HEADER CELL ADHESION/BLOOD CLOTTING 22-NOV-08 3FCU
TITLE STRUCTURE OF HEADPIECE OF INTEGRIN AIIBB3 IN OPEN CONFORMATION
CAVEAT 3FCU MAN G 3 HAS WRONG CHIRALITY AT ATOM C1 MAN H 3 HAS WRONG
CAVEAT 2 3FCU CHIRALITY AT ATOM C1 MAN I 3 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN, ALPHA 2B;
COMPND 3 CHAIN: A, C, E;
COMPND 4 FRAGMENT: UNP RESIDUES 32-488, HEADPIECE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTEGRIN BETA-3;
COMPND 8 CHAIN: B, D, F;
COMPND 9 FRAGMENT: UNP RESIDUES 27-487;
COMPND 10 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;
COMPND 11 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: ITGA2B;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: ITGB3, GP3A;
SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS CRYSTAL STRUCTURE; PLATELET INTEGRIN ALPHAIIBBETA3; FIBRINOGEN
KEYWDS 2 BINDING; ALLOSTERY; THERAPEUTIC ANTAGONISM, CELL ADHESION, INTEGRIN,
KEYWDS 3 MEMBRANE, RECEPTOR, TRANSMEMBRANE, DISEASE MUTATION, GLYCOPROTEIN,
KEYWDS 4 HOST-VIRUS INTERACTION, PHOSPHOPROTEIN, CELL ADHESION-IMMUNE SYSTEM
KEYWDS 5 COMPLEX, CELL ADHESION-BLOOD CLOTTING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHU,B.-H.LUO,T.XIAO,C.ZHANG,N.NISHIDA,T.A.SPRINGER
REVDAT 4 06-SEP-23 3FCU 1 HETSYN
REVDAT 3 29-JUL-20 3FCU 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 13-JUL-11 3FCU 1 VERSN
REVDAT 1 20-JAN-09 3FCU 0
JRNL AUTH J.ZHU,B.H.LUO,T.XIAO,C.ZHANG,N.NISHIDA,T.A.SPRINGER
JRNL TITL STRUCTURE OF A COMPLETE INTEGRIN ECTODOMAIN IN A PHYSIOLOGIC
JRNL TITL 2 RESTING STATE AND ACTIVATION AND DEACTIVATION BY APPLIED
JRNL TITL 3 FORCES.
JRNL REF MOL.CELL V. 32 849 2008
JRNL REFN ISSN 1097-2765
JRNL PMID 19111664
JRNL DOI 10.1016/J.MOLCEL.2008.11.018
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 115380
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 3098
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7316
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 323
REMARK 3 SOLVENT ATOMS : 298
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) : 60.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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): 0.447
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.254
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.189
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.427
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21878 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 14771 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 29791 ; 0.657 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35772 ; 0.645 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2726 ; 5.541 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 992 ;31.407 ;24.123
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3425 ;12.696 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 143 ;11.570 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3301 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 24519 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4399 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 13556 ; 2.238 ; 8.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5536 ; 0.361 ; 8.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21825 ; 3.887 ;16.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8322 ; 2.536 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7964 ; 4.194 ;16.000
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 : 7
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 27 5
REMARK 3 1 C 2 C 27 5
REMARK 3 1 E 2 E 27 5
REMARK 3 2 A 33 A 43 4
REMARK 3 2 C 33 C 43 4
REMARK 3 2 E 33 E 43 4
REMARK 3 3 A 47 A 207 4
REMARK 3 3 C 47 C 207 4
REMARK 3 3 E 47 E 207 4
REMARK 3 4 A 209 A 212 4
REMARK 3 4 C 209 C 212 4
REMARK 3 4 E 209 E 212 4
REMARK 3 5 A 216 A 221 4
REMARK 3 5 C 216 C 221 4
REMARK 3 5 E 216 E 221 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2483 ; 0.280 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2483 ; 0.200 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 2483 ; 0.220 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 197 ; 0.300 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 197 ; 0.250 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 E (A): 197 ; 0.330 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2483 ; 0.300 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2483 ; 0.300 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 2483 ; 0.310 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 197 ; 0.190 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 197 ; 0.200 ;10.000
REMARK 3 LOOSE THERMAL 1 E (A**2): 197 ; 0.190 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 224 A 271 5
REMARK 3 1 C 224 C 271 5
REMARK 3 1 E 224 E 271 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 280 ; 0.110 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 C (A): 280 ; 0.080 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 E (A): 280 ; 0.100 ; 0.500
REMARK 3 LOOSE POSITIONAL 2 A (A): 329 ; 0.150 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 C (A): 329 ; 0.130 ; 5.000
REMARK 3 LOOSE POSITIONAL 2 E (A): 329 ; 0.160 ; 5.000
REMARK 3 MEDIUM THERMAL 2 A (A**2): 280 ; 0.320 ; 2.000
REMARK 3 MEDIUM THERMAL 2 C (A**2): 280 ; 0.270 ; 2.000
REMARK 3 MEDIUM THERMAL 2 E (A**2): 280 ; 0.320 ; 2.000
REMARK 3 LOOSE THERMAL 2 A (A**2): 329 ; 0.250 ;10.000
REMARK 3 LOOSE THERMAL 2 C (A**2): 329 ; 0.270 ;10.000
REMARK 3 LOOSE THERMAL 2 E (A**2): 329 ; 0.230 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A C E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 280 A 451 5
REMARK 3 1 C 280 C 451 5
REMARK 3 1 E 280 E 451 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 994 ; 0.090 ; 0.500
REMARK 3 MEDIUM POSITIONAL 3 C (A): 994 ; 0.090 ; 0.500
REMARK 3 MEDIUM POSITIONAL 3 E (A): 994 ; 0.090 ; 0.500
REMARK 3 LOOSE POSITIONAL 3 A (A): 1164 ; 0.170 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 C (A): 1164 ; 0.130 ; 5.000
REMARK 3 LOOSE POSITIONAL 3 E (A): 1164 ; 0.150 ; 5.000
REMARK 3 MEDIUM THERMAL 3 A (A**2): 994 ; 0.270 ; 2.000
REMARK 3 MEDIUM THERMAL 3 C (A**2): 994 ; 0.220 ; 2.000
REMARK 3 MEDIUM THERMAL 3 E (A**2): 994 ; 0.260 ; 2.000
REMARK 3 LOOSE THERMAL 3 A (A**2): 1164 ; 0.180 ;10.000
REMARK 3 LOOSE THERMAL 3 C (A**2): 1164 ; 0.190 ;10.000
REMARK 3 LOOSE THERMAL 3 E (A**2): 1164 ; 0.170 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B D F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 7 5
REMARK 3 1 D 1 D 7 5
REMARK 3 1 F 1 F 7 5
REMARK 3 2 B 11 B 32 5
REMARK 3 2 D 11 D 32 5
REMARK 3 2 F 11 F 32 5
REMARK 3 3 B 36 B 57 5
REMARK 3 3 D 36 D 57 5
REMARK 3 3 F 36 F 57 5
REMARK 3 4 B 434 B 436 5
REMARK 3 4 D 434 D 436 5
REMARK 3 4 F 434 F 436 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 316 ; 0.170 ; 0.500
REMARK 3 MEDIUM POSITIONAL 4 C (A): 316 ; 0.110 ; 0.500
REMARK 3 MEDIUM POSITIONAL 4 E (A): 316 ; 0.120 ; 0.500
REMARK 3 LOOSE POSITIONAL 4 A (A): 362 ; 0.310 ; 5.000
REMARK 3 LOOSE POSITIONAL 4 C (A): 362 ; 0.200 ; 5.000
REMARK 3 LOOSE POSITIONAL 4 E (A): 362 ; 0.200 ; 5.000
REMARK 3 MEDIUM THERMAL 4 A (A**2): 316 ; 0.160 ; 2.000
REMARK 3 MEDIUM THERMAL 4 C (A**2): 316 ; 0.170 ; 2.000
REMARK 3 MEDIUM THERMAL 4 E (A**2): 316 ; 0.140 ; 2.000
REMARK 3 LOOSE THERMAL 4 A (A**2): 362 ; 0.150 ;10.000
REMARK 3 LOOSE THERMAL 4 C (A**2): 362 ; 0.140 ;10.000
REMARK 3 LOOSE THERMAL 4 E (A**2): 362 ; 0.100 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B D F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 58 B 108 5
REMARK 3 1 D 58 D 108 5
REMARK 3 1 F 58 F 108 5
REMARK 3 2 B 353 B 433 5
REMARK 3 2 D 353 D 433 5
REMARK 3 2 F 353 F 433 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 B (A): 744 ; 0.110 ; 0.500
REMARK 3 MEDIUM POSITIONAL 5 D (A): 744 ; 0.090 ; 0.500
REMARK 3 MEDIUM POSITIONAL 5 F (A): 744 ; 0.090 ; 0.500
REMARK 3 LOOSE POSITIONAL 5 B (A): 958 ; 0.200 ; 5.000
REMARK 3 LOOSE POSITIONAL 5 D (A): 958 ; 0.210 ; 5.000
REMARK 3 LOOSE POSITIONAL 5 F (A): 958 ; 0.160 ; 5.000
REMARK 3 MEDIUM THERMAL 5 B (A**2): 744 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 5 D (A**2): 744 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 5 F (A**2): 744 ; 0.110 ; 2.000
REMARK 3 LOOSE THERMAL 5 B (A**2): 958 ; 0.100 ;10.000
REMARK 3 LOOSE THERMAL 5 D (A**2): 958 ; 0.110 ;10.000
REMARK 3 LOOSE THERMAL 5 F (A**2): 958 ; 0.110 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : B D F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 109 B 352 5
REMARK 3 1 D 109 D 352 5
REMARK 3 1 F 109 F 352 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 6 B (A): 1438 ; 0.090 ; 0.500
REMARK 3 MEDIUM POSITIONAL 6 D (A): 1438 ; 0.100 ; 0.500
REMARK 3 MEDIUM POSITIONAL 6 F (A): 1438 ; 0.090 ; 0.500
REMARK 3 LOOSE POSITIONAL 6 B (A): 1765 ; 0.180 ; 5.000
REMARK 3 LOOSE POSITIONAL 6 D (A): 1765 ; 0.200 ; 5.000
REMARK 3 LOOSE POSITIONAL 6 F (A): 1765 ; 0.210 ; 5.000
REMARK 3 MEDIUM THERMAL 6 B (A**2): 1438 ; 0.230 ; 2.000
REMARK 3 MEDIUM THERMAL 6 D (A**2): 1438 ; 0.240 ; 2.000
REMARK 3 MEDIUM THERMAL 6 F (A**2): 1438 ; 0.210 ; 2.000
REMARK 3 LOOSE THERMAL 6 B (A**2): 1765 ; 0.210 ;10.000
REMARK 3 LOOSE THERMAL 6 D (A**2): 1765 ; 0.210 ;10.000
REMARK 3 LOOSE THERMAL 6 F (A**2): 1765 ; 0.180 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : B D F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 437 B 461 5
REMARK 3 1 D 437 D 461 5
REMARK 3 1 F 437 F 461 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 7 B (A): 146 ; 0.160 ; 0.500
REMARK 3 MEDIUM POSITIONAL 7 D (A): 146 ; 0.210 ; 0.500
REMARK 3 MEDIUM POSITIONAL 7 F (A): 146 ; 0.310 ; 0.500
REMARK 3 LOOSE POSITIONAL 7 B (A): 169 ; 0.180 ; 5.000
REMARK 3 LOOSE POSITIONAL 7 D (A): 169 ; 0.260 ; 5.000
REMARK 3 LOOSE POSITIONAL 7 F (A): 169 ; 0.300 ; 5.000
REMARK 3 MEDIUM THERMAL 7 B (A**2): 146 ; 0.070 ; 2.000
REMARK 3 MEDIUM THERMAL 7 D (A**2): 146 ; 0.070 ; 2.000
REMARK 3 MEDIUM THERMAL 7 F (A**2): 146 ; 0.070 ; 2.000
REMARK 3 LOOSE THERMAL 7 B (A**2): 169 ; 0.060 ;10.000
REMARK 3 LOOSE THERMAL 7 D (A**2): 169 ; 0.060 ;10.000
REMARK 3 LOOSE THERMAL 7 F (A**2): 169 ; 0.070 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 452
REMARK 3 RESIDUE RANGE : A 2004 A 2006
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9738 329.1421 23.9453
REMARK 3 T TENSOR
REMARK 3 T11: 0.2822 T22: -0.2373
REMARK 3 T33: -0.1454 T12: -0.0559
REMARK 3 T13: 0.0378 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 0.8760 L22: 1.3721
REMARK 3 L33: 1.1353 L12: -0.1752
REMARK 3 L13: -0.2604 L23: -0.1992
REMARK 3 S TENSOR
REMARK 3 S11: 0.1265 S12: 0.1265 S13: 0.1198
REMARK 3 S21: -0.1923 S22: -0.0026 S23: -0.0685
REMARK 3 S31: -0.2483 S32: 0.0441 S33: -0.1238
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 452
REMARK 3 RESIDUE RANGE : C 2004 C 2006
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2886 287.5998 3.5237
REMARK 3 T TENSOR
REMARK 3 T11: -0.0261 T22: -0.1747
REMARK 3 T33: -0.0106 T12: 0.0074
REMARK 3 T13: -0.0993 T23: -0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 0.6219 L22: 1.8798
REMARK 3 L33: 0.6575 L12: -0.2096
REMARK 3 L13: 0.0059 L23: 0.1952
REMARK 3 S TENSOR
REMARK 3 S11: 0.0537 S12: -0.0875 S13: -0.0356
REMARK 3 S21: 0.1476 S22: 0.0227 S23: -0.3297
REMARK 3 S31: -0.0308 S32: 0.1241 S33: -0.0764
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 452
REMARK 3 RESIDUE RANGE : E 2004 E 2006
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5458 325.6202 -24.0282
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: -0.2194
REMARK 3 T33: -0.1055 T12: -0.1234
REMARK 3 T13: 0.0584 T23: -0.0688
REMARK 3 L TENSOR
REMARK 3 L11: 0.4598 L22: 1.0875
REMARK 3 L33: 1.1919 L12: 0.0033
REMARK 3 L13: 0.1113 L23: -0.2441
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.0783 S13: -0.0249
REMARK 3 S21: 0.0638 S22: 0.0047 S23: -0.0714
REMARK 3 S31: -0.2025 S32: 0.1037 S33: -0.0279
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 109 B 352
REMARK 3 RESIDUE RANGE : B 2001 B 2003
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5815 319.3215 42.2503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0855 T22: -0.2321
REMARK 3 T33: 0.0215 T12: 0.0489
REMARK 3 T13: 0.0123 T23: 0.1135
REMARK 3 L TENSOR
REMARK 3 L11: 1.3412 L22: 0.7866
REMARK 3 L33: 1.3272 L12: -0.2006
REMARK 3 L13: -0.7959 L23: -0.0762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0400 S12: 0.2563 S13: -0.1429
REMARK 3 S21: -0.0794 S22: 0.0931 S23: 0.3786
REMARK 3 S31: -0.1794 S32: -0.2880 S33: -0.0532
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 109 D 352
REMARK 3 RESIDUE RANGE : D 2001 D 2003
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5248 263.6294 -5.7713
REMARK 3 T TENSOR
REMARK 3 T11: -0.0693 T22: -0.3404
REMARK 3 T33: 0.0419 T12: 0.0291
REMARK 3 T13: -0.1137 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.3189 L22: 2.7812
REMARK 3 L33: 0.7799 L12: 0.4869
REMARK 3 L13: 0.0525 L23: 0.5071
REMARK 3 S TENSOR
REMARK 3 S11: 0.1357 S12: -0.0156 S13: -0.2119
REMARK 3 S21: 0.0681 S22: -0.1127 S23: 0.3616
REMARK 3 S31: 0.0671 S32: 0.0217 S33: -0.0230
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 109 F 352
REMARK 3 RESIDUE RANGE : F 2001 F 2003
REMARK 3 ORIGIN FOR THE GROUP (A): 63.1314 323.1791 -45.8958
REMARK 3 T TENSOR
REMARK 3 T11: 0.0314 T22: 0.2489
REMARK 3 T33: 0.1482 T12: -0.1871
REMARK 3 T13: 0.1770 T23: -0.0767
REMARK 3 L TENSOR
REMARK 3 L11: 1.1280 L22: 1.5608
REMARK 3 L33: 0.8102 L12: 0.1304
REMARK 3 L13: -0.3956 L23: -0.0535
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: 0.2596 S13: -0.0157
REMARK 3 S21: -0.2362 S22: 0.0044 S23: -0.5150
REMARK 3 S31: -0.0634 S32: 0.5422 S33: 0.0184
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 58 B 108
REMARK 3 RESIDUE RANGE : B 353 B 433
REMARK 3 ORIGIN FOR THE GROUP (A): -53.6462 340.4174 40.5821
REMARK 3 T TENSOR
REMARK 3 T11: -0.0823 T22: -0.3421
REMARK 3 T33: -0.0690 T12: 0.3006
REMARK 3 T13: 0.1142 T23: 0.3276
REMARK 3 L TENSOR
REMARK 3 L11: 9.4402 L22: 3.0206
REMARK 3 L33: 4.4383 L12: -3.0355
REMARK 3 L13: 4.3372 L23: -2.0292
REMARK 3 S TENSOR
REMARK 3 S11: -0.2892 S12: -0.5950 S13: -0.4398
REMARK 3 S21: -0.1728 S22: 0.3925 S23: 0.1849
REMARK 3 S31: 0.0005 S32: -0.2695 S33: -0.1033
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 58 D 108
REMARK 3 RESIDUE RANGE : D 353 D 433
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8454 218.6586 4.5529
REMARK 3 T TENSOR
REMARK 3 T11: -0.3477 T22: -0.4243
REMARK 3 T33: 0.0231 T12: 0.2519
REMARK 3 T13: -0.0444 T23: -0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 2.2114 L22: 9.2520
REMARK 3 L33: 5.5579 L12: -2.3639
REMARK 3 L13: 1.9626 L23: -5.3207
REMARK 3 S TENSOR
REMARK 3 S11: -0.1655 S12: -0.7329 S13: 0.2230
REMARK 3 S21: -0.2590 S22: 0.2945 S23: 1.0265
REMARK 3 S31: -0.2227 S32: 0.0992 S33: -0.1290
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 58 F 108
REMARK 3 RESIDUE RANGE : F 353 F 433
REMARK 3 ORIGIN FOR THE GROUP (A): 101.4461 349.0582 -42.0582
REMARK 3 T TENSOR
REMARK 3 T11: -0.0772 T22: -0.1712
REMARK 3 T33: 0.4928 T12: -0.2066
REMARK 3 T13: 0.1814 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 9.1226 L22: 5.2492
REMARK 3 L33: 4.1269 L12: 4.2884
REMARK 3 L13: 3.8653 L23: 3.1601
REMARK 3 S TENSOR
REMARK 3 S11: -0.5239 S12: 0.8234 S13: -0.7580
REMARK 3 S21: 0.3585 S22: 0.5835 S23: -0.9164
REMARK 3 S31: 0.4717 S32: -0.2900 S33: -0.0596
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 57
REMARK 3 RESIDUE RANGE : B 434 B 436
REMARK 3 ORIGIN FOR THE GROUP (A): -81.3268 357.5117 33.8367
REMARK 3 T TENSOR
REMARK 3 T11: -0.1812 T22: 0.0174
REMARK 3 T33: -0.1037 T12: 0.3090
REMARK 3 T13: 0.0510 T23: 0.4855
REMARK 3 L TENSOR
REMARK 3 L11: 7.0648 L22: 9.6004
REMARK 3 L33: 8.0763 L12: -1.5707
REMARK 3 L13: -2.2215 L23: 0.2923
REMARK 3 S TENSOR
REMARK 3 S11: -0.3055 S12: -0.8520 S13: -0.5806
REMARK 3 S21: 0.3156 S22: 0.2912 S23: 0.8378
REMARK 3 S31: 0.0077 S32: -0.8967 S33: 0.0143
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 57
REMARK 3 RESIDUE RANGE : D 434 D 436
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3707 188.4819 15.2911
REMARK 3 T TENSOR
REMARK 3 T11: -0.4143 T22: -0.1805
REMARK 3 T33: -0.1828 T12: 0.2800
REMARK 3 T13: -0.0730 T23: 0.3151
REMARK 3 L TENSOR
REMARK 3 L11: 9.2123 L22: 8.5314
REMARK 3 L33: 4.7646 L12: 2.7962
REMARK 3 L13: -2.3186 L23: -0.9773
REMARK 3 S TENSOR
REMARK 3 S11: 0.6355 S12: -0.7509 S13: -1.2360
REMARK 3 S21: 0.0370 S22: -0.0649 S23: -0.0280
REMARK 3 S31: 0.3084 S32: -0.1036 S33: -0.5706
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 57
REMARK 3 RESIDUE RANGE : F 434 F 436
REMARK 3 ORIGIN FOR THE GROUP (A): 126.9953 368.4969 -33.9701
REMARK 3 T TENSOR
REMARK 3 T11: -0.3835 T22: 0.0163
REMARK 3 T33: 1.0591 T12: 0.0106
REMARK 3 T13: -0.1112 T23: -0.1680
REMARK 3 L TENSOR
REMARK 3 L11: 6.3492 L22: 4.7408
REMARK 3 L33: 7.9442 L12: -0.6601
REMARK 3 L13: -0.7503 L23: 2.1612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0817 S12: -0.2841 S13: -0.4925
REMARK 3 S21: 0.3004 S22: 0.5713 S23: -1.5356
REMARK 3 S31: -0.1009 S32: 1.7743 S33: -0.6530
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 437 B 461
REMARK 3 ORIGIN FOR THE GROUP (A): -92.9542 345.9742 26.4548
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.3462
REMARK 3 T33: 0.2872 T12: 0.0701
REMARK 3 T13: 0.0467 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 3.8457 L22: 9.0251
REMARK 3 L33: 1.9436 L12: 2.0424
REMARK 3 L13: 2.3313 L23: -0.8141
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: 0.3822 S13: 0.1417
REMARK 3 S21: 0.0106 S22: -0.3310 S23: 0.6809
REMARK 3 S31: 0.3250 S32: -0.4176 S33: 0.1790
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 437 D 461
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8413 182.7272 28.6945
REMARK 3 T TENSOR
REMARK 3 T11: -0.0283 T22: 0.1720
REMARK 3 T33: 0.0463 T12: -0.0880
REMARK 3 T13: -0.0223 T23: 0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 5.8090 L22: 6.3359
REMARK 3 L33: 11.3125 L12: -3.8696
REMARK 3 L13: -0.4155 L23: -6.2350
REMARK 3 S TENSOR
REMARK 3 S11: -0.0432 S12: -0.2513 S13: -0.3565
REMARK 3 S21: 0.6283 S22: -0.1177 S23: 0.0776
REMARK 3 S31: 0.0198 S32: -0.3571 S33: 0.1608
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 437 F 461
REMARK 3 ORIGIN FOR THE GROUP (A): 139.4097 358.7966 -25.3761
REMARK 3 T TENSOR
REMARK 3 T11: 0.4865 T22: 1.1106
REMARK 3 T33: 1.5366 T12: 0.2384
REMARK 3 T13: -0.3268 T23: 0.1267
REMARK 3 L TENSOR
REMARK 3 L11: 0.2895 L22: 4.8293
REMARK 3 L33: 0.2651 L12: 1.1824
REMARK 3 L13: -0.2770 L23: -1.1315
REMARK 3 S TENSOR
REMARK 3 S11: 0.9178 S12: -0.9769 S13: 0.4618
REMARK 3 S21: 0.5165 S22: -1.1181 S23: -0.3661
REMARK 3 S31: 0.4329 S32: 0.3585 S33: 0.2003
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 3FCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050431.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9760
REMARK 200 MONOCHROMATOR : RH-COATED SI
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
REMARK 200 R SYM FOR SHELL (I) : 0.60200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2VDR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.4 M MAGNESIUM ACETATE,
REMARK 280 0.1 M SODIUM CACODYLATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K, PH 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
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
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 58.85867
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 29.42933
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 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 58.85867
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 29.42933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: HETER-DIMER
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: 5710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, I
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 B 73
REMARK 465 SER B 74
REMARK 465 GLY B 75
REMARK 465 ASP B 76
REMARK 465 SER B 77
REMARK 465 SER B 78
REMARK 465 LEU C 1
REMARK 465 VAL C 453
REMARK 465 VAL C 454
REMARK 465 LYS C 455
REMARK 465 ALA C 456
REMARK 465 SER C 457
REMARK 465 GLY D 73
REMARK 465 SER D 74
REMARK 465 GLY D 75
REMARK 465 ASP D 76
REMARK 465 SER D 77
REMARK 465 SER D 78
REMARK 465 VAL E 453
REMARK 465 VAL E 454
REMARK 465 LYS E 455
REMARK 465 ALA E 456
REMARK 465 SER E 457
REMARK 465 GLY F 73
REMARK 465 SER F 74
REMARK 465 GLY F 75
REMARK 465 ASP F 76
REMARK 465 SER F 77
REMARK 465 SER F 78
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 MG MG D 2001 O2 CAC D 462 1.66
REMARK 500 MG MG F 2001 O2 CAC F 462 1.67
REMARK 500 ND2 ASN E 15 C2 NAG E 3015 2.12
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 28 -83.51 -46.29
REMARK 500 SER A 29 75.63 -171.08
REMARK 500 HIS A 30 74.77 -154.90
REMARK 500 PRO A 45 82.99 -60.28
REMARK 500 SER A 46 -18.47 161.62
REMARK 500 GLN A 47 31.22 70.96
REMARK 500 SER A 101 -127.82 53.05
REMARK 500 LYS A 118 -123.70 54.84
REMARK 500 GLU A 123 135.38 84.04
REMARK 500 LEU A 212 -45.13 79.26
REMARK 500 SER A 261 70.55 38.67
REMARK 500 VAL A 453 -154.08 -142.11
REMARK 500 ASP B 47 35.74 -98.41
REMARK 500 ASP B 71 -140.68 -107.85
REMARK 500 VAL B 157 -74.93 -131.63
REMARK 500 GLN B 199 82.63 -68.61
REMARK 500 SER B 213 -157.59 -107.20
REMARK 500 LEU B 258 -9.34 88.26
REMARK 500 VAL B 275 -77.01 -83.50
REMARK 500 ALA B 309 78.24 -110.04
REMARK 500 CYS B 374 -154.33 -91.00
REMARK 500 LYS B 410 -75.14 67.77
REMARK 500 GLN B 440 55.31 -93.46
REMARK 500 SER C 46 -18.53 124.92
REMARK 500 SER C 81 -14.18 78.51
REMARK 500 SER C 101 -126.11 50.85
REMARK 500 LYS C 118 -121.05 55.58
REMARK 500 GLU C 123 131.76 86.10
REMARK 500 LEU C 212 -45.82 78.99
REMARK 500 ASP D 47 31.57 -95.48
REMARK 500 ASP D 71 -143.72 -107.94
REMARK 500 ASN D 148 67.95 -103.01
REMARK 500 VAL D 157 -76.48 -127.51
REMARK 500 VAL D 193 -60.32 -100.89
REMARK 500 SER D 213 -150.25 -105.00
REMARK 500 LYS D 253 -179.63 -67.91
REMARK 500 LEU D 258 -6.44 87.21
REMARK 500 VAL D 275 -75.68 -83.38
REMARK 500 CYS D 374 -153.51 -92.02
REMARK 500 LYS D 410 -72.20 70.47
REMARK 500 GLN D 440 43.26 -95.33
REMARK 500 SER E 101 -124.48 53.17
REMARK 500 LYS E 118 -125.36 54.31
REMARK 500 GLU E 123 128.64 91.23
REMARK 500 LEU E 212 -52.65 78.32
REMARK 500 SER E 261 72.22 44.75
REMARK 500 ASP F 71 -142.08 -118.34
REMARK 500 PRO F 94 122.06 -38.22
REMARK 500 VAL F 157 -76.02 -133.67
REMARK 500 SER F 213 -152.28 -110.66
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 CA A2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 243 OE1
REMARK 620 2 GLU A 243 OE2 49.3
REMARK 620 3 ASP A 245 OD2 111.6 63.6
REMARK 620 4 ASP A 247 O 76.4 78.4 104.2
REMARK 620 5 THR A 250 O 75.0 123.3 173.0 79.5
REMARK 620 6 THR A 250 OG1 153.0 146.3 92.3 85.8 81.9
REMARK 620 7 GLU A 252 OE1 77.8 69.3 67.1 147.1 113.1 125.0
REMARK 620 8 GLU A 252 OE2 117.4 115.6 78.1 164.5 96.8 78.7 48.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 297 OD1
REMARK 620 2 ASN A 299 OD1 79.8
REMARK 620 3 ASP A 301 OD1 76.5 78.6
REMARK 620 4 ARG A 303 O 76.7 155.7 101.2
REMARK 620 5 ASP A 305 OD1 134.2 105.0 149.2 87.6
REMARK 620 6 ASP A 305 OD2 92.0 77.7 155.1 97.4 47.2
REMARK 620 7 HOH A 583 O 155.1 106.1 80.9 97.8 68.6 112.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 365 OD2
REMARK 620 2 ASP A 367 OD1 88.0
REMARK 620 3 ASP A 369 OD1 80.9 80.8
REMARK 620 4 TYR A 371 O 73.1 160.6 91.4
REMARK 620 5 ASP A 373 OD1 96.2 93.3 173.5 93.3
REMARK 620 6 ASP A 373 OD2 129.4 121.8 138.5 75.5 47.5
REMARK 620 7 HOH A 512 O 146.4 106.3 72.0 87.9 112.7 68.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 426 OD1
REMARK 620 2 ASP A 428 OD1 92.6
REMARK 620 3 ASN A 430 OD1 87.7 88.4
REMARK 620 4 TYR A 432 O 79.1 171.6 92.8
REMARK 620 5 ASP A 434 OD1 95.6 84.5 172.3 94.6
REMARK 620 6 ASP A 434 OD2 137.6 101.8 131.8 83.5 47.5
REMARK 620 7 HOH A 589 O 159.3 70.0 80.8 118.4 93.9 60.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 458 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 467 O
REMARK 620 2 HOH C 468 O 136.4
REMARK 620 3 HOH C 470 O 67.7 146.4
REMARK 620 4 HOH C 472 O 70.0 81.1 90.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 478 O
REMARK 620 2 ASP E 297 OD1 161.3
REMARK 620 3 ASN E 299 OD1 83.5 85.3
REMARK 620 4 ASP E 301 OD1 78.4 84.9 79.3
REMARK 620 5 ARG E 303 O 99.3 91.1 175.7 97.9
REMARK 620 6 ASP E 305 OD1 56.4 141.3 103.3 133.5 81.0
REMARK 620 7 ASP E 305 OD2 98.6 95.9 88.3 167.5 94.5 47.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 523 O
REMARK 620 2 ASP E 426 OD1 146.3
REMARK 620 3 ASP E 428 OD1 70.6 80.4
REMARK 620 4 ASN E 430 OD1 76.2 83.6 82.8
REMARK 620 5 TYR E 432 O 130.2 76.7 157.1 92.6
REMARK 620 6 ASP E 434 OD1 101.7 91.1 82.7 165.3 99.6
REMARK 620 7 ASP E 434 OD2 69.4 136.6 104.5 139.5 93.5 48.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 550 O
REMARK 620 2 HOH A 590 O 108.3
REMARK 620 3 SER B 123 O 85.8 146.5
REMARK 620 4 ASP B 126 OD1 104.7 128.4 73.1
REMARK 620 5 ASP B 127 OD1 161.1 71.3 85.6 88.9
REMARK 620 6 ASP B 251 OD2 79.7 77.8 75.0 147.4 81.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 582 O
REMARK 620 2 ASP C 297 OD1 160.2
REMARK 620 3 ASN C 299 OD1 86.9 82.2
REMARK 620 4 ASP C 301 OD1 80.7 81.1 79.6
REMARK 620 5 ARG C 303 O 105.7 83.6 165.5 95.1
REMARK 620 6 ASP C 305 OD1 62.4 137.0 109.2 140.9 83.5
REMARK 620 7 ASP C 305 OD2 102.9 92.9 86.3 165.3 97.5 48.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 584 O
REMARK 620 2 HOH A 585 O 91.3
REMARK 620 3 SER D 123 O 147.4 93.0
REMARK 620 4 ASP D 126 OD1 133.5 114.0 72.8
REMARK 620 5 ASP D 127 OD1 72.4 146.2 86.6 98.1
REMARK 620 6 ASP D 251 OD2 79.4 68.8 72.2 145.0 79.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 586 O
REMARK 620 2 ASP E 365 OD2 149.1
REMARK 620 3 ASP E 367 OD1 104.1 81.1
REMARK 620 4 ASP E 369 OD1 72.3 80.0 75.3
REMARK 620 5 TYR E 371 O 87.3 78.8 156.4 89.1
REMARK 620 6 ASP E 373 OD1 109.3 100.7 92.8 167.9 102.9
REMARK 620 7 ASP E 373 OD2 67.4 134.3 125.4 137.9 77.9 48.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 587 O
REMARK 620 2 HOH A 588 O 130.1
REMARK 620 3 SER F 123 O 68.8 157.1
REMARK 620 4 ASP F 126 OD1 85.7 121.5 66.9
REMARK 620 5 ASP F 127 OD1 157.5 70.2 89.3 90.5
REMARK 620 6 ASP F 251 OD2 85.5 91.9 75.5 141.9 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 591 O
REMARK 620 2 ASP C 365 OD2 152.3
REMARK 620 3 ASP C 367 OD1 97.0 88.7
REMARK 620 4 ASP C 369 OD1 68.5 86.7 77.0
REMARK 620 5 TYR C 371 O 92.1 77.9 165.0 95.5
REMARK 620 6 ASP C 373 OD1 111.3 95.8 89.1 165.9 98.6
REMARK 620 7 ASP C 373 OD2 70.8 129.4 118.6 137.9 75.6 47.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 592 O
REMARK 620 2 ASP C 426 OD1 148.3
REMARK 620 3 ASP C 428 OD1 67.0 82.0
REMARK 620 4 ASN C 430 OD1 83.4 87.4 84.7
REMARK 620 5 TYR C 432 O 130.9 80.4 161.9 99.0
REMARK 620 6 ASP C 434 OD1 89.5 90.4 77.9 162.6 97.7
REMARK 620 7 ASP C 434 OD2 61.4 134.7 100.5 137.8 88.7 47.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 458 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 605 O
REMARK 620 2 HOH C 473 O 151.1
REMARK 620 3 HOH C 474 O 77.0 124.2
REMARK 620 4 HOH C 475 O 84.0 80.5 153.5
REMARK 620 5 HOH C 477 O 84.2 116.6 80.0 79.8
REMARK 620 6 HOH C 478 O 81.3 83.0 81.0 114.4 158.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 458 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 607 O
REMARK 620 2 HOH A 608 O 75.2
REMARK 620 3 HOH C 484 O 136.8 71.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 121 OG
REMARK 620 2 SER B 123 OG 104.9
REMARK 620 3 GLU B 220 OE1 77.6 167.1
REMARK 620 4 HOH C 463 O 78.9 82.8 85.3
REMARK 620 5 HOH C 464 O 155.9 88.4 85.2 83.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 158 OD2
REMARK 620 2 ASN B 215 OD1 101.4
REMARK 620 3 ASP B 217 O 160.2 89.4
REMARK 620 4 ASP B 217 OD1 91.0 85.5 73.2
REMARK 620 5 PRO B 219 O 85.0 173.5 84.2 93.8
REMARK 620 6 GLU B 220 OE2 104.7 91.9 91.3 164.3 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 243 OE1
REMARK 620 2 GLU C 243 OE2 51.9
REMARK 620 3 ASP C 245 OD2 119.2 67.6
REMARK 620 4 ASP C 247 O 76.0 80.5 101.1
REMARK 620 5 THR C 250 O 71.9 123.7 168.6 83.4
REMARK 620 6 THR C 250 OG1 146.4 145.3 88.3 80.2 82.2
REMARK 620 7 GLU C 252 OE1 85.3 77.6 76.5 157.1 103.4 122.1
REMARK 620 8 GLU C 252 OE2 129.7 119.1 73.6 153.5 97.6 73.8 48.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 459 O
REMARK 620 2 HOH C 460 O 88.5
REMARK 620 3 SER D 121 OG 77.7 157.3
REMARK 620 4 SER D 123 OG 85.3 91.8 104.7
REMARK 620 5 GLU D 220 OE1 94.1 81.0 82.1 172.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 465 O
REMARK 620 2 HOH C 466 O 89.9
REMARK 620 3 SER F 121 OG 73.8 160.0
REMARK 620 4 SER F 123 OG 83.0 88.3 100.8
REMARK 620 5 GLU F 220 OE1 93.5 85.6 83.9 173.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 158 OD2
REMARK 620 2 ASN D 215 OD1 100.4
REMARK 620 3 ASP D 217 O 163.2 95.2
REMARK 620 4 ASP D 217 OD1 100.5 89.5 73.4
REMARK 620 5 PRO D 219 O 84.9 171.2 80.4 96.4
REMARK 620 6 GLU D 220 OE2 97.4 87.8 89.3 162.1 84.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 243 OE1
REMARK 620 2 GLU E 243 OE2 50.5
REMARK 620 3 ASP E 245 OD2 119.7 70.1
REMARK 620 4 ASP E 247 O 74.9 75.5 101.3
REMARK 620 5 THR E 250 O 71.3 121.5 168.1 85.5
REMARK 620 6 THR E 250 OG1 144.7 150.5 92.5 85.4 78.3
REMARK 620 7 GLU E 252 OE1 81.7 77.0 76.1 151.4 102.5 123.0
REMARK 620 8 GLU E 252 OE2 123.5 122.1 77.9 159.6 92.3 74.3 48.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 158 OD2
REMARK 620 2 ASN F 215 OD1 104.2
REMARK 620 3 ASP F 217 O 159.2 92.7
REMARK 620 4 ASP F 217 OD1 94.5 87.9 73.7
REMARK 620 5 PRO F 219 O 85.6 169.5 78.6 95.2
REMARK 620 6 GLU F 220 OE2 101.2 89.4 90.9 164.2 84.9
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VDO RELATED DB: PDB
REMARK 900 RELATED ID: 2VDP RELATED DB: PDB
REMARK 900 RELATED ID: 2VDQ RELATED DB: PDB
REMARK 900 RELATED ID: 2VDR RELATED DB: PDB
REMARK 900 RELATED ID: 1TYE RELATED DB: PDB
REMARK 900 RELATED ID: 3FCS RELATED DB: PDB
DBREF 3FCU A 1 457 UNP Q17R67 Q17R67_HUMAN 32 488
DBREF 3FCU B 1 461 UNP P05106 ITB3_HUMAN 27 487
DBREF 3FCU C 1 457 UNP Q17R67 Q17R67_HUMAN 32 488
DBREF 3FCU D 1 461 UNP P05106 ITB3_HUMAN 27 487
DBREF 3FCU E 1 457 UNP Q17R67 Q17R67_HUMAN 32 488
DBREF 3FCU F 1 461 UNP P05106 ITB3_HUMAN 27 487
SEQRES 1 A 457 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 A 457 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 A 457 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 A 457 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 A 457 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 A 457 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 A 457 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 A 457 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 A 457 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 A 457 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 A 457 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 A 457 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 A 457 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 A 457 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 A 457 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 A 457 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 A 457 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 A 457 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 A 457 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 A 457 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 A 457 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 A 457 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 A 457 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 A 457 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 A 457 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 A 457 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 A 457 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 A 457 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 A 457 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 A 457 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 A 457 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 A 457 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 A 457 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 A 457 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 A 457 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 A 457 ALA SER
SEQRES 1 B 461 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 461 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 461 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 461 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 461 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 461 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 461 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 461 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 461 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 461 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 461 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 461 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 461 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 461 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 461 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 461 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 461 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 461 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 461 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 461 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 461 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 461 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 461 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 461 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 461 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 461 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 461 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 461 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 461 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 461 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 461 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 461 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 461 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 461 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 B 461 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 B 461 GLU CYS GLY VAL CYS ARG
SEQRES 1 C 457 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 C 457 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 C 457 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 C 457 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 C 457 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 C 457 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 C 457 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 C 457 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 C 457 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 C 457 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 C 457 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 C 457 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 C 457 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 C 457 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 C 457 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 C 457 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 C 457 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 C 457 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 C 457 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 C 457 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 C 457 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 C 457 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 C 457 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 C 457 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 C 457 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 C 457 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 C 457 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 C 457 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 C 457 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 C 457 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 C 457 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 C 457 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 C 457 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 C 457 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 C 457 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 C 457 ALA SER
SEQRES 1 D 461 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 D 461 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 D 461 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 D 461 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 D 461 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 D 461 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 D 461 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 D 461 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 D 461 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 D 461 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 D 461 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 D 461 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 D 461 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 D 461 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 D 461 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 D 461 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 D 461 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 D 461 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 D 461 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 D 461 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 D 461 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 D 461 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 D 461 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 D 461 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 D 461 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 D 461 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 D 461 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 D 461 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 D 461 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 D 461 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 D 461 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 D 461 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 D 461 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 D 461 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 D 461 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 D 461 GLU CYS GLY VAL CYS ARG
SEQRES 1 E 457 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 E 457 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 E 457 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 E 457 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 E 457 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 E 457 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 E 457 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 E 457 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 E 457 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 E 457 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 E 457 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 E 457 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 E 457 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 E 457 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 E 457 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 E 457 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 E 457 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 E 457 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 E 457 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 E 457 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 E 457 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 E 457 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 E 457 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 E 457 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 E 457 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 E 457 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 E 457 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 E 457 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 E 457 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 E 457 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 E 457 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 E 457 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 E 457 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 E 457 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 E 457 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 E 457 ALA SER
SEQRES 1 F 461 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 F 461 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 F 461 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 F 461 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 F 461 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 F 461 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 F 461 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 F 461 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 F 461 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 F 461 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 F 461 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 F 461 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 F 461 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 F 461 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 F 461 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 F 461 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 F 461 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 F 461 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 F 461 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 F 461 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 F 461 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 F 461 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 F 461 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 F 461 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 F 461 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 F 461 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 F 461 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 F 461 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 F 461 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 F 461 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 F 461 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 F 461 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 F 461 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 F 461 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 F 461 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 F 461 GLU CYS GLY VAL CYS ARG
MODRES 3FCU ASN A 15 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN B 99 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN B 320 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN B 371 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN C 15 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN D 99 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN D 320 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN D 371 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN E 15 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN F 320 ASN GLYCOSYLATION SITE
MODRES 3FCU ASN F 371 ASN GLYCOSYLATION SITE
HET NAG G 1 14
HET NAG G 2 14
HET MAN G 3 11
HET MAN G 4 11
HET MAN G 5 11
HET NAG H 1 14
HET NAG H 2 14
HET MAN H 3 11
HET MAN H 4 11
HET NAG I 1 14
HET NAG I 2 14
HET MAN I 3 11
HET MAN I 4 11
HET MAN I 5 11
HET CA A2004 1
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET NAG A3015 14
HET MG A 458 1
HET MG B2001 1
HET CA B2002 1
HET CA B2003 1
HET NAG B3099 14
HET NAG B3371 14
HET CAC B 462 5
HET CA C2004 1
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET NAG C3015 14
HET MG C 458 1
HET MG D2001 1
HET CA D2002 1
HET CA D2003 1
HET NAG D3099 14
HET NAG D3371 14
HET CAC D 462 5
HET CA E2004 1
HET CA E2005 1
HET CA E2006 1
HET CA E2007 1
HET NAG E3015 14
HET MG E 458 1
HET MG F2001 1
HET CA F2002 1
HET CA F2003 1
HET NAG F3371 14
HET CAC F 462 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM CAC CACODYLATE 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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN CAC DIMETHYLARSINATE
FORMUL 7 NAG 14(C8 H15 N O6)
FORMUL 7 MAN 8(C6 H12 O6)
FORMUL 10 CA 18(CA 2+)
FORMUL 15 MG 6(MG 2+)
FORMUL 21 CAC 3(C2 H6 AS O2 1-)
FORMUL 45 HOH *298(H2 O)
HELIX 1 1 LEU A 151 ASP A 159 1 9
HELIX 2 2 GLY A 187 LEU A 192 1 6
HELIX 3 3 VAL A 200 TYR A 207 1 8
HELIX 4 4 ASN A 227 PHE A 231 5 5
HELIX 5 5 THR A 259 LEU A 264 1 6
HELIX 6 6 ALA A 318 ARG A 320 5 3
HELIX 7 7 TYR A 440 ALA A 442 5 3
HELIX 8 8 ASN B 3 ARG B 8 1 6
HELIX 9 9 SER B 12 SER B 20 1 9
HELIX 10 10 LEU B 40 ASP B 47 1 8
HELIX 11 11 ALA B 50 GLU B 52 5 3
HELIX 12 12 SER B 121 ASP B 126 5 6
HELIX 13 13 ASP B 127 LYS B 144 1 18
HELIX 14 14 PRO B 169 ASN B 175 1 7
HELIX 15 15 CYS B 177 LYS B 181 5 5
HELIX 16 16 GLN B 199 LYS B 209 1 11
HELIX 17 17 GLY B 221 CYS B 232 1 12
HELIX 18 18 CYS B 232 GLY B 237 1 6
HELIX 19 19 LEU B 258 GLY B 264 5 7
HELIX 20 20 SER B 291 LYS B 302 1 12
HELIX 21 21 VAL B 314 ILE B 325 1 12
HELIX 22 22 SER B 337 GLY B 349 1 13
HELIX 23 23 CYS B 435 ALA B 439 5 5
HELIX 24 24 LEU C 151 ASP C 159 1 9
HELIX 25 25 GLY C 187 LEU C 192 1 6
HELIX 26 26 VAL C 200 TYR C 207 1 8
HELIX 27 27 ASN C 227 PHE C 231 5 5
HELIX 28 28 THR C 259 LEU C 264 1 6
HELIX 29 29 ALA C 318 ARG C 320 5 3
HELIX 30 30 TYR C 440 ALA C 442 5 3
HELIX 31 31 CYS D 5 GLY D 9 5 5
HELIX 32 32 SER D 12 SER D 20 1 9
HELIX 33 33 LEU D 40 ASP D 47 1 8
HELIX 34 34 ALA D 50 GLU D 52 5 3
HELIX 35 35 SER D 121 LYS D 125 5 5
HELIX 36 36 ASP D 127 LYS D 144 1 18
HELIX 37 37 PRO D 170 ASN D 175 1 6
HELIX 38 38 CYS D 177 LYS D 181 5 5
HELIX 39 39 GLN D 199 LYS D 209 1 11
HELIX 40 40 GLY D 221 CYS D 232 1 12
HELIX 41 41 CYS D 232 GLY D 237 1 6
HELIX 42 42 ASP D 259 GLY D 264 5 6
HELIX 43 43 SER D 291 LYS D 302 1 12
HELIX 44 44 VAL D 314 LEU D 324 1 11
HELIX 45 45 SER D 337 GLY D 349 1 13
HELIX 46 46 CYS D 435 ALA D 439 5 5
HELIX 47 47 GLY E 44 GLU E 48 5 5
HELIX 48 48 LEU E 151 ASP E 159 1 9
HELIX 49 49 GLY E 187 LEU E 192 1 6
HELIX 50 50 VAL E 200 TYR E 207 1 8
HELIX 51 51 ASN E 227 PHE E 231 5 5
HELIX 52 52 THR E 259 LEU E 264 1 6
HELIX 53 53 ALA E 318 ARG E 320 5 3
HELIX 54 54 ASN F 3 ARG F 8 1 6
HELIX 55 55 SER F 12 SER F 20 1 9
HELIX 56 56 LEU F 40 ASP F 47 1 8
HELIX 57 57 SER F 121 ASP F 126 5 6
HELIX 58 58 ASP F 127 THR F 146 1 20
HELIX 59 59 PRO F 169 ASN F 175 1 7
HELIX 60 60 CYS F 177 LYS F 181 5 5
HELIX 61 61 GLN F 199 GLN F 210 1 12
HELIX 62 62 GLY F 221 CYS F 232 1 12
HELIX 63 63 CYS F 232 GLY F 237 1 6
HELIX 64 64 LEU F 258 GLY F 264 5 7
HELIX 65 65 SER F 291 LYS F 302 1 12
HELIX 66 66 VAL F 314 ILE F 325 1 12
HELIX 67 67 SER F 337 GLY F 349 1 13
HELIX 68 68 CYS F 435 ALA F 439 5 5
SHEET 1 A 5 GLY A 62 GLY A 63 0
SHEET 2 A 5 THR A 9 ALA A 12 1 N ALA A 12 O GLY A 63
SHEET 3 A 5 GLN A 444 TYR A 448 -1 O VAL A 447 N THR A 9
SHEET 4 A 5 ASP A 434 ALA A 439 -1 N LEU A 435 O TYR A 448
SHEET 5 A 5 SER A 420 VAL A 425 -1 N ARG A 422 O ILE A 436
SHEET 1 B 4 LEU A 23 LYS A 27 0
SHEET 2 B 4 VAL A 33 ALA A 39 -1 O ALA A 34 N HIS A 26
SHEET 3 B 4 GLY A 52 PRO A 57 -1 O CYS A 56 N ILE A 35
SHEET 4 B 4 SER A 67 LEU A 68 -1 O LEU A 68 N VAL A 53
SHEET 1 C 4 GLU A 75 VAL A 79 0
SHEET 2 C 4 GLN A 82 PHE A 87 -1 O LEU A 84 N ARG A 77
SHEET 3 C 4 HIS A 112 GLU A 117 -1 O ASN A 114 N GLN A 85
SHEET 4 C 4 GLU A 120 GLU A 121 -1 O GLU A 120 N GLU A 117
SHEET 1 D 4 VAL A 97 TRP A 100 0
SHEET 2 D 4 VAL A 103 ALA A 108 -1 O VAL A 105 N VAL A 98
SHEET 3 D 4 SER A 129 GLN A 134 -1 O PHE A 131 N ALA A 106
SHEET 4 D 4 ARG A 139 TYR A 143 -1 O ALA A 141 N LEU A 132
SHEET 1 E 4 SER A 173 VAL A 175 0
SHEET 2 E 4 GLU A 180 ALA A 185 -1 O VAL A 182 N VAL A 174
SHEET 3 E 4 LEU A 194 PRO A 199 -1 O ALA A 196 N LEU A 183
SHEET 4 E 4 SER A 220 LEU A 221 -1 O SER A 220 N GLN A 197
SHEET 1 F 4 VAL A 239 GLY A 242 0
SHEET 2 F 4 GLU A 252 ALA A 257 -1 O VAL A 254 N ALA A 240
SHEET 3 F 4 ALA A 266 LEU A 270 -1 O ALA A 266 N ALA A 257
SHEET 4 F 4 ARG A 276 ARG A 281 -1 O LEU A 277 N ILE A 269
SHEET 1 G 4 VAL A 293 THR A 296 0
SHEET 2 G 4 ASP A 305 ALA A 310 -1 O LEU A 307 N ALA A 294
SHEET 3 G 4 ARG A 327 PHE A 331 -1 O ARG A 327 N ALA A 310
SHEET 4 G 4 LEU A 345 THR A 348 -1 O LEU A 347 N VAL A 328
SHEET 1 H 2 MET A 314 ARG A 317 0
SHEET 2 H 2 LYS A 321 GLU A 324 -1 O ALA A 323 N GLU A 315
SHEET 1 I 4 ILE A 360 GLY A 364 0
SHEET 2 I 4 ASP A 373 ALA A 378 -1 O ASP A 373 N GLY A 364
SHEET 3 I 4 GLN A 388 PHE A 392 -1 O GLN A 388 N ALA A 378
SHEET 4 I 4 GLN A 405 ASP A 408 -1 O LEU A 407 N VAL A 389
SHEET 1 J 2 GLY A 394 GLN A 395 0
SHEET 2 J 2 GLY A 398 LEU A 399 -1 O GLY A 398 N GLN A 395
SHEET 1 K 3 CYS B 38 ASP B 39 0
SHEET 2 K 3 ALA B 24 CYS B 26 -1 N ALA B 24 O ASP B 39
SHEET 3 K 3 ILE B 54 GLU B 55 -1 O GLU B 55 N TRP B 25
SHEET 1 L 6 GLU B 60 GLU B 65 0
SHEET 2 L 6 ARG B 87 LEU B 92 -1 O ARG B 91 N GLU B 60
SHEET 3 L 6 LEU B 425 PHE B 431 1 O GLN B 428 N LEU B 90
SHEET 4 L 6 LYS B 412 PRO B 418 -1 N PHE B 414 O VAL B 427
SHEET 5 L 6 SER B 353 ARG B 360 -1 N ARG B 360 O THR B 415
SHEET 6 L 6 SER B 385 LEU B 389 -1 O LEU B 389 N SER B 353
SHEET 1 M 5 VAL B 83 SER B 84 0
SHEET 2 M 5 SER B 97 ARG B 105 -1 O GLN B 103 N SER B 84
SHEET 3 M 5 THR B 394 VAL B 403 -1 O ILE B 399 N PHE B 100
SHEET 4 M 5 LEU B 366 THR B 373 -1 N THR B 373 O SER B 396
SHEET 5 M 5 VAL B 379 PRO B 381 -1 O ILE B 380 N ALA B 372
SHEET 1 N 6 TYR B 190 THR B 197 0
SHEET 2 N 6 LEU B 149 PHE B 156 -1 N ALA B 155 O LYS B 191
SHEET 3 N 6 VAL B 112 ASP B 119 1 N MET B 118 O GLY B 154
SHEET 4 N 6 SER B 243 THR B 250 1 O LEU B 245 N ASP B 113
SHEET 5 N 6 ILE B 304 VAL B 310 1 O ALA B 309 N PHE B 248
SHEET 6 N 6 THR B 329 VAL B 332 1 O GLY B 331 N PHE B 308
SHEET 1 O 2 PHE B 455 GLU B 456 0
SHEET 2 O 2 VAL B 459 CYS B 460 -1 O VAL B 459 N GLU B 456
SHEET 1 P 5 GLY C 63 GLN C 64 0
SHEET 2 P 5 LEU C 3 ALA C 12 1 N ALA C 12 O GLY C 63
SHEET 3 P 5 GLN C 444 ALA C 450 -1 O ARG C 449 N ASP C 4
SHEET 4 P 5 ASP C 434 ALA C 439 -1 N LEU C 435 O TYR C 448
SHEET 5 P 5 SER C 420 VAL C 425 -1 N ARG C 422 O ILE C 436
SHEET 1 Q 4 LEU C 23 LYS C 27 0
SHEET 2 Q 4 VAL C 33 ALA C 39 -1 O ALA C 34 N HIS C 26
SHEET 3 Q 4 GLY C 52 PRO C 57 -1 O CYS C 56 N ILE C 35
SHEET 4 Q 4 SER C 67 LEU C 68 -1 O LEU C 68 N VAL C 53
SHEET 1 R 4 GLU C 75 VAL C 79 0
SHEET 2 R 4 GLN C 82 PHE C 87 -1 O LEU C 84 N ARG C 77
SHEET 3 R 4 HIS C 112 GLU C 117 -1 O HIS C 112 N PHE C 87
SHEET 4 R 4 GLU C 120 GLU C 121 -1 O GLU C 120 N GLU C 117
SHEET 1 S 4 VAL C 97 TRP C 100 0
SHEET 2 S 4 VAL C 103 ALA C 108 -1 O VAL C 105 N VAL C 98
SHEET 3 S 4 SER C 129 ALA C 133 -1 O PHE C 131 N ALA C 106
SHEET 4 S 4 ARG C 140 TYR C 143 -1 O ALA C 141 N LEU C 132
SHEET 1 T 4 SER C 172 VAL C 175 0
SHEET 2 T 4 GLU C 180 ALA C 185 -1 O GLY C 184 N SER C 172
SHEET 3 T 4 LEU C 194 PRO C 199 -1 O ALA C 196 N LEU C 183
SHEET 4 T 4 SER C 220 LEU C 221 -1 O SER C 220 N GLN C 197
SHEET 1 U 4 VAL C 239 GLY C 242 0
SHEET 2 U 4 GLU C 252 ALA C 257 -1 O VAL C 254 N ALA C 240
SHEET 3 U 4 ALA C 266 ASP C 271 -1 O ALA C 266 N ALA C 257
SHEET 4 U 4 ARG C 276 ARG C 281 -1 O LEU C 277 N ILE C 269
SHEET 1 V 4 VAL C 293 THR C 296 0
SHEET 2 V 4 ASP C 305 ALA C 310 -1 O LEU C 307 N ALA C 294
SHEET 3 V 4 ARG C 327 PHE C 331 -1 O PHE C 331 N LEU C 306
SHEET 4 V 4 LEU C 345 THR C 348 -1 O LEU C 347 N VAL C 328
SHEET 1 W 2 MET C 314 ARG C 317 0
SHEET 2 W 2 LYS C 321 GLU C 324 -1 O ALA C 323 N GLU C 315
SHEET 1 X 4 ILE C 360 GLY C 364 0
SHEET 2 X 4 ASP C 373 ALA C 378 -1 O ASP C 373 N GLY C 364
SHEET 3 X 4 GLN C 388 PHE C 392 -1 O GLN C 388 N ALA C 378
SHEET 4 X 4 GLN C 405 ASP C 408 -1 O LEU C 407 N VAL C 389
SHEET 1 Y 2 GLY C 394 GLN C 395 0
SHEET 2 Y 2 GLY C 398 LEU C 399 -1 O GLY C 398 N GLN C 395
SHEET 1 Z 3 CYS D 38 ASP D 39 0
SHEET 2 Z 3 ALA D 24 CYS D 26 -1 N ALA D 24 O ASP D 39
SHEET 3 Z 3 ILE D 54 GLU D 55 -1 O GLU D 55 N TRP D 25
SHEET 1 AA 6 GLU D 60 GLU D 65 0
SHEET 2 AA 6 ARG D 87 LEU D 92 -1 O ALA D 89 N ARG D 62
SHEET 3 AA 6 LEU D 425 PHE D 431 1 O GLN D 428 N LEU D 90
SHEET 4 AA 6 LYS D 412 PRO D 418 -1 N ILE D 416 O LEU D 425
SHEET 5 AA 6 SER D 353 ARG D 360 -1 N ARG D 360 O THR D 415
SHEET 6 AA 6 SER D 385 LEU D 389 -1 O CYS D 386 N VAL D 355
SHEET 1 AB 5 VAL D 83 SER D 84 0
SHEET 2 AB 5 SER D 97 ARG D 105 -1 O GLN D 103 N SER D 84
SHEET 3 AB 5 THR D 394 VAL D 403 -1 O VAL D 395 N VAL D 104
SHEET 4 AB 5 LEU D 366 THR D 373 -1 N THR D 373 O SER D 396
SHEET 5 AB 5 VAL D 379 PRO D 381 -1 O ILE D 380 N ALA D 372
SHEET 1 AC 6 TYR D 190 THR D 197 0
SHEET 2 AC 6 LEU D 149 PHE D 156 -1 N ALA D 155 O LYS D 191
SHEET 3 AC 6 VAL D 112 ASP D 119 1 N MET D 118 O GLY D 154
SHEET 4 AC 6 SER D 243 THR D 250 1 O LEU D 245 N ASP D 113
SHEET 5 AC 6 ILE D 304 VAL D 310 1 O ALA D 309 N PHE D 248
SHEET 6 AC 6 THR D 329 VAL D 332 1 O THR D 329 N PHE D 308
SHEET 1 AD 2 PHE D 455 GLU D 456 0
SHEET 2 AD 2 VAL D 459 CYS D 460 -1 O VAL D 459 N GLU D 456
SHEET 1 AE 5 GLY E 63 GLN E 64 0
SHEET 2 AE 5 THR E 9 ALA E 12 1 N PHE E 10 O GLY E 63
SHEET 3 AE 5 GLN E 444 TYR E 448 -1 O VAL E 447 N THR E 9
SHEET 4 AE 5 ASP E 434 ALA E 439 -1 N LEU E 435 O TYR E 448
SHEET 5 AE 5 SER E 420 VAL E 425 -1 N ARG E 422 O ILE E 436
SHEET 1 AF 3 LEU E 23 LYS E 27 0
SHEET 2 AF 3 VAL E 33 ALA E 39 -1 O ALA E 34 N HIS E 26
SHEET 3 AF 3 GLY E 52 PRO E 57 -1 O CYS E 56 N ILE E 35
SHEET 1 AG 4 THR E 76 VAL E 79 0
SHEET 2 AG 4 GLN E 82 PHE E 87 -1 O LEU E 84 N ARG E 77
SHEET 3 AG 4 HIS E 112 GLU E 117 -1 O HIS E 112 N PHE E 87
SHEET 4 AG 4 GLU E 120 GLU E 121 -1 O GLU E 120 N GLU E 117
SHEET 1 AH 4 VAL E 97 TRP E 100 0
SHEET 2 AH 4 VAL E 103 ALA E 108 -1 O VAL E 105 N VAL E 98
SHEET 3 AH 4 SER E 129 GLN E 134 -1 O SER E 129 N ALA E 108
SHEET 4 AH 4 ARG E 139 TYR E 143 -1 O ALA E 141 N LEU E 132
SHEET 1 AI 4 SER E 173 VAL E 175 0
SHEET 2 AI 4 GLU E 180 ALA E 185 -1 O VAL E 182 N VAL E 174
SHEET 3 AI 4 LEU E 194 PRO E 199 -1 O ALA E 196 N LEU E 183
SHEET 4 AI 4 SER E 220 LEU E 221 -1 O SER E 220 N GLN E 197
SHEET 1 AJ 4 VAL E 239 GLY E 242 0
SHEET 2 AJ 4 GLU E 252 ALA E 257 -1 O VAL E 254 N ALA E 240
SHEET 3 AJ 4 ALA E 266 LEU E 270 -1 O ALA E 266 N ALA E 257
SHEET 4 AJ 4 ARG E 276 ARG E 281 -1 O LEU E 277 N ILE E 269
SHEET 1 AK 4 VAL E 293 THR E 296 0
SHEET 2 AK 4 ASP E 305 ALA E 310 -1 O LEU E 307 N ALA E 294
SHEET 3 AK 4 ARG E 327 PHE E 331 -1 O ARG E 327 N ALA E 310
SHEET 4 AK 4 LEU E 345 THR E 348 -1 O LEU E 347 N VAL E 328
SHEET 1 AL 2 MET E 314 SER E 316 0
SHEET 2 AL 2 LEU E 322 GLU E 324 -1 O ALA E 323 N GLU E 315
SHEET 1 AM 4 ILE E 360 GLY E 364 0
SHEET 2 AM 4 ASP E 373 ALA E 378 -1 O ASP E 373 N GLY E 364
SHEET 3 AM 4 GLN E 388 PHE E 392 -1 O GLN E 388 N ALA E 378
SHEET 4 AM 4 GLN E 405 ASP E 408 -1 O LEU E 407 N VAL E 389
SHEET 1 AN 2 GLY E 394 GLN E 395 0
SHEET 2 AN 2 GLY E 398 LEU E 399 -1 O GLY E 398 N GLN E 395
SHEET 1 AO 3 CYS F 38 ASP F 39 0
SHEET 2 AO 3 ALA F 24 CYS F 26 -1 N ALA F 24 O ASP F 39
SHEET 3 AO 3 ILE F 54 GLU F 55 -1 O GLU F 55 N TRP F 25
SHEET 1 AP 6 GLU F 60 GLU F 65 0
SHEET 2 AP 6 ARG F 87 LEU F 92 -1 O ALA F 89 N ARG F 62
SHEET 3 AP 6 LEU F 425 PHE F 431 1 O THR F 430 N LEU F 90
SHEET 4 AP 6 LYS F 412 PRO F 418 -1 N PHE F 414 O VAL F 427
SHEET 5 AP 6 SER F 353 ARG F 360 -1 N ARG F 360 O THR F 415
SHEET 6 AP 6 SER F 385 LEU F 389 -1 O CYS F 386 N VAL F 355
SHEET 1 AQ 5 VAL F 83 SER F 84 0
SHEET 2 AQ 5 SER F 97 ARG F 105 -1 O GLN F 103 N SER F 84
SHEET 3 AQ 5 THR F 394 VAL F 403 -1 O ILE F 399 N PHE F 100
SHEET 4 AQ 5 LEU F 366 THR F 373 -1 N THR F 373 O SER F 396
SHEET 5 AQ 5 VAL F 379 PRO F 381 -1 O ILE F 380 N ALA F 372
SHEET 1 AR 6 TYR F 190 THR F 197 0
SHEET 2 AR 6 LEU F 149 PHE F 156 -1 N ALA F 155 O LYS F 191
SHEET 3 AR 6 VAL F 112 ASP F 119 1 N MET F 118 O GLY F 154
SHEET 4 AR 6 SER F 243 THR F 250 1 O LEU F 245 N ASP F 113
SHEET 5 AR 6 ILE F 304 VAL F 310 1 O ALA F 309 N PHE F 248
SHEET 6 AR 6 THR F 329 VAL F 332 1 O GLY F 331 N PHE F 308
SSBOND 1 CYS A 56 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.05
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.03
SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.03
SSBOND 5 CYS B 13 CYS B 435 1555 1555 2.03
SSBOND 6 CYS B 16 CYS B 38 1555 1555 2.03
SSBOND 7 CYS B 26 CYS B 49 1555 1555 2.04
SSBOND 8 CYS B 177 CYS B 184 1555 1555 2.04
SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.04
SSBOND 10 CYS B 374 CYS B 386 1555 1555 2.04
SSBOND 11 CYS B 406 CYS B 433 1555 1555 2.03
SSBOND 12 CYS B 437 CYS B 457 1555 1555 2.03
SSBOND 13 CYS B 448 CYS B 460 1555 1555 2.04
SSBOND 14 CYS C 56 CYS C 65 1555 1555 2.03
SSBOND 15 CYS C 107 CYS C 130 1555 1555 2.06
SSBOND 16 CYS C 146 CYS C 167 1555 1555 2.03
SSBOND 17 CYS D 5 CYS D 23 1555 1555 2.04
SSBOND 18 CYS D 13 CYS D 435 1555 1555 2.03
SSBOND 19 CYS D 16 CYS D 38 1555 1555 2.04
SSBOND 20 CYS D 26 CYS D 49 1555 1555 2.04
SSBOND 21 CYS D 177 CYS D 184 1555 1555 2.05
SSBOND 22 CYS D 232 CYS D 273 1555 1555 2.04
SSBOND 23 CYS D 374 CYS D 386 1555 1555 2.04
SSBOND 24 CYS D 406 CYS D 433 1555 1555 2.03
SSBOND 25 CYS D 437 CYS D 457 1555 1555 2.04
SSBOND 26 CYS D 448 CYS D 460 1555 1555 2.04
SSBOND 27 CYS E 56 CYS E 65 1555 1555 2.03
SSBOND 28 CYS E 107 CYS E 130 1555 1555 2.05
SSBOND 29 CYS E 146 CYS E 167 1555 1555 2.03
SSBOND 30 CYS F 5 CYS F 23 1555 1555 2.04
SSBOND 31 CYS F 13 CYS F 435 1555 1555 2.04
SSBOND 32 CYS F 16 CYS F 38 1555 1555 2.03
SSBOND 33 CYS F 26 CYS F 49 1555 1555 2.03
SSBOND 34 CYS F 177 CYS F 184 1555 1555 2.04
SSBOND 35 CYS F 232 CYS F 273 1555 1555 2.04
SSBOND 36 CYS F 374 CYS F 386 1555 1555 2.04
SSBOND 37 CYS F 406 CYS F 433 1555 1555 2.03
SSBOND 38 CYS F 437 CYS F 457 1555 1555 2.03
SSBOND 39 CYS F 448 CYS F 460 1555 1555 2.03
LINK ND2 ASN A 15 C1 NAG A3015 1555 1555 1.44
LINK ND2 ASN B 99 C1 NAG B3099 1555 1555 1.44
LINK ND2 ASN B 320 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN B 371 C1 NAG B3371 1555 1555 1.44
LINK ND2 ASN C 15 C1 NAG C3015 1555 1555 1.44
LINK ND2 ASN D 99 C1 NAG D3099 1555 1555 1.44
LINK ND2 ASN D 320 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN D 371 C1 NAG D3371 1555 1555 1.45
LINK ND2 ASN E 15 C1 NAG E3015 1555 1555 1.44
LINK ND2 ASN F 320 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN F 371 C1 NAG F3371 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG G 2 C1 MAN G 3 1555 1555 1.44
LINK O3 MAN G 3 C1 MAN G 4 1555 1555 1.45
LINK O6 MAN G 3 C1 MAN G 5 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 MAN H 3 1555 1555 1.44
LINK O3 MAN H 3 C1 MAN H 4 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG I 2 C1 MAN I 3 1555 1555 1.45
LINK O3 MAN I 3 C1 MAN I 4 1555 1555 1.45
LINK O6 MAN I 3 C1 MAN I 5 1555 1555 1.44
LINK OE1 GLU A 243 CA CA A2004 1555 1555 2.42
LINK OE2 GLU A 243 CA CA A2004 1555 1555 2.78
LINK OD2 ASP A 245 CA CA A2004 1555 1555 2.35
LINK O ASP A 247 CA CA A2004 1555 1555 2.32
LINK O THR A 250 CA CA A2004 1555 1555 2.36
LINK OG1 THR A 250 CA CA A2004 1555 1555 2.44
LINK OE1 GLU A 252 CA CA A2004 1555 1555 2.88
LINK OE2 GLU A 252 CA CA A2004 1555 1555 2.42
LINK OD1 ASP A 297 CA CA A2005 1555 1555 2.37
LINK OD1 ASN A 299 CA CA A2005 1555 1555 2.27
LINK OD1 ASP A 301 CA CA A2005 1555 1555 2.36
LINK O ARG A 303 CA CA A2005 1555 1555 2.30
LINK OD1 ASP A 305 CA CA A2005 1555 1555 2.85
LINK OD2 ASP A 305 CA CA A2005 1555 1555 2.63
LINK OD2 ASP A 365 CA CA A2006 1555 1555 2.59
LINK OD1 ASP A 367 CA CA A2006 1555 1555 2.25
LINK OD1 ASP A 369 CA CA A2006 1555 1555 2.51
LINK O TYR A 371 CA CA A2006 1555 1555 2.36
LINK OD1 ASP A 373 CA CA A2006 1555 1555 2.78
LINK OD2 ASP A 373 CA CA A2006 1555 1555 2.66
LINK OD1 ASP A 426 CA CA A2007 1555 1555 2.29
LINK OD1 ASP A 428 CA CA A2007 1555 1555 2.32
LINK OD1 ASN A 430 CA CA A2007 1555 1555 2.26
LINK O TYR A 432 CA CA A2007 1555 1555 2.39
LINK OD1 ASP A 434 CA CA A2007 1555 1555 2.76
LINK OD2 ASP A 434 CA CA A2007 1555 1555 2.69
LINK MG MG A 458 O HOH C 467 1555 1555 2.38
LINK MG MG A 458 O HOH C 468 1555 1555 2.23
LINK MG MG A 458 O HOH C 470 1555 1555 2.03
LINK MG MG A 458 O HOH C 472 1555 1555 2.02
LINK O HOH A 478 CA CA E2005 1555 1555 2.21
LINK O HOH A 512 CA CA A2006 1555 1555 2.29
LINK O HOH A 523 CA CA E2007 1555 1555 2.56
LINK O HOH A 550 CA CA B2002 1555 1555 2.19
LINK O HOH A 582 CA CA C2005 1555 1555 2.31
LINK O HOH A 583 CA CA A2005 1555 1555 2.29
LINK O HOH A 584 CA CA D2002 1555 1555 2.38
LINK O HOH A 585 CA CA D2002 1555 1555 2.21
LINK O HOH A 586 CA CA E2006 1555 1555 2.12
LINK O HOH A 587 CA CA F2002 1555 1555 2.36
LINK O HOH A 588 CA CA F2002 1555 1555 2.57
LINK O HOH A 589 CA CA A2007 1555 1555 2.33
LINK O HOH A 590 CA CA B2002 1555 1555 2.20
LINK O HOH A 591 CA CA C2006 1555 1555 2.32
LINK O HOH A 592 CA CA C2007 1555 1555 2.40
LINK O HOH A 605 MG MG C 458 1555 1555 1.97
LINK O HOH A 607 MG MG E 458 1555 1555 2.09
LINK O HOH A 608 MG MG E 458 1555 1555 2.47
LINK OG SER B 121 MG MG B2001 1555 1555 2.27
LINK OG SER B 123 MG MG B2001 1555 1555 2.08
LINK O SER B 123 CA CA B2002 1555 1555 2.24
LINK OD1 ASP B 126 CA CA B2002 1555 1555 2.73
LINK OD1 ASP B 127 CA CA B2002 1555 1555 2.27
LINK OD2 ASP B 158 CA CA B2003 1555 1555 2.26
LINK OD1 ASN B 215 CA CA B2003 1555 1555 2.17
LINK O ASP B 217 CA CA B2003 1555 1555 2.32
LINK OD1 ASP B 217 CA CA B2003 1555 1555 2.17
LINK O PRO B 219 CA CA B2003 1555 1555 2.11
LINK OE1 GLU B 220 MG MG B2001 1555 1555 2.00
LINK OE2 GLU B 220 CA CA B2003 1555 1555 2.35
LINK OD2 ASP B 251 CA CA B2002 1555 1555 2.33
LINK MG MG B2001 O HOH C 463 1555 1555 2.19
LINK MG MG B2001 O HOH C 464 1555 1555 1.93
LINK OE1 GLU C 243 CA CA C2004 1555 1555 2.41
LINK OE2 GLU C 243 CA CA C2004 1555 1555 2.60
LINK OD2 ASP C 245 CA CA C2004 1555 1555 2.34
LINK O ASP C 247 CA CA C2004 1555 1555 2.41
LINK O THR C 250 CA CA C2004 1555 1555 2.36
LINK OG1 THR C 250 CA CA C2004 1555 1555 2.38
LINK OE1 GLU C 252 CA CA C2004 1555 1555 2.57
LINK OE2 GLU C 252 CA CA C2004 1555 1555 2.79
LINK OD1 ASP C 297 CA CA C2005 1555 1555 2.27
LINK OD1 ASN C 299 CA CA C2005 1555 1555 2.14
LINK OD1 ASP C 301 CA CA C2005 1555 1555 2.34
LINK O ARG C 303 CA CA C2005 1555 1555 2.26
LINK OD1 ASP C 305 CA CA C2005 1555 1555 2.81
LINK OD2 ASP C 305 CA CA C2005 1555 1555 2.45
LINK OD2 ASP C 365 CA CA C2006 1555 1555 2.43
LINK OD1 ASP C 367 CA CA C2006 1555 1555 2.36
LINK OD1 ASP C 369 CA CA C2006 1555 1555 2.49
LINK O TYR C 371 CA CA C2006 1555 1555 2.25
LINK OD1 ASP C 373 CA CA C2006 1555 1555 2.76
LINK OD2 ASP C 373 CA CA C2006 1555 1555 2.64
LINK OD1 ASP C 426 CA CA C2007 1555 1555 2.37
LINK OD1 ASP C 428 CA CA C2007 1555 1555 2.41
LINK OD1 ASN C 430 CA CA C2007 1555 1555 2.25
LINK O TYR C 432 CA CA C2007 1555 1555 2.24
LINK OD1 ASP C 434 CA CA C2007 1555 1555 2.71
LINK OD2 ASP C 434 CA CA C2007 1555 1555 2.74
LINK MG MG C 458 O HOH C 473 1555 1555 2.03
LINK MG MG C 458 O HOH C 474 1555 1555 2.21
LINK MG MG C 458 O HOH C 475 1555 1555 2.04
LINK MG MG C 458 O HOH C 477 1555 1555 2.07
LINK MG MG C 458 O HOH C 478 1555 1555 1.88
LINK O HOH C 459 MG MG D2001 1555 1555 1.97
LINK O HOH C 460 MG MG D2001 1555 1555 1.86
LINK O HOH C 465 MG MG F2001 1555 1555 2.03
LINK O HOH C 466 MG MG F2001 1555 1555 2.12
LINK O HOH C 484 MG MG E 458 1555 1555 2.15
LINK OG SER D 121 MG MG D2001 1555 1555 2.21
LINK OG SER D 123 MG MG D2001 1555 1555 2.01
LINK O SER D 123 CA CA D2002 1555 1555 2.19
LINK OD1 ASP D 126 CA CA D2002 1555 1555 2.95
LINK OD1 ASP D 127 CA CA D2002 1555 1555 2.24
LINK OD2 ASP D 158 CA CA D2003 1555 1555 2.20
LINK OD1 ASN D 215 CA CA D2003 1555 1555 2.18
LINK O ASP D 217 CA CA D2003 1555 1555 2.41
LINK OD1 ASP D 217 CA CA D2003 1555 1555 2.16
LINK O PRO D 219 CA CA D2003 1555 1555 2.14
LINK OE1 GLU D 220 MG MG D2001 1555 1555 2.13
LINK OE2 GLU D 220 CA CA D2003 1555 1555 2.27
LINK OD2 ASP D 251 CA CA D2002 1555 1555 2.48
LINK OE1 GLU E 243 CA CA E2004 1555 1555 2.65
LINK OE2 GLU E 243 CA CA E2004 1555 1555 2.50
LINK OD2 ASP E 245 CA CA E2004 1555 1555 2.21
LINK O ASP E 247 CA CA E2004 1555 1555 2.30
LINK O THR E 250 CA CA E2004 1555 1555 2.16
LINK OG1 THR E 250 CA CA E2004 1555 1555 2.49
LINK OE1 GLU E 252 CA CA E2004 1555 1555 2.63
LINK OE2 GLU E 252 CA CA E2004 1555 1555 2.70
LINK OD1 ASP E 297 CA CA E2005 1555 1555 2.21
LINK OD1 ASN E 299 CA CA E2005 1555 1555 2.22
LINK OD1 ASP E 301 CA CA E2005 1555 1555 2.32
LINK O ARG E 303 CA CA E2005 1555 1555 2.24
LINK OD1 ASP E 305 CA CA E2005 1555 1555 2.90
LINK OD2 ASP E 305 CA CA E2005 1555 1555 2.40
LINK OD2 ASP E 365 CA CA E2006 1555 1555 2.47
LINK OD1 ASP E 367 CA CA E2006 1555 1555 2.40
LINK OD1 ASP E 369 CA CA E2006 1555 1555 2.44
LINK O TYR E 371 CA CA E2006 1555 1555 2.23
LINK OD1 ASP E 373 CA CA E2006 1555 1555 2.70
LINK OD2 ASP E 373 CA CA E2006 1555 1555 2.64
LINK OD1 ASP E 426 CA CA E2007 1555 1555 2.37
LINK OD1 ASP E 428 CA CA E2007 1555 1555 2.39
LINK OD1 ASN E 430 CA CA E2007 1555 1555 2.37
LINK O TYR E 432 CA CA E2007 1555 1555 2.30
LINK OD1 ASP E 434 CA CA E2007 1555 1555 2.78
LINK OD2 ASP E 434 CA CA E2007 1555 1555 2.57
LINK OG SER F 121 MG MG F2001 1555 1555 2.25
LINK OG SER F 123 MG MG F2001 1555 1555 2.07
LINK O SER F 123 CA CA F2002 1555 1555 2.29
LINK OD1 ASP F 126 CA CA F2002 1555 1555 2.95
LINK OD1 ASP F 127 CA CA F2002 1555 1555 2.12
LINK OD2 ASP F 158 CA CA F2003 1555 1555 2.21
LINK OD1 ASN F 215 CA CA F2003 1555 1555 2.14
LINK O ASP F 217 CA CA F2003 1555 1555 2.40
LINK OD1 ASP F 217 CA CA F2003 1555 1555 2.25
LINK O PRO F 219 CA CA F2003 1555 1555 2.14
LINK OE1 GLU F 220 MG MG F2001 1555 1555 2.11
LINK OE2 GLU F 220 CA CA F2003 1555 1555 2.29
LINK OD2 ASP F 251 CA CA F2002 1555 1555 2.35
CISPEP 1 SER A 29 HIS A 30 0 -0.66
CISPEP 2 SER B 84 PRO B 85 0 7.04
CISPEP 3 SER B 162 PRO B 163 0 3.97
CISPEP 4 SER B 168 PRO B 169 0 -5.61
CISPEP 5 SER D 84 PRO D 85 0 3.24
CISPEP 6 SER D 162 PRO D 163 0 5.38
CISPEP 7 SER D 168 PRO D 169 0 -5.89
CISPEP 8 SER F 84 PRO F 85 0 3.86
CISPEP 9 SER F 162 PRO F 163 0 5.78
CISPEP 10 SER F 168 PRO F 169 0 -6.49
CRYST1 332.093 332.093 88.288 90.00 90.00 120.00 P 62 18
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 0.003011 0.001739 0.000000 0.00000
SCALE2 0.000000 0.003477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
