HEADER IMMUNE SYSTEM 26-SEP-19 6UGW
TITLE CRYSTAL STRUCTURE OF THE FC FRAGMENT OF PF06438179/GP1111 AN
TITLE 2 INFLIXIMAB BIOSIMILAR IN A C-CENTERED ORTHORHOMBIC CRYSTAL FORM, LOT
TITLE 3 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PF-06438179/GP1111 FC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LOTA_FC;
COMPND 5 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: MUS MUSCULUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: MOUSE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10090
KEYWDS ANTIBODY, BIOLOGIC, BIOSIMILAR, INFLIXIMAB, FRAGMENT CRYSTALLIZABLE,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.MAYCLIN,T.E.EDWARDS
REVDAT 4 11-OCT-23 6UGW 1 HETSYN LINK
REVDAT 3 29-JUL-20 6UGW 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 12-FEB-20 6UGW 1 JRNL
REVDAT 1 13-NOV-19 6UGW 0
JRNL AUTH T.F.LERCH,P.SHARPE,S.J.MAYCLIN,T.E.EDWARDS,S.POLLECK,
JRNL AUTH 2 J.C.ROUSE,Q.ZOU,H.D.CONLON
JRNL TITL CRYSTAL STRUCTURES OF PF-06438179/GP1111, AN INFLIXIMAB
JRNL TITL 2 BIOSIMILAR.
JRNL REF BIODRUGS V. 34 77 2020
JRNL REFN ISSN 1179-190X
JRNL PMID 31650490
JRNL DOI 10.1007/S40259-019-00390-1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 972
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 50.0000 - 3.8244 0.99 2765 145 0.1586 0.1938
REMARK 3 2 3.8244 - 3.0361 1.00 2651 140 0.1826 0.2140
REMARK 3 3 3.0361 - 2.6524 1.00 2635 139 0.1942 0.2289
REMARK 3 4 2.6524 - 2.4100 1.00 2621 137 0.1930 0.2317
REMARK 3 5 2.4100 - 2.2373 1.00 2619 137 0.1939 0.2352
REMARK 3 6 2.2373 - 2.1054 1.00 2597 137 0.1965 0.2389
REMARK 3 7 2.1054 - 2.0000 1.00 2590 137 0.2110 0.2802
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.26
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 : 0.007 1771
REMARK 3 ANGLE : 0.891 2431
REMARK 3 CHIRALITY : 0.054 294
REMARK 3 PLANARITY : 0.005 299
REMARK 3 DIHEDRAL : 15.163 1069
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 240 THROUGH 267 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5205 17.2204 -5.4923
REMARK 3 T TENSOR
REMARK 3 T11: 0.3314 T22: 0.4151
REMARK 3 T33: 0.4484 T12: -0.0100
REMARK 3 T13: -0.0700 T23: -0.2277
REMARK 3 L TENSOR
REMARK 3 L11: 0.2469 L22: 4.8424
REMARK 3 L33: 1.3479 L12: 0.9649
REMARK 3 L13: 0.0994 L23: -0.3764
REMARK 3 S TENSOR
REMARK 3 S11: 0.1455 S12: -0.7251 S13: 0.5836
REMARK 3 S21: 0.7097 S22: -0.1529 S23: -0.2441
REMARK 3 S31: -0.2504 S32: 0.0925 S33: 0.0016
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 268 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5314 32.0399 -2.4616
REMARK 3 T TENSOR
REMARK 3 T11: 0.5449 T22: 0.2257
REMARK 3 T33: 0.9853 T12: -0.0943
REMARK 3 T13: -0.1143 T23: -0.6944
REMARK 3 L TENSOR
REMARK 3 L11: 0.6452 L22: 0.5259
REMARK 3 L33: 0.3007 L12: 0.5949
REMARK 3 L13: 0.4418 L23: 0.3974
REMARK 3 S TENSOR
REMARK 3 S11: 0.1094 S12: -0.3011 S13: 0.7715
REMARK 3 S21: 0.2806 S22: 0.1490 S23: -0.2590
REMARK 3 S31: -0.5484 S32: 0.0483 S33: 0.6230
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 305 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5756 15.8775 -4.6525
REMARK 3 T TENSOR
REMARK 3 T11: 0.2871 T22: 0.3443
REMARK 3 T33: 0.3420 T12: 0.0154
REMARK 3 T13: -0.0292 T23: -0.2054
REMARK 3 L TENSOR
REMARK 3 L11: 1.6184 L22: 0.5182
REMARK 3 L33: 1.9737 L12: 0.8453
REMARK 3 L13: 0.4173 L23: 0.5692
REMARK 3 S TENSOR
REMARK 3 S11: 0.0807 S12: -0.5642 S13: 0.8605
REMARK 3 S21: 0.3975 S22: -0.0576 S23: -0.0135
REMARK 3 S31: -0.1520 S32: -0.1026 S33: 0.1992
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1949 28.6211 -11.5912
REMARK 3 T TENSOR
REMARK 3 T11: 0.4952 T22: 0.2643
REMARK 3 T33: 0.8614 T12: 0.0255
REMARK 3 T13: -0.0339 T23: -0.1364
REMARK 3 L TENSOR
REMARK 3 L11: 0.5244 L22: 4.6474
REMARK 3 L33: 1.7266 L12: 1.5076
REMARK 3 L13: 0.0334 L23: 0.7863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: -0.0883 S13: 1.2817
REMARK 3 S21: -0.2340 S22: 0.1188 S23: 0.1079
REMARK 3 S31: -0.8031 S32: -0.0872 S33: 0.1495
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 340 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1925 -6.2366 -16.5769
REMARK 3 T TENSOR
REMARK 3 T11: 0.1841 T22: 0.2074
REMARK 3 T33: 0.3008 T12: -0.0012
REMARK 3 T13: 0.0008 T23: 0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 6.5581 L22: 2.9476
REMARK 3 L33: 1.2460 L12: -2.5331
REMARK 3 L13: 0.8255 L23: -0.4828
REMARK 3 S TENSOR
REMARK 3 S11: 0.1727 S12: -0.0096 S13: -0.8227
REMARK 3 S21: -0.1571 S22: -0.2215 S23: -0.2584
REMARK 3 S31: 0.2085 S32: 0.1083 S33: -0.0168
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6275 -4.0111 -11.2895
REMARK 3 T TENSOR
REMARK 3 T11: 0.2028 T22: 0.4509
REMARK 3 T33: 0.2206 T12: 0.0205
REMARK 3 T13: -0.0136 T23: 0.1667
REMARK 3 L TENSOR
REMARK 3 L11: 1.4869 L22: 1.7375
REMARK 3 L33: 2.6613 L12: 0.3277
REMARK 3 L13: -0.3432 L23: 0.0953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0381 S12: -0.7159 S13: -0.8285
REMARK 3 S21: 0.1946 S22: -0.0158 S23: -0.0688
REMARK 3 S31: 0.0375 S32: 0.0930 S33: -0.0149
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 446 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8393 -8.5087 -8.1238
REMARK 3 T TENSOR
REMARK 3 T11: 0.3156 T22: 0.4148
REMARK 3 T33: 0.3952 T12: 0.0272
REMARK 3 T13: 0.0071 T23: 0.2571
REMARK 3 L TENSOR
REMARK 3 L11: 3.3058 L22: 1.1128
REMARK 3 L33: 1.0918 L12: -1.1801
REMARK 3 L13: 0.9491 L23: -0.5912
REMARK 3 S TENSOR
REMARK 3 S11: -0.2051 S12: -0.8510 S13: -1.0090
REMARK 3 S21: 0.1315 S22: -0.2951 S23: -0.3449
REMARK 3 S31: 0.1426 S32: 0.2943 S33: -0.0720
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 6UGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1000244505.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19460
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.103
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.18
REMARK 200 R MERGE FOR SHELL (I) : 0.49700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.690
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 4CDH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PROTEIN WITH JCSG+ E7
REMARK 280 (266849E7): 10% 2-PROPANOL, 200 MM ZINC ACETATE, 100 MM SODIUM
REMARK 280 CACODYLATE, PH 6.5, CRYOPROTECTANT: 20% ETHYLENE GLYCOL, PUCKID
REMARK 280 KUX1-2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.89500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.89500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.04500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.04500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.89500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.04500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 37.89500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.04500
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 BIOMT1 2 -1.000000 0.000000 0.000000 50.09000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -37.89500
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A 503 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 745 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 196
REMARK 465 LYS A 197
REMARK 465 LYS A 198
REMARK 465 THR A 199
REMARK 465 ALA A 200
REMARK 465 ILE A 201
REMARK 465 ALA A 202
REMARK 465 ILE A 203
REMARK 465 ALA A 204
REMARK 465 VAL A 205
REMARK 465 ALA A 206
REMARK 465 LEU A 207
REMARK 465 ALA A 208
REMARK 465 GLY A 209
REMARK 465 PHE A 210
REMARK 465 ALA A 211
REMARK 465 THR A 212
REMARK 465 VAL A 213
REMARK 465 ALA A 214
REMARK 465 GLN A 215
REMARK 465 ALA A 216
REMARK 465 ASP A 217
REMARK 465 VAL A 218
REMARK 465 GLU A 219
REMARK 465 SER A 220
REMARK 465 LYS A 221
REMARK 465 SER A 222
REMARK 465 CYS A 223
REMARK 465 ASP A 224
REMARK 465 LYS A 225
REMARK 465 THR A 226
REMARK 465 HIS A 227
REMARK 465 THR A 228
REMARK 465 CYS A 229
REMARK 465 PRO A 230
REMARK 465 PRO A 231
REMARK 465 CYS A 232
REMARK 465 PRO A 233
REMARK 465 ALA A 234
REMARK 465 PRO A 235
REMARK 465 GLU A 236
REMARK 465 LEU A 237
REMARK 465 LEU A 238
REMARK 465 GLY A 239
REMARK 465 SER A 447
REMARK 465 PRO A 448
REMARK 465 GLY A 449
REMARK 465 LYS A 450
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 LYS A 249 CG CD CE NZ
REMARK 470 GLU A 272 CG CD OE1 OE2
REMARK 470 GLU A 275 CG CD OE1 OE2
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 ARG A 295 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 ARG A 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 363 CG CD CE NZ
REMARK 470 ASN A 364 CG OD1 ND2
REMARK 470 LYS A 417 CG CD CE NZ
REMARK 470 GLN A 422 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O3 BMA B 3 O5 MAN B 7 1.47
REMARK 500 O6 NAG B 1 O5 FUC B 8 1.85
REMARK 500 O HOH A 641 O HOH A 734 2.06
REMARK 500 ND1 HIS A 436 O HOH A 601 2.11
REMARK 500 O3 GAL B 6 O HOH A 602 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 622 O HOH A 622 4555 2.06
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 A 751 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 752 DISTANCE = 7.31 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 313 NE2
REMARK 620 2 HIS A 438 NE2 110.8
REMARK 620 3 ACT A 504 O 119.4 88.6
REMARK 620 4 ACT A 504 OXT 101.1 142.7 58.2
REMARK 620 5 HOH A 641 O 115.2 103.9 114.2 78.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 321 OE1
REMARK 620 2 GLU A 321 OE2 55.3
REMARK 620 3 GLU A 321 OE1 0.0 55.3
REMARK 620 4 GLU A 321 OE2 55.3 0.0 55.3
REMARK 620 5 HOH A 692 O 133.1 80.2 133.1 80.2
REMARK 620 6 HOH A 692 O 81.7 133.6 81.7 133.6 131.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 649 O
REMARK 620 2 HOH A 736 O 144.8
REMARK 620 N 1
DBREF 6UGW A 196 220 PDB 6UGW 6UGW 196 220
DBREF 6UGW A 221 450 UNP P0DOX5 IGG1_HUMAN 220 449
SEQRES 1 A 255 MET LYS LYS THR ALA ILE ALA ILE ALA VAL ALA LEU ALA
SEQRES 2 A 255 GLY PHE ALA THR VAL ALA GLN ALA ASP VAL GLU SER LYS
SEQRES 3 A 255 SER CYS ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA
SEQRES 4 A 255 PRO GLU LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO
SEQRES 5 A 255 PRO LYS PRO LYS ASP THR LEU MET ILE SER ARG THR PRO
SEQRES 6 A 255 GLU VAL THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP
SEQRES 7 A 255 PRO GLU VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU
SEQRES 8 A 255 VAL HIS ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR
SEQRES 9 A 255 ASN SER THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU
SEQRES 10 A 255 HIS GLN ASP TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS
SEQRES 11 A 255 VAL SER ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR
SEQRES 12 A 255 ILE SER LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL
SEQRES 13 A 255 TYR THR LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN
SEQRES 14 A 255 GLN VAL SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO
SEQRES 15 A 255 SER ASP ILE ALA VAL GLU TRP GLU SER ASN GLY GLN PRO
SEQRES 16 A 255 GLU ASN ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER
SEQRES 17 A 255 ASP GLY SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP
SEQRES 18 A 255 LYS SER ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER
SEQRES 19 A 255 VAL MET HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS
SEQRES 20 A 255 SER LEU SER LEU SER PRO GLY LYS
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HET NAG B 5 14
HET GAL B 6 11
HET MAN B 7 11
HET FUC B 8 10
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET ACT A 504 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 2 GAL C6 H12 O6
FORMUL 2 FUC C6 H12 O5
FORMUL 3 ZN 3(ZN 2+)
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 HOH *152(H2 O)
HELIX 1 AA1 LYS A 249 MET A 255 1 7
HELIX 2 AA2 LEU A 312 ASN A 318 1 7
HELIX 3 AA3 SER A 357 LYS A 363 5 7
HELIX 4 AA4 LYS A 417 GLN A 422 1 6
HELIX 5 AA5 LEU A 435 ASN A 437 5 3
SHEET 1 AA1 4 SER A 242 PHE A 246 0
SHEET 2 AA1 4 GLU A 261 VAL A 269 -1 O VAL A 265 N PHE A 244
SHEET 3 AA1 4 TYR A 303 THR A 310 -1 O TYR A 303 N VAL A 269
SHEET 4 AA1 4 LYS A 291 THR A 292 -1 N LYS A 291 O VAL A 308
SHEET 1 AA2 4 SER A 242 PHE A 246 0
SHEET 2 AA2 4 GLU A 261 VAL A 269 -1 O VAL A 265 N PHE A 244
SHEET 3 AA2 4 TYR A 303 THR A 310 -1 O TYR A 303 N VAL A 269
SHEET 4 AA2 4 GLU A 296 GLU A 297 -1 N GLU A 296 O ARG A 304
SHEET 1 AA3 4 VAL A 285 VAL A 287 0
SHEET 2 AA3 4 LYS A 277 VAL A 282 -1 N VAL A 282 O VAL A 285
SHEET 3 AA3 4 TYR A 322 SER A 327 -1 O LYS A 325 N ASN A 279
SHEET 4 AA3 4 ILE A 335 ILE A 339 -1 O ILE A 335 N VAL A 326
SHEET 1 AA4 4 GLN A 350 LEU A 354 0
SHEET 2 AA4 4 GLN A 365 PHE A 375 -1 O LEU A 371 N TYR A 352
SHEET 3 AA4 4 PHE A 407 ASP A 416 -1 O LEU A 413 N LEU A 368
SHEET 4 AA4 4 TYR A 394 THR A 396 -1 N LYS A 395 O LYS A 412
SHEET 1 AA5 4 GLN A 350 LEU A 354 0
SHEET 2 AA5 4 GLN A 365 PHE A 375 -1 O LEU A 371 N TYR A 352
SHEET 3 AA5 4 PHE A 407 ASP A 416 -1 O LEU A 413 N LEU A 368
SHEET 4 AA5 4 VAL A 400 LEU A 401 -1 N VAL A 400 O PHE A 408
SHEET 1 AA6 4 GLN A 389 GLU A 391 0
SHEET 2 AA6 4 ALA A 381 SER A 386 -1 N SER A 386 O GLN A 389
SHEET 3 AA6 4 PHE A 426 MET A 431 -1 O SER A 429 N GLU A 383
SHEET 4 AA6 4 TYR A 439 LEU A 444 -1 O LYS A 442 N CYS A 428
SSBOND 1 CYS A 264 CYS A 324 1555 1555 2.06
SSBOND 2 CYS A 370 CYS A 428 1555 1555 2.04
LINK ND2 ASN A 300 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.46
LINK O6 NAG B 1 C1 FUC B 8 1555 1555 1.44
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.43
LINK O6 BMA B 3 C1 MAN B 4 1555 1555 1.44
LINK O3 BMA B 3 C1 MAN B 7 1555 1555 1.45
LINK O2 MAN B 4 C1 NAG B 5 1555 1555 1.43
LINK O4 NAG B 5 C1 GAL B 6 1555 1555 1.44
LINK NE2 HIS A 313 ZN ZN A 501 1555 1555 2.00
LINK OE1 GLU A 321 ZN ZN A 503 1555 1555 2.58
LINK OE2 GLU A 321 ZN ZN A 503 1555 1555 2.07
LINK OE1 GLU A 321 ZN ZN A 503 1555 3554 2.58
LINK OE2 GLU A 321 ZN ZN A 503 1555 3554 2.07
LINK NE2 HIS A 438 ZN ZN A 501 1555 1555 2.06
LINK ZN ZN A 501 O ACT A 504 1555 1555 2.04
LINK ZN ZN A 501 OXT ACT A 504 1555 1555 2.26
LINK ZN ZN A 501 O HOH A 641 1555 1555 1.98
LINK ZN ZN A 502 O HOH A 649 1555 1555 2.06
LINK ZN ZN A 502 O HOH A 736 1555 1555 2.16
LINK ZN ZN A 503 O HOH A 692 1555 1555 2.42
LINK ZN ZN A 503 O HOH A 692 1555 3554 2.43
CISPEP 1 TYR A 376 PRO A 377 0 0.45
CRYST1 50.090 148.090 75.790 90.00 90.00 90.00 C 2 2 21 8
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 0.019964 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006753 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
