HEADER CELL ADHESION 07-MAR-07 2P28
TITLE STRUCTURE OF THE PHE2 AND PHE3 FRAGMENTS OF THE INTEGRIN BETA2 SUBUNIT
CAVEAT 2P28 NAG A 401 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN BETA-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHE2 FRAGMENT;
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;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTEGRIN BETA-2;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: PHE3 FRAGMENT;
COMPND 12 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA- 1/CR3/P150,95
COMPND 13 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT BETA, CD18 ANTIGEN;
COMPND 14 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;
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_GNTI;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 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 6 25-OCT-23 2P28 1 HETSYN
REVDAT 5 29-JUL-20 2P28 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM SITE
REVDAT 4 13-JUL-11 2P28 1 VERSN
REVDAT 3 24-FEB-09 2P28 1 VERSN
REVDAT 2 17-JUN-08 2P28 1 JRNL
REVDAT 1 14-AUG-07 2P28 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 18723
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) : 0.263
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 964
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1255
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2355
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 199
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : UNVERIFIED
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.24000
REMARK 3 B12 (A**2) : 0.08000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.341
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.262
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.734
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2408 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2053 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3257 ; 1.223 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4816 ; 0.800 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 305 ; 6.312 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 355 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2710 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 466 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 442 ; 0.174 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2404 ; 0.221 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1536 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 142 ; 0.174 ; 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): 28 ; 0.185 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 100 ; 0.231 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.158 ; 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): 1532 ; 0.716 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2453 ; 1.337 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 876 ; 1.332 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 804 ; 2.281 ; 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 : 3
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 B 431
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5719 19.7650 9.1114
REMARK 3 T TENSOR
REMARK 3 T11: 0.5006 T22: 0.4081
REMARK 3 T33: 0.4655 T12: 0.0153
REMARK 3 T13: -0.0505 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 1.1953 L22: 0.6294
REMARK 3 L33: 2.0810 L12: -0.3745
REMARK 3 L13: -0.5242 L23: 0.9519
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: 0.1246 S13: -0.0428
REMARK 3 S21: 0.1741 S22: 0.0322 S23: -0.0664
REMARK 3 S31: 0.3092 S32: -0.1245 S33: -0.0679
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 : B 435 B 466
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9354 23.4167 42.1519
REMARK 3 T TENSOR
REMARK 3 T11: 0.7003 T22: 0.2709
REMARK 3 T33: 0.3286 T12: -0.3067
REMARK 3 T13: 0.0132 T23: -0.2175
REMARK 3 L TENSOR
REMARK 3 L11: 13.9432 L22: 6.7843
REMARK 3 L33: 28.2786 L12: -6.6546
REMARK 3 L13: -12.2910 L23: 11.4915
REMARK 3 S TENSOR
REMARK 3 S11: 0.2904 S12: -0.1926 S13: 0.7016
REMARK 3 S21: -0.1336 S22: -0.8847 S23: 0.3085
REMARK 3 S31: 1.7915 S32: -0.7804 S33: 0.5943
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 : B 470 B 556
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1695 44.7480 69.1864
REMARK 3 T TENSOR
REMARK 3 T11: 0.4187 T22: 0.4547
REMARK 3 T33: 0.5230 T12: -0.0847
REMARK 3 T13: 0.0100 T23: -0.0696
REMARK 3 L TENSOR
REMARK 3 L11: 1.7190 L22: 0.5953
REMARK 3 L33: 3.9696 L12: 0.7188
REMARK 3 L13: -1.6289 L23: 0.3703
REMARK 3 S TENSOR
REMARK 3 S11: 0.2513 S12: -0.0634 S13: 0.0195
REMARK 3 S21: 0.0830 S22: -0.1227 S23: -0.0328
REMARK 3 S31: -0.2204 S32: 0.2268 S33: -0.1286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2P28 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_1000041874.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-06
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18866
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
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: AMORE, PHASES
REMARK 200 STARTING MODEL: 1YUK, 1L3Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULPHATE, 15% PEG4000,
REMARK 280 5% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 282.61600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 141.30800
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 211.96200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.65400
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 353.27000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 282.61600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 141.30800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 70.65400
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 211.96200
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 353.27000
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: 4430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 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 HIS A 69
REMARK 465 ASN A 70
REMARK 465 GLY A 71
REMARK 465 GLY A 72
REMARK 465 ASP B 433
REMARK 465 ARG B 434
REMARK 465 SER B 467
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG B 466 CG CD NE CZ NH1 NH2
REMARK 470 SER B 468 OG
REMARK 470 GLN B 469 CG CD OE1 NE2
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 B 557 O HOH B 594 8665 1.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 68 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 377 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 515 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 2 115.44 -176.51
REMARK 500 PHE A 6 -79.35 -75.85
REMARK 500 ASP A 58 74.33 -159.06
REMARK 500 LYS A 74 -76.22 -84.66
REMARK 500 GLU B 444 110.39 -169.10
REMARK 500 GLN B 464 -153.10 -106.24
REMARK 500 ASN B 480 46.12 -108.13
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 431 ARG B 432 -134.39
REMARK 500 SER B 435 LEU B 436 -58.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P26 RELATED DB: PDB
DBREF 2P28 A 1 100 UNP P05107 ITB2_HUMAN 23 122
DBREF 2P28 B 340 552 UNP P05107 ITB2_HUMAN 362 574
SEQADV 2P28 HIS B 553 UNP P05107 EXPRESSION TAG
SEQADV 2P28 HIS B 554 UNP P05107 EXPRESSION TAG
SEQADV 2P28 HIS B 555 UNP P05107 EXPRESSION TAG
SEQADV 2P28 HIS B 556 UNP P05107 EXPRESSION TAG
SEQRES 1 A 100 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU
SEQRES 2 A 100 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS
SEQRES 3 A 100 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG
SEQRES 4 A 100 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA
SEQRES 5 A 100 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR
SEQRES 6 A 100 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO
SEQRES 7 A 100 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA
SEQRES 8 A 100 ALA PHE ASN VAL THR PHE ARG ARG ALA
SEQRES 1 B 217 LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA LEU
SEQRES 2 B 217 PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS SER
SEQRES 3 B 217 ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP CYS
SEQRES 4 B 217 ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN VAL
SEQRES 5 B 217 LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER PHE
SEQRES 6 B 217 VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR VAL
SEQRES 7 B 217 GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP GLN
SEQRES 8 B 217 SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE LEU
SEQRES 9 B 217 GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE GLY
SEQRES 10 B 217 LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER GLN
SEQRES 11 B 217 GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER ILE
SEQRES 12 B 217 ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN CYS
SEQRES 13 B 217 LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE TYR
SEQRES 14 B 217 GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU ARG
SEQRES 15 B 217 TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY LEU
SEQRES 16 B 217 CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE GLU
SEQRES 17 B 217 GLY SER ALA CYS GLN HIS HIS HIS HIS
HET NAG A 401 15
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 3 NAG C8 H15 N O6
FORMUL 4 HOH *199(H2 O)
HELIX 1 1 SER A 10 GLY A 18 1 9
HELIX 2 2 LYS A 26 THR A 30 5 5
HELIX 3 3 PRO A 35 ILE A 38 5 4
HELIX 4 4 THR A 42 MET A 48 1 7
HELIX 5 5 ALA A 52 ASP A 54 5 3
HELIX 6 6 SER B 468 ARG B 476 5 9
HELIX 7 7 ILE B 482 GLY B 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 GLU A 67 0
SHEET 2 B 6 LYS A 80 LEU A 85 -1 O THR A 82 N GLU A 64
SHEET 3 B 6 ILE B 414 PRO B 421 1 O GLN B 418 N LEU A 83
SHEET 4 B 6 GLN B 402 ALA B 408 -1 N GLN B 402 O VAL B 419
SHEET 5 B 6 VAL B 345 HIS B 349 -1 N ASP B 348 O ARG B 407
SHEET 6 B 6 GLY B 376 CYS B 378 -1 O CYS B 378 N VAL B 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 B 387 ALA B 395 -1 O VAL B 393 N ALA A 91
SHEET 4 C 5 LEU B 356 PHE B 363 -1 N PHE B 363 O THR B 388
SHEET 5 C 5 THR B 369 GLN B 373 -1 O GLN B 373 N TYR B 360
SHEET 1 D 2 GLY B 441 GLU B 444 0
SHEET 2 D 2 ILE B 447 CYS B 450 -1 O ARG B 449 N PHE B 442
SHEET 1 E 2 TYR B 454 ILE B 455 0
SHEET 2 E 2 CYS B 461 GLN B 462 -1 O CYS B 461 N ILE B 455
SHEET 1 F 2 GLY B 488 VAL B 491 0
SHEET 2 F 2 GLN B 494 CYS B 497 -1 O GLN B 494 N VAL B 491
SHEET 1 G 2 ILE B 507 TYR B 508 0
SHEET 2 G 2 CYS B 514 ASP B 515 -1 O CYS B 514 N TYR B 508
SHEET 1 H 2 ARG B 521 TYR B 522 0
SHEET 2 H 2 GLN B 525 VAL B 526 -1 O GLN B 525 N TYR B 522
SHEET 1 I 2 GLY B 533 PHE B 536 0
SHEET 2 I 2 LYS B 539 CYS B 542 -1 O ARG B 541 N LEU B 534
SHEET 1 J 2 PHE B 546 GLU B 547 0
SHEET 2 J 2 HIS B 553 HIS B 554 -1 O HIS B 553 N GLU B 547
SSBOND 1 CYS A 3 CYS A 21 1555 1555 2.06
SSBOND 2 CYS A 11 CYS B 425 1555 1555 2.03
SSBOND 3 CYS A 14 CYS A 40 1555 1555 2.05
SSBOND 4 CYS A 24 CYS A 51 1555 1555 2.04
SSBOND 5 CYS B 364 CYS B 378 1555 1555 2.02
SSBOND 6 CYS B 398 CYS B 423 1555 1555 2.03
SSBOND 7 CYS B 427 CYS B 445 1555 1555 2.03
SSBOND 8 CYS B 437 CYS B 448 1555 1555 2.04
SSBOND 9 CYS B 450 CYS B 459 1555 1555 2.04
SSBOND 10 CYS B 461 CYS B 492 1555 1555 2.07
SSBOND 11 CYS B 475 CYS B 490 1555 1555 2.06
SSBOND 12 CYS B 484 CYS B 495 1555 1555 2.06
SSBOND 13 CYS B 497 CYS B 512 1555 1555 2.06
SSBOND 14 CYS B 514 CYS B 537 1555 1555 2.07
SSBOND 15 CYS B 519 CYS B 535 1555 1555 2.04
SSBOND 16 CYS B 527 CYS B 540 1555 1555 1.83
SSBOND 17 CYS B 542 CYS B 551 1555 1555 2.03
CISPEP 1 SER A 77 PRO A 78 0 -1.55
CRYST1 52.260 52.260 423.924 90.00 90.00 120.00 P 65 2 2 12
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 0.019135 0.011048 0.000000 0.00000
SCALE2 0.000000 0.022095 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002359 0.00000
(ATOM LINES ARE NOT SHOWN.)
END