HEADER CELL ADHESION 06-MAR-07 2P26
TITLE STRUCTURE OF THE PHE2 AND PHE3 FRAGMENTS OF THE INTEGRIN BETA2 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN BETA-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHE2 AND PHE3;
COMPND 5 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA- 1/CR3/P150,95
COMPND 6 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT BETA, CD18 ANTIGEN;
COMPND 7 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_GNTI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PIRES2-EGFP
KEYWDS INTEGRIN BETA2 SUBUNIT, HYBRID DOMAIN, PSI DOMAIN, I-EGF DOMAINS,
KEYWDS 2 CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SHI,S.Y.FOO,S.M.TAN,E.P.MITCHELL,S.K.A.LAW,J.LESCAR
REVDAT 7 25-OCT-23 2P26 1 HETSYN
REVDAT 6 29-JUL-20 2P26 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE
REVDAT 5 16-AUG-17 2P26 1 SOURCE REMARK
REVDAT 4 13-JUL-11 2P26 1 VERSN
REVDAT 3 24-FEB-09 2P26 1 VERSN
REVDAT 2 17-JUN-08 2P26 1 JRNL
REVDAT 1 14-AUG-07 2P26 0
JRNL AUTH M.SHI,S.Y.FOO,S.M.TAN,E.P.MITCHELL,S.K.A.LAW,J.LESCAR
JRNL TITL A STRUCTURAL HYPOTHESIS FOR THE TRANSITION BETWEEN BENT AND
JRNL TITL 2 EXTENDED CONFORMATIONS OF THE LEUKOCYTE BETA2 INTEGRINS
JRNL REF J.BIOL.CHEM. V. 282 30198 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17673459
JRNL DOI 10.1074/JBC.M701670200
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 21815
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1117
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 817
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 48.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.4040
REMARK 3 BIN FREE R VALUE SET COUNT : 36
REMARK 3 BIN FREE R VALUE : 0.5920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2156
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.179
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.870
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2281 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3095 ; 1.169 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 5.817 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;35.744 ;24.220
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 384 ;15.033 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;12.783 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 338 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1740 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 957 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1516 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 207 ; 0.111 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 157 ; 0.185 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 41 ; 0.133 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1448 ; 0.378 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2275 ; 0.649 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 907 ; 1.101 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 820 ; 1.794 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 63
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8980 -7.8590 -32.0500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0622 T22: 0.0056
REMARK 3 T33: 0.0181 T12: 0.0117
REMARK 3 T13: -0.0035 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 2.0658 L22: 2.2788
REMARK 3 L33: 1.7243 L12: 0.1150
REMARK 3 L13: 0.7279 L23: -0.2921
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: -0.0400 S13: -0.0597
REMARK 3 S21: 0.0526 S22: -0.0008 S23: 0.0902
REMARK 3 S31: -0.0941 S32: -0.1010 S33: -0.0240
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 64 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0320 -18.8270 -11.8320
REMARK 3 T TENSOR
REMARK 3 T11: 0.3017 T22: 0.3394
REMARK 3 T33: 0.4643 T12: 0.0437
REMARK 3 T13: -0.0759 T23: 0.1047
REMARK 3 L TENSOR
REMARK 3 L11: 7.8094 L22: 2.0915
REMARK 3 L33: 9.0043 L12: -1.5293
REMARK 3 L13: 2.8790 L23: -2.5158
REMARK 3 S TENSOR
REMARK 3 S11: 0.5910 S12: -0.0352 S13: -1.8147
REMARK 3 S21: 0.0828 S22: -0.2474 S23: -0.1995
REMARK 3 S31: 0.9772 S32: 1.0782 S33: -0.3436
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 76 A 351
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6760 -7.7560 -11.0730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0689 T22: 0.0287
REMARK 3 T33: -0.0397 T12: -0.0193
REMARK 3 T13: -0.0096 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 3.9144 L22: 1.3659
REMARK 3 L33: 1.3444 L12: -0.4509
REMARK 3 L13: 0.9498 L23: -0.0421
REMARK 3 S TENSOR
REMARK 3 S11: 0.0428 S12: -0.4148 S13: -0.1406
REMARK 3 S21: 0.2024 S22: 0.0556 S23: 0.0413
REMARK 3 S31: 0.0195 S32: -0.0226 S33: -0.0983
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 352 A 388
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1490 -2.3460 -5.1440
REMARK 3 T TENSOR
REMARK 3 T11: 0.0431 T22: 0.0937
REMARK 3 T33: -0.0337 T12: -0.0103
REMARK 3 T13: -0.0001 T23: -0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 3.2338 L22: 2.6518
REMARK 3 L33: 8.0144 L12: -0.6692
REMARK 3 L13: 1.3006 L23: -1.5501
REMARK 3 S TENSOR
REMARK 3 S11: -0.0421 S12: -0.6335 S13: 0.2584
REMARK 3 S21: 0.2909 S22: 0.2343 S23: 0.0960
REMARK 3 S31: -0.0785 S32: -0.2294 S33: -0.1921
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 389 A 426
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9660 -6.9340 -20.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.0098
REMARK 3 T33: 0.0089 T12: -0.0193
REMARK 3 T13: -0.0066 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 3.6964 L22: 0.3879
REMARK 3 L33: 1.2595 L12: -0.1352
REMARK 3 L13: 1.5244 L23: -0.0132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: 0.0895 S13: -0.0657
REMARK 3 S21: 0.0496 S22: -0.0321 S23: 0.0536
REMARK 3 S31: -0.0029 S32: 0.1464 S33: -0.0073
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 427 A 447
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3420 -20.1960 -45.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0737 T22: -0.0050
REMARK 3 T33: -0.0001 T12: -0.0058
REMARK 3 T13: -0.0172 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.9944 L22: 2.2312
REMARK 3 L33: 3.8742 L12: -1.8910
REMARK 3 L13: -0.0582 L23: 0.5789
REMARK 3 S TENSOR
REMARK 3 S11: 0.0916 S12: 0.0142 S13: -0.0987
REMARK 3 S21: -0.1132 S22: -0.0895 S23: 0.0570
REMARK 3 S31: 0.2312 S32: -0.0664 S33: -0.0021
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 448 A 461
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8670 -12.5890 -52.9150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0536 T22: 0.0600
REMARK 3 T33: -0.0193 T12: 0.0378
REMARK 3 T13: -0.0075 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 6.5756 L22: 4.9567
REMARK 3 L33: 5.1811 L12: -2.8482
REMARK 3 L13: 0.8871 L23: -0.5513
REMARK 3 S TENSOR
REMARK 3 S11: 0.1884 S12: 0.3508 S13: 0.4120
REMARK 3 S21: -0.1237 S22: -0.2035 S23: -0.1579
REMARK 3 S31: -0.1364 S32: -0.0458 S33: 0.0151
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 462 A 484
REMARK 3 ORIGIN FOR THE GROUP (A): -29.1840 -0.7220 -57.0380
REMARK 3 T TENSOR
REMARK 3 T11: 0.2639 T22: 0.2003
REMARK 3 T33: 0.0157 T12: 0.0120
REMARK 3 T13: 0.0995 T23: 0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 3.3570 L22: 6.2386
REMARK 3 L33: 3.2061 L12: 1.2123
REMARK 3 L13: 2.9453 L23: -0.8359
REMARK 3 S TENSOR
REMARK 3 S11: 0.3735 S12: 0.3832 S13: 0.4884
REMARK 3 S21: -1.1835 S22: 0.1059 S23: -0.4308
REMARK 3 S31: -0.6054 S32: 0.6698 S33: -0.4793
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 485 A 511
REMARK 3 ORIGIN FOR THE GROUP (A): -38.5940 -5.8630 -45.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0273 T22: 0.0824
REMARK 3 T33: -0.0674 T12: 0.0670
REMARK 3 T13: -0.0362 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 3.1521 L22: 1.8016
REMARK 3 L33: 4.3139 L12: -0.6472
REMARK 3 L13: -2.9893 L23: 1.1772
REMARK 3 S TENSOR
REMARK 3 S11: 0.1389 S12: 0.4367 S13: 0.0610
REMARK 3 S21: -0.1408 S22: -0.1960 S23: 0.1949
REMARK 3 S31: 0.0180 S32: -0.1287 S33: 0.0571
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 512 A 519
REMARK 3 ORIGIN FOR THE GROUP (A): -46.1830 -1.7230 -41.8920
REMARK 3 T TENSOR
REMARK 3 T11: 0.0190 T22: 0.0563
REMARK 3 T33: -0.0246 T12: -0.0229
REMARK 3 T13: -0.0506 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 10.1320 L22: 8.2715
REMARK 3 L33: 7.5520 L12: -6.2355
REMARK 3 L13: -5.7186 L23: 0.1195
REMARK 3 S TENSOR
REMARK 3 S11: 0.0468 S12: 0.4270 S13: -0.2568
REMARK 3 S21: 0.0407 S22: 0.2147 S23: 0.7462
REMARK 3 S31: 0.3460 S32: -0.5641 S33: -0.2614
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2P26 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.6
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 : RIGAKU RU300
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21822
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 27.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 1YUK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE, 0.1M SODIUM
REMARK 280 ACETATE, PH4.6, 18% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 15.42650
REMARK 290 SMTRY3 2 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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 766 O HOH A 784 2.15
REMARK 500 O HOH A 766 O HOH A 787 2.16
REMARK 500 O HOH A 641 O HOH A 772 2.19
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 766 O HOH A 783 2454 1.59
REMARK 500 O7 NAG A 302 O HOH A 771 1565 2.17
REMARK 500 NH2 ARG A 466 O HOH A 688 2453 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 484 CB CYS A 484 SG -0.118
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 58 67.63 -160.57
REMARK 500 HIS A 69 -88.52 -49.57
REMARK 500 HIS A 69 -97.63 -36.65
REMARK 500 LYS A 340 -55.83 -128.75
REMARK 500 ASN A 384 -1.48 72.94
REMARK 500 HIS A 438 18.07 56.12
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 HIS A 69 ASN A 70 149.61
REMARK 500 HIS A 69 ASN A 70 148.17
REMARK 500 GLY A 465 ARG A 466 130.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P28 RELATED DB: PDB
DBREF 2P26 A 1 100 UNP P05107 ITB2_HUMAN 23 122
DBREF 2P26 A 340 513 UNP P05107 ITB2_HUMAN 362 535
SEQADV 2P26 HIS A 514 UNP P05107 EXPRESSION TAG
SEQADV 2P26 HIS A 515 UNP P05107 EXPRESSION TAG
SEQADV 2P26 HIS A 516 UNP P05107 EXPRESSION TAG
SEQADV 2P26 HIS A 517 UNP P05107 EXPRESSION TAG
SEQADV 2P26 HIS A 518 UNP P05107 EXPRESSION TAG
SEQADV 2P26 HIS A 519 UNP P05107 EXPRESSION TAG
SEQRES 1 A 280 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 A 280 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 A 280 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 A 280 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 A 280 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 A 280 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 A 280 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 A 280 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS LEU SER SER
SEQRES 9 A 280 ARG VAL PHE LEU ASP HIS ASN ALA LEU PRO ASP THR LEU
SEQRES 10 A 280 LYS VAL THR TYR ASP SER PHE CYS SER ASN GLY VAL THR
SEQRES 11 A 280 HIS ARG ASN GLN PRO ARG GLY ASP CYS ASP GLY VAL GLN
SEQRES 12 A 280 ILE ASN VAL PRO ILE THR PHE GLN VAL LYS VAL THR ALA
SEQRES 13 A 280 THR GLU CYS ILE GLN GLU GLN SER PHE VAL ILE ARG ALA
SEQRES 14 A 280 LEU GLY PHE THR ASP ILE VAL THR VAL GLN VAL LEU PRO
SEQRES 15 A 280 GLN CYS GLU CYS ARG CYS ARG ASP GLN SER ARG ASP ARG
SEQRES 16 A 280 SER LEU CYS HIS GLY LYS GLY PHE LEU GLU CYS GLY ILE
SEQRES 17 A 280 CYS ARG CYS ASP THR GLY TYR ILE GLY LYS ASN CYS GLU
SEQRES 18 A 280 CYS GLN THR GLN GLY ARG SER SER GLN GLU LEU GLU GLY
SEQRES 19 A 280 SER CYS ARG LYS ASP ASN ASN SER ILE ILE CYS SER GLY
SEQRES 20 A 280 LEU GLY ASP CYS VAL CYS GLY GLN CYS LEU CYS HIS THR
SEQRES 21 A 280 SER ASP VAL PRO GLY LYS LEU ILE TYR GLY GLN TYR CYS
SEQRES 22 A 280 GLU HIS HIS HIS HIS HIS HIS
MODRES 2P26 ASN A 28 ASN GLYCOSYLATION SITE
MODRES 2P26 ASN A 94 ASN GLYCOSYLATION SITE
MODRES 2P26 ASN A 479 ASN GLYCOSYLATION SITE
HET NAG A 301 14
HET NAG A 302 14
HET NAG A 303 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 5 HOH *268(H2 O)
HELIX 1 1 SER A 10 GLU A 16 1 7
HELIX 2 2 PRO A 35 ILE A 38 5 4
HELIX 3 3 THR A 42 ARG A 49 1 8
HELIX 4 4 ALA A 52 ASP A 54 5 3
HELIX 5 5 SER A 435 GLY A 439 5 5
HELIX 6 6 SER A 467 SER A 474 1 8
HELIX 7 7 ILE A 482 GLY A 486 5 5
SHEET 1 A 3 CYS A 40 ASP A 41 0
SHEET 2 A 3 THR A 22 CYS A 24 -1 N THR A 22 O ASP A 41
SHEET 3 A 3 ILE A 56 MET A 57 -1 O MET A 57 N TRP A 23
SHEET 1 B 6 LEU A 62 GLN A 66 0
SHEET 2 B 6 LYS A 80 LEU A 85 -1 O THR A 82 N GLU A 64
SHEET 3 B 6 VAL A 415 PRO A 421 1 O GLN A 418 N LEU A 83
SHEET 4 B 6 GLN A 402 ALA A 408 -1 N GLN A 402 O VAL A 419
SHEET 5 B 6 VAL A 345 HIS A 349 -1 N ASP A 348 O ARG A 407
SHEET 6 B 6 GLY A 376 CYS A 378 -1 O CYS A 378 N VAL A 345
SHEET 1 C 5 LEU A 76 SER A 77 0
SHEET 2 C 5 ALA A 91 PHE A 97 -1 O THR A 96 N SER A 77
SHEET 3 C 5 ILE A 387 ALA A 395 -1 O VAL A 391 N PHE A 93
SHEET 4 C 5 LEU A 356 PHE A 363 -1 N PHE A 363 O THR A 388
SHEET 5 C 5 THR A 369 GLN A 373 -1 O HIS A 370 N SER A 362
SHEET 1 D 2 GLY A 441 GLU A 444 0
SHEET 2 D 2 ILE A 447 CYS A 450 -1 O ARG A 449 N PHE A 442
SHEET 1 E 2 TYR A 454 ILE A 455 0
SHEET 2 E 2 CYS A 461 GLN A 462 -1 O CYS A 461 N ILE A 455
SHEET 1 F 2 GLY A 488 VAL A 491 0
SHEET 2 F 2 GLN A 494 CYS A 497 -1 O LEU A 496 N ASP A 489
SHEET 1 G 2 LEU A 506 TYR A 508 0
SHEET 2 G 2 HIS A 514 HIS A 516 -1 O HIS A 516 N LEU A 506
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.04
SSBOND 2 CYS A 11 CYS A 425 1555 1555 2.01
SSBOND 3 CYS A 14 CYS A 40 1555 1555 2.02
SSBOND 4 CYS A 24 CYS A 51 1555 1555 2.04
SSBOND 5 CYS A 364 CYS A 378 1555 1555 2.04
SSBOND 6 CYS A 398 CYS A 423 1555 1555 2.03
SSBOND 7 CYS A 427 CYS A 445 1555 1555 2.02
SSBOND 8 CYS A 437 CYS A 448 1555 1555 2.03
SSBOND 9 CYS A 450 CYS A 459 1555 1555 2.04
SSBOND 10 CYS A 461 CYS A 492 1555 1555 2.03
SSBOND 11 CYS A 475 CYS A 490 1555 1555 2.03
SSBOND 12 CYS A 484 CYS A 495 1555 1555 2.07
SSBOND 13 CYS A 497 CYS A 512 1555 1555 2.03
LINK ND2 ASN A 28 C1 NAG A 303 1555 1555 1.44
LINK ND2 ASN A 94 C1 NAG A 301 1555 1555 1.44
LINK C1 NAG A 302 ND2 ASN A 479 1555 1555 1.45
CISPEP 1 GLN A 1 GLU A 2 0 6.41
CISPEP 2 GLN A 1 GLU A 2 0 0.31
CISPEP 3 GLY A 71 GLY A 72 0 24.64
CISPEP 4 SER A 77 PRO A 78 0 -2.70
CISPEP 5 LEU A 341 SER A 342 0 4.21
CISPEP 6 ASN A 366 GLY A 367 0 -6.57
CISPEP 7 PRO A 503 GLY A 504 0 -14.71
CRYST1 58.489 30.853 65.157 90.00 94.29 90.00 P 1 21 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 0.017097 0.000000 0.001283 0.00000
SCALE2 0.000000 0.032412 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015391 0.00000
(ATOM LINES ARE NOT SHOWN.)
END