HEADER CELL ADHESION 10-NOV-08 3F7Q
TITLE FIRST PAIR OF FIBRONECTIN TYPE III DOMAINS AND PART OF THE CONNECTING
TITLE 2 SEGMENT OF THE INTEGRIN BETA4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN BETA-4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FIBRONECTIN TYPE-III, RESIDUES 1126-1355;
COMPND 5 SYNONYM: GP150;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ITGB4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: DERIVATIVE OF PET15B
KEYWDS INTEGRIN, HEMIDESMOSOME, CELL ADHESION, CARCINOMA, EPIDERMOLYSIS
KEYWDS 2 BULLOSA, ALTERNATIVE SPLICING, DISEASE MUTATION, GLYCOPROTEIN,
KEYWDS 3 MEMBRANE, PHOSPHOPROTEIN, POLYMORPHISM, RECEPTOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.DE PEREDA
REVDAT 3 01-NOV-23 3F7Q 1 REMARK SEQADV
REVDAT 2 28-APR-09 3F7Q 1 JRNL
REVDAT 1 10-MAR-09 3F7Q 0
JRNL AUTH J.M.DE PEREDA,M.P.LILLO,A.SONNENBERG
JRNL TITL STRUCTURAL BASIS OF THE INTERACTION BETWEEN INTEGRIN
JRNL TITL 2 ALPHA6BETA4 AND PLECTIN AT THE HEMIDESMOSOMES
JRNL REF EMBO J. V. 28 1180 2009
JRNL REFN ISSN 0261-4189
JRNL PMID 19242489
JRNL DOI 10.1038/EMBOJ.2009.48
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.870
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 50835
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2589
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 22.2735 - 4.5738 0.95 2790 144 0.1547 0.1546
REMARK 3 2 4.5738 - 3.6355 0.96 2799 154 0.1316 0.1317
REMARK 3 3 3.6355 - 3.1774 0.95 2777 163 0.1395 0.1633
REMARK 3 4 3.1774 - 2.8876 0.95 2783 139 0.1434 0.2092
REMARK 3 5 2.8876 - 2.6810 0.94 2761 159 0.1433 0.1667
REMARK 3 6 2.6810 - 2.5231 0.94 2713 160 0.1381 0.1502
REMARK 3 7 2.5231 - 2.3969 0.94 2744 113 0.1327 0.1790
REMARK 3 8 2.3969 - 2.2927 0.93 2757 150 0.1341 0.1860
REMARK 3 9 2.2927 - 2.2045 0.90 2660 141 0.1379 0.1619
REMARK 3 10 2.2045 - 2.1285 0.92 2660 140 0.1392 0.1857
REMARK 3 11 2.1285 - 2.0620 0.90 2599 137 0.1499 0.1710
REMARK 3 12 2.0620 - 2.0031 0.91 2711 129 0.1557 0.1856
REMARK 3 13 2.0031 - 1.9504 0.90 2616 152 0.1643 0.2113
REMARK 3 14 1.9504 - 1.9028 0.89 2598 139 0.1804 0.2404
REMARK 3 15 1.9028 - 1.8596 0.90 2638 143 0.1991 0.2617
REMARK 3 16 1.8596 - 1.8200 0.90 2644 159 0.2048 0.2332
REMARK 3 17 1.8200 - 1.7836 0.89 2585 135 0.2231 0.2205
REMARK 3 18 1.7836 - 1.7500 0.82 2411 132 0.2548 0.3079
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 : 0.43
REMARK 3 B_SOL : 49.66
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.43820
REMARK 3 B22 (A**2) : -5.44840
REMARK 3 B33 (A**2) : -8.26380
REMARK 3 B12 (A**2) : 3.80150
REMARK 3 B13 (A**2) : -1.07710
REMARK 3 B23 (A**2) : 1.32350
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 : 0.005 6981
REMARK 3 ANGLE : 0.878 12628
REMARK 3 CHIRALITY : 0.068 513
REMARK 3 PLANARITY : 0.004 1111
REMARK 3 DIHEDRAL : 17.145 1804
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1126-1207
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2218 -3.8919 43.8523
REMARK 3 T TENSOR
REMARK 3 T11: 0.1365 T22: 0.1649
REMARK 3 T33: 0.1673 T12: -0.0237
REMARK 3 T13: -0.0013 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.2905 L22: 1.0082
REMARK 3 L33: 1.0326 L12: 0.0068
REMARK 3 L13: -0.3696 L23: -0.1755
REMARK 3 S TENSOR
REMARK 3 S11: 0.0549 S12: -0.0958 S13: -0.0195
REMARK 3 S21: -0.0137 S22: -0.0454 S23: -0.0801
REMARK 3 S31: -0.1011 S32: 0.1149 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1208-1229
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0968 -16.4944 26.9127
REMARK 3 T TENSOR
REMARK 3 T11: 0.2281 T22: 0.2171
REMARK 3 T33: 0.2233 T12: 0.0184
REMARK 3 T13: -0.0120 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: -0.1296 L22: 0.0795
REMARK 3 L33: 0.0652 L12: 0.0354
REMARK 3 L13: -0.2652 L23: 0.1980
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: 0.1117 S13: 0.0791
REMARK 3 S21: -0.0383 S22: 0.0436 S23: 0.0443
REMARK 3 S31: -0.0610 S32: 0.0046 S33: 0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1230-1254
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4776 -27.4318 14.2894
REMARK 3 T TENSOR
REMARK 3 T11: 0.1960 T22: 0.2021
REMARK 3 T33: 0.1753 T12: 0.0351
REMARK 3 T13: -0.0094 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.4463 L22: 0.1274
REMARK 3 L33: 0.5180 L12: -0.2367
REMARK 3 L13: -0.2710 L23: -0.2070
REMARK 3 S TENSOR
REMARK 3 S11: -0.0660 S12: -0.0465 S13: 0.0957
REMARK 3 S21: -0.0802 S22: 0.0432 S23: 0.0558
REMARK 3 S31: -0.2308 S32: -0.1585 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1255-1282
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3804 -36.3143 11.5727
REMARK 3 T TENSOR
REMARK 3 T11: 0.1877 T22: 0.1821
REMARK 3 T33: 0.1794 T12: 0.0197
REMARK 3 T13: -0.0088 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.4528 L22: 0.1905
REMARK 3 L33: 0.4050 L12: -0.4281
REMARK 3 L13: -0.2584 L23: 0.6791
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: 0.0210 S13: -0.1065
REMARK 3 S21: 0.1622 S22: 0.0671 S23: -0.1749
REMARK 3 S31: -0.0564 S32: 0.0445 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1283-1317
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2901 -37.1152 12.6306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1603 T22: 0.2075
REMARK 3 T33: 0.2109 T12: -0.0039
REMARK 3 T13: -0.0151 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.6008 L22: 0.3258
REMARK 3 L33: 0.1353 L12: -0.0093
REMARK 3 L13: -0.0424 L23: -0.3951
REMARK 3 S TENSOR
REMARK 3 S11: 0.0651 S12: -0.0016 S13: -0.1195
REMARK 3 S21: 0.0397 S22: 0.0989 S23: -0.0045
REMARK 3 S31: 0.0086 S32: -0.0890 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1318-1339
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2646 -32.6168 1.7199
REMARK 3 T TENSOR
REMARK 3 T11: 0.2470 T22: 0.2969
REMARK 3 T33: 0.2578 T12: -0.0250
REMARK 3 T13: -0.0207 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.2935 L22: 0.1402
REMARK 3 L33: -0.0825 L12: -0.0704
REMARK 3 L13: 0.3822 L23: 0.1168
REMARK 3 S TENSOR
REMARK 3 S11: -0.3178 S12: -0.0355 S13: 0.0698
REMARK 3 S21: 0.1187 S22: 0.2345 S23: -0.1283
REMARK 3 S31: -0.0919 S32: 0.0050 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND RESSEQ 1126-1163
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5622 -38.4006 28.4976
REMARK 3 T TENSOR
REMARK 3 T11: 0.1810 T22: 0.1664
REMARK 3 T33: 0.1773 T12: 0.0262
REMARK 3 T13: 0.0061 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.1664 L22: 0.3956
REMARK 3 L33: 0.5210 L12: -0.1687
REMARK 3 L13: 0.2619 L23: -0.5234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0431 S12: 0.0836 S13: 0.0342
REMARK 3 S21: 0.0245 S22: -0.0298 S23: -0.0894
REMARK 3 S31: 0.1120 S32: 0.0375 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND RESSEQ 1164-1215
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2193 -37.2544 30.9006
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.1600
REMARK 3 T33: 0.1595 T12: 0.0032
REMARK 3 T13: 0.0045 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: -0.0656 L22: 0.7308
REMARK 3 L33: 0.5114 L12: -0.2848
REMARK 3 L13: 0.0927 L23: 0.0170
REMARK 3 S TENSOR
REMARK 3 S11: 0.0614 S12: 0.0729 S13: 0.0165
REMARK 3 S21: 0.0516 S22: 0.0065 S23: 0.0023
REMARK 3 S31: 0.0667 S32: -0.1355 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND RESSEQ 1216-1249
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7599 -13.9738 55.6634
REMARK 3 T TENSOR
REMARK 3 T11: 0.1835 T22: 0.1915
REMARK 3 T33: 0.2050 T12: -0.0510
REMARK 3 T13: 0.0246 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.2710 L22: 0.1935
REMARK 3 L33: 0.5629 L12: -0.1537
REMARK 3 L13: 0.4433 L23: -0.2601
REMARK 3 S TENSOR
REMARK 3 S11: 0.0198 S12: 0.1458 S13: -0.0136
REMARK 3 S21: -0.0254 S22: 0.0112 S23: 0.0554
REMARK 3 S31: 0.1949 S32: -0.2238 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND RESSEQ 1250-1277
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3549 -4.5087 60.4161
REMARK 3 T TENSOR
REMARK 3 T11: 0.1878 T22: 0.1785
REMARK 3 T33: 0.1625 T12: -0.0147
REMARK 3 T13: -0.0116 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.1898 L22: 0.1382
REMARK 3 L33: 0.5624 L12: 0.1179
REMARK 3 L13: 0.0764 L23: 0.2807
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: -0.0386 S13: 0.0462
REMARK 3 S21: -0.2314 S22: 0.0300 S23: -0.1110
REMARK 3 S31: -0.0743 S32: -0.0288 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND RESSEQ 1278-1301
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8647 -6.0406 63.3346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1790 T22: 0.1795
REMARK 3 T33: 0.1752 T12: -0.0052
REMARK 3 T13: 0.0160 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.2503 L22: 0.1003
REMARK 3 L33: 0.4059 L12: 0.1777
REMARK 3 L13: -0.3265 L23: -0.3493
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: -0.0647 S13: 0.0418
REMARK 3 S21: 0.1403 S22: 0.1162 S23: 0.0073
REMARK 3 S31: 0.0373 S32: -0.0825 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND RESSEQ 1302-1339
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0904 -8.7685 64.3113
REMARK 3 T TENSOR
REMARK 3 T11: 0.1743 T22: 0.1941
REMARK 3 T33: 0.1964 T12: 0.0043
REMARK 3 T13: 0.0014 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.5510 L22: -0.0533
REMARK 3 L33: 0.0780 L12: -0.3855
REMARK 3 L13: -0.2026 L23: -0.1887
REMARK 3 S TENSOR
REMARK 3 S11: -0.0853 S12: -0.0440 S13: -0.0440
REMARK 3 S21: 0.0559 S22: 0.0842 S23: 0.0049
REMARK 3 S31: 0.0748 S32: -0.0165 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 3F7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50835
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 69.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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 1QG3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.3M NACL, 24% PEG 200,
REMARK 280 PH 7.5, VAPOR DIFFUSION, TEMPERATURE 298K
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
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 300 REMARK: THE MONOMERIC FORM IS BELIEVED TO BE THE BIOLOGICAL UNIT.
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 1122
REMARK 465 SER A 1123
REMARK 465 HIS A 1124
REMARK 465 MET A 1125
REMARK 465 GLY A 1340
REMARK 465 GLU A 1341
REMARK 465 ASP A 1342
REMARK 465 TYR A 1343
REMARK 465 ASP A 1344
REMARK 465 SER A 1345
REMARK 465 PHE A 1346
REMARK 465 LEU A 1347
REMARK 465 MET A 1348
REMARK 465 TYR A 1349
REMARK 465 SER A 1350
REMARK 465 ASP A 1351
REMARK 465 ASP A 1352
REMARK 465 VAL A 1353
REMARK 465 LEU A 1354
REMARK 465 ARG A 1355
REMARK 465 GLY B 1122
REMARK 465 SER B 1123
REMARK 465 HIS B 1124
REMARK 465 MET B 1125
REMARK 465 GLY B 1340
REMARK 465 GLU B 1341
REMARK 465 ASP B 1342
REMARK 465 TYR B 1343
REMARK 465 ASP B 1344
REMARK 465 SER B 1345
REMARK 465 PHE B 1346
REMARK 465 LEU B 1347
REMARK 465 MET B 1348
REMARK 465 TYR B 1349
REMARK 465 SER B 1350
REMARK 465 ASP B 1351
REMARK 465 ASP B 1352
REMARK 465 VAL B 1353
REMARK 465 LEU B 1354
REMARK 465 ARG B 1355
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 ASP A1166 -133.01 -93.64
REMARK 500 PRO A1179 45.98 -83.62
REMARK 500 ASN A1261 -155.58 -83.81
REMARK 500 GLU B1168 -7.37 -52.06
REMARK 500 PRO B1179 43.55 -83.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 1169 GLU B 1170 146.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 705
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QG3 RELATED DB: PDB
REMARK 900 SIMILAR FRAGMENT LACKING THE CONNECTING SEGMENT
REMARK 900 RELATED ID: 3F7P RELATED DB: PDB
REMARK 900 STRUCTURE OF A SIMILAR FRAGMENT OF INTEGRIN BETA4 IN COMPLEX WITH
REMARK 900 PLECTIN
REMARK 900 RELATED ID: 3F7R RELATED DB: PDB
REMARK 900 STRUCTURE AT 2.04A OF AN EQUIVALENT FRAGMENT OF INTEGRIN BETA4
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 2 IN THE DATABASE, ITB4_HUMAN.
DBREF 3F7Q A 1126 1355 UNP P16144 ITB4_HUMAN 1126 1355
DBREF 3F7Q B 1126 1355 UNP P16144 ITB4_HUMAN 1126 1355
SEQADV 3F7Q GLY A 1122 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q SER A 1123 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q HIS A 1124 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q MET A 1125 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q GLY B 1122 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q SER B 1123 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q HIS B 1124 UNP P16144 EXPRESSION TAG
SEQADV 3F7Q MET B 1125 UNP P16144 EXPRESSION TAG
SEQRES 1 A 234 GLY SER HIS MET ASP LEU GLY ALA PRO GLN ASN PRO ASN
SEQRES 2 A 234 ALA LYS ALA ALA GLY SER ARG LYS ILE HIS PHE ASN TRP
SEQRES 3 A 234 LEU PRO PRO SER GLY LYS PRO MET GLY TYR ARG VAL LYS
SEQRES 4 A 234 TYR TRP ILE GLN GLY ASP SER GLU SER GLU ALA HIS LEU
SEQRES 5 A 234 LEU ASP SER LYS VAL PRO SER VAL GLU LEU THR ASN LEU
SEQRES 6 A 234 TYR PRO TYR CYS ASP TYR GLU MET LYS VAL CYS ALA TYR
SEQRES 7 A 234 GLY ALA GLN GLY GLU GLY PRO TYR SER SER LEU VAL SER
SEQRES 8 A 234 CYS ARG THR HIS GLN GLU VAL PRO SER GLU PRO GLY ARG
SEQRES 9 A 234 LEU ALA PHE ASN VAL VAL SER SER THR VAL THR GLN LEU
SEQRES 10 A 234 SER TRP ALA GLU PRO ALA GLU THR ASN GLY GLU ILE THR
SEQRES 11 A 234 ALA TYR GLU VAL CYS TYR GLY LEU VAL ASN ASP ASP ASN
SEQRES 12 A 234 ARG PRO ILE GLY PRO MET LYS LYS VAL LEU VAL ASP ASN
SEQRES 13 A 234 PRO LYS ASN ARG MET LEU LEU ILE GLU ASN LEU ARG GLU
SEQRES 14 A 234 SER GLN PRO TYR ARG TYR THR VAL LYS ALA ARG ASN GLY
SEQRES 15 A 234 ALA GLY TRP GLY PRO GLU ARG GLU ALA ILE ILE ASN LEU
SEQRES 16 A 234 ALA THR GLN PRO LYS ARG PRO MET SER ILE PRO ILE ILE
SEQRES 17 A 234 PRO ASP ILE PRO ILE VAL ASP ALA GLN SER GLY GLU ASP
SEQRES 18 A 234 TYR ASP SER PHE LEU MET TYR SER ASP ASP VAL LEU ARG
SEQRES 1 B 234 GLY SER HIS MET ASP LEU GLY ALA PRO GLN ASN PRO ASN
SEQRES 2 B 234 ALA LYS ALA ALA GLY SER ARG LYS ILE HIS PHE ASN TRP
SEQRES 3 B 234 LEU PRO PRO SER GLY LYS PRO MET GLY TYR ARG VAL LYS
SEQRES 4 B 234 TYR TRP ILE GLN GLY ASP SER GLU SER GLU ALA HIS LEU
SEQRES 5 B 234 LEU ASP SER LYS VAL PRO SER VAL GLU LEU THR ASN LEU
SEQRES 6 B 234 TYR PRO TYR CYS ASP TYR GLU MET LYS VAL CYS ALA TYR
SEQRES 7 B 234 GLY ALA GLN GLY GLU GLY PRO TYR SER SER LEU VAL SER
SEQRES 8 B 234 CYS ARG THR HIS GLN GLU VAL PRO SER GLU PRO GLY ARG
SEQRES 9 B 234 LEU ALA PHE ASN VAL VAL SER SER THR VAL THR GLN LEU
SEQRES 10 B 234 SER TRP ALA GLU PRO ALA GLU THR ASN GLY GLU ILE THR
SEQRES 11 B 234 ALA TYR GLU VAL CYS TYR GLY LEU VAL ASN ASP ASP ASN
SEQRES 12 B 234 ARG PRO ILE GLY PRO MET LYS LYS VAL LEU VAL ASP ASN
SEQRES 13 B 234 PRO LYS ASN ARG MET LEU LEU ILE GLU ASN LEU ARG GLU
SEQRES 14 B 234 SER GLN PRO TYR ARG TYR THR VAL LYS ALA ARG ASN GLY
SEQRES 15 B 234 ALA GLY TRP GLY PRO GLU ARG GLU ALA ILE ILE ASN LEU
SEQRES 16 B 234 ALA THR GLN PRO LYS ARG PRO MET SER ILE PRO ILE ILE
SEQRES 17 B 234 PRO ASP ILE PRO ILE VAL ASP ALA GLN SER GLY GLU ASP
SEQRES 18 B 234 TYR ASP SER PHE LEU MET TYR SER ASP ASP VAL LEU ARG
HET CL A 601 1
HET PEG A 701 7
HET 1PE A 703 16
HET EDO A 706 4
HET EDO A 707 4
HET CL B 602 1
HET PEG B 702 7
HET PG4 B 704 13
HET EDO B 705 4
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN 1PE PEG400
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CL 2(CL 1-)
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 5 1PE C10 H22 O6
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 10 PG4 C8 H18 O5
FORMUL 12 HOH *502(H2 O)
HELIX 1 1 SER A 1167 ALA A 1171 5 5
HELIX 2 2 ASN A 1315 GLN A 1319 5 5
HELIX 3 3 SER B 1167 ALA B 1171 5 5
HELIX 4 4 ASN B 1315 GLN B 1319 5 5
SHEET 1 A 3 GLN A1131 ALA A1137 0
SHEET 2 A 3 ILE A1143 LEU A1148 -1 O HIS A1144 N LYS A1136
SHEET 3 A 3 SER A1180 LEU A1183 -1 O LEU A1183 N ILE A1143
SHEET 1 B 4 HIS A1172 SER A1176 0
SHEET 2 B 4 GLY A1156 ILE A1163 -1 N TYR A1157 O SER A1176
SHEET 3 B 4 ASP A1191 GLY A1200 -1 O GLU A1193 N TRP A1162
SHEET 4 B 4 GLY A1203 GLU A1204 -1 O GLY A1203 N GLY A1200
SHEET 1 C 4 HIS A1172 SER A1176 0
SHEET 2 C 4 GLY A1156 ILE A1163 -1 N TYR A1157 O SER A1176
SHEET 3 C 4 ASP A1191 GLY A1200 -1 O GLU A1193 N TRP A1162
SHEET 4 C 4 VAL A1211 ARG A1214 -1 O CYS A1213 N TYR A1192
SHEET 1 D 4 ALA A1227 VAL A1230 0
SHEET 2 D 4 THR A1236 SER A1239 -1 O SER A1239 N ALA A1227
SHEET 3 D 4 MET A1282 GLU A1286 -1 O LEU A1283 N LEU A1238
SHEET 4 D 4 ILE A1334 ASP A1336 1 O VAL A1335 N GLU A1286
SHEET 1 E 4 LYS A1271 LYS A1272 0
SHEET 2 E 4 ALA A1252 LEU A1259 -1 N TYR A1257 O LYS A1271
SHEET 3 E 4 TYR A1294 ASN A1302 -1 O ARG A1301 N ALA A1252
SHEET 4 E 4 GLY A1305 TRP A1306 -1 O GLY A1305 N ASN A1302
SHEET 1 F 4 LYS A1271 LYS A1272 0
SHEET 2 F 4 ALA A1252 LEU A1259 -1 N TYR A1257 O LYS A1271
SHEET 3 F 4 TYR A1294 ASN A1302 -1 O ARG A1301 N ALA A1252
SHEET 4 F 4 ARG A1310 ILE A1314 -1 O ALA A1312 N TYR A1296
SHEET 1 G 3 GLN B1131 ALA B1137 0
SHEET 2 G 3 ILE B1143 LEU B1148 -1 O LEU B1148 N GLN B1131
SHEET 3 G 3 SER B1180 LEU B1183 -1 O LEU B1183 N ILE B1143
SHEET 1 H 4 HIS B1172 SER B1176 0
SHEET 2 H 4 GLY B1156 ILE B1163 -1 N TYR B1161 O HIS B1172
SHEET 3 H 4 ASP B1191 GLY B1200 -1 O GLU B1193 N TRP B1162
SHEET 4 H 4 GLY B1203 GLU B1204 -1 O GLY B1203 N GLY B1200
SHEET 1 I 4 HIS B1172 SER B1176 0
SHEET 2 I 4 GLY B1156 ILE B1163 -1 N TYR B1161 O HIS B1172
SHEET 3 I 4 ASP B1191 GLY B1200 -1 O GLU B1193 N TRP B1162
SHEET 4 I 4 VAL B1211 ARG B1214 -1 O CYS B1213 N TYR B1192
SHEET 1 J 4 ALA B1227 SER B1232 0
SHEET 2 J 4 VAL B1235 SER B1239 -1 O SER B1239 N ALA B1227
SHEET 3 J 4 MET B1282 GLU B1286 -1 O ILE B1285 N THR B1236
SHEET 4 J 4 ILE B1334 ASP B1336 1 O VAL B1335 N GLU B1286
SHEET 1 K 4 LYS B1271 LYS B1272 0
SHEET 2 K 4 ALA B1252 LEU B1259 -1 N TYR B1257 O LYS B1271
SHEET 3 K 4 TYR B1294 ASN B1302 -1 O ARG B1301 N ALA B1252
SHEET 4 K 4 GLY B1305 TRP B1306 -1 O GLY B1305 N ASN B1302
SHEET 1 L 4 LYS B1271 LYS B1272 0
SHEET 2 L 4 ALA B1252 LEU B1259 -1 N TYR B1257 O LYS B1271
SHEET 3 L 4 TYR B1294 ASN B1302 -1 O ARG B1301 N ALA B1252
SHEET 4 L 4 ARG B1310 ILE B1314 -1 O ALA B1312 N TYR B1296
SITE 1 AC1 6 HOH A 238 GLY A1139 SER A1140 ARG A1141
SITE 2 AC1 6 LYS A1142 LYS B1142
SITE 1 AC2 3 ASN A1185 TYR A1187 GLU B1245
SITE 1 AC3 5 HOH A 201 GLU A1254 LYS A1272 GLU B1286
SITE 2 AC3 5 ILE B1334
SITE 1 AC4 2 GLU A1170 HIS A1172
SITE 1 AC5 2 GLU A1222 GLU B1170
SITE 1 AC6 5 LYS A1142 GLY B1139 SER B1140 ARG B1141
SITE 2 AC6 5 LYS B1142
SITE 1 AC7 4 HOH B 365 HOH B 418 ASN B1185 TYR B1187
SITE 1 AC8 5 GLU A1286 ILE A1326 HOH B 410 LYS B1272
SITE 2 AC8 5 LEU B1274
SITE 1 AC9 6 HOH B 252 TYR B1161 LEU B1174 GLU B1182
SITE 2 AC9 6 LEU B1183 THR B1184
CRYST1 43.110 49.470 74.360 107.22 96.06 106.60 P 1 2
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 0.023196 0.006915 0.005141 0.00000
SCALE2 0.000000 0.021093 0.007686 0.00000
SCALE3 0.000000 0.000000 0.014394 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
