO E 147 0 -7.55
CISPEP 27 GLU E 148 PRO E 149 0 0.25
CRYST1 68.023 85.471 103.274 97.90 107.72 91.67 P 1 4
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 0.014701 0.000429 0.004822 0.00000
SCALE2 0.000000 0.011705 0.001820 0.00000
SCALE3 0.000000 0.000000 0.010288 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
