HEADER CELL ADHESION/BLOOD CLOTTING 22-NOV-08 3FCS
TITLE STRUCTURE OF COMPLETE ECTODOMAIN OF INTEGRIN AIIBB3
CAVEAT 3FCS MAN F 3 HAS WRONG CHIRALITY AT ATOM C1 MAN G 3 HAS WRONG
CAVEAT 2 3FCS CHIRALITY AT ATOM C1 MAN I 3 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 3FCS NAG C 3570 HAS WRONG CHIRALITY AT ATOM C1 NAG D 3099 HAS
CAVEAT 4 3FCS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN, ALPHA 2B;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 32-989, ECTODOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTEGRIN BETA-3;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: UNP RESIDUES 27-716, EXTRACELLULAR DOMAIN;
COMPND 10 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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: 3.2.8.1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1, PEF1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: ITGB3, GP3A;
SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS BETA PROPELLER, ROSSMANN FOLD, EGF DOMAIN, CELL ADHESION, DISEASE
KEYWDS 2 MUTATION, GLYCOPROTEIN, HOST-VIRUS INTERACTION, INTEGRIN, MEMBRANE,
KEYWDS 3 PHOSPHOPROTEIN, RECEPTOR, TRANSMEMBRANE, CELL ADHESION-IMMUNE SYSTEM
KEYWDS 4 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 5 06-SEP-23 3FCS 1 REMARK
REVDAT 4 20-OCT-21 3FCS 1 SEQADV HETSYN
REVDAT 3 29-JUL-20 3FCS 1 CAVEAT COMPND REMARK SEQADV
REVDAT 3 2 1 HETNAM SSBOND LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 13-JUL-11 3FCS 1 VERSN
REVDAT 1 20-JAN-09 3FCS 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. 2.55 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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 133242
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1785
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8771
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.4110
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.4230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 462
REMARK 3 SOLVENT ATOMS : 678
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) : 31.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.03000
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): 0.516
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.297
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.317
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.421
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24891 ; 0.003 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 16841 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33907 ; 0.741 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 40845 ; 0.647 ; 3.007
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3122 ; 4.263 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1104 ;28.826 ;24.583
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3967 ;11.482 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 151 ; 9.957 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3794 ; 0.046 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27816 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4792 ; 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): 15479 ; 0.880 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6292 ; 0.159 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 24955 ; 1.542 ;10.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9412 ; 0.777 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8943 ; 1.330 ;10.000
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 : 12
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 221 2
REMARK 3 1 C 1 C 221 2
REMARK 3 2 A 224 A 271 2
REMARK 3 2 C 224 C 271 2
REMARK 3 3 A 275 A 276 2
REMARK 3 3 C 275 C 276 2
REMARK 3 4 A 280 A 452 2
REMARK 3 4 C 280 C 452 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2568 ; 0.050 ; 0.250
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3097 ; 0.090 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 2568 ; 0.020 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3097 ; 0.020 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 453 A 600 2
REMARK 3 1 C 453 C 600 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 871 ; 0.050 ; 0.250
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1026 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 2 A (A**2): 871 ; 0.020 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 1026 ; 0.010 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 610 A 743 2
REMARK 3 1 C 610 C 743 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 774 ; 0.050 ; 0.250
REMARK 3 MEDIUM POSITIONAL 3 A (A): 865 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 3 A (A**2): 774 ; 0.010 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 865 ; 0.010 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 744 A 763 4
REMARK 3 1 C 744 C 763 4
REMARK 3 2 A 772 A 959 4
REMARK 3 2 C 772 C 959 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 2050 ; 0.280 ; 0.500
REMARK 3 MEDIUM THERMAL 4 A (A**2): 2050 ; 0.090 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 7 4
REMARK 3 1 D 1 D 7 4
REMARK 3 2 B 8 B 10 6
REMARK 3 2 D 8 D 10 6
REMARK 3 3 B 11 B 32 4
REMARK 3 3 D 11 D 32 4
REMARK 3 4 B 36 B 57 4
REMARK 3 4 D 36 D 57 4
REMARK 3 5 B 434 B 436 4
REMARK 3 5 D 434 D 436 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 B (A): 663 ; 0.200 ; 0.500
REMARK 3 LOOSE POSITIONAL 5 B (A): 41 ; 0.260 ; 5.000
REMARK 3 MEDIUM THERMAL 5 B (A**2): 663 ; 0.100 ; 2.000
REMARK 3 LOOSE THERMAL 5 B (A**2): 41 ; 0.060 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 58 B 108 4
REMARK 3 1 D 58 D 108 4
REMARK 3 2 B 353 B 433 4
REMARK 3 2 D 353 D 433 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 6 B (A): 1719 ; 0.170 ; 0.500
REMARK 3 MEDIUM THERMAL 6 B (A**2): 1719 ; 0.120 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 109 B 352 4
REMARK 3 1 D 109 D 352 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 7 B (A): 3174 ; 0.170 ; 0.500
REMARK 3 MEDIUM THERMAL 7 B (A**2): 3174 ; 0.130 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 437 B 472 4
REMARK 3 1 D 437 D 472 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 8 B (A): 449 ; 0.140 ; 0.500
REMARK 3 MEDIUM THERMAL 8 B (A**2): 449 ; 0.060 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 473 B 522 4
REMARK 3 1 D 473 D 522 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 9 B (A): 573 ; 0.170 ; 0.500
REMARK 3 MEDIUM THERMAL 9 B (A**2): 573 ; 0.070 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 523 B 559 4
REMARK 3 1 D 523 D 559 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 10 B (A): 475 ; 0.240 ; 0.500
REMARK 3 MEDIUM THERMAL 10 B (A**2): 475 ; 0.100 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 560 B 605 4
REMARK 3 1 D 560 D 605 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 11 B (A): 554 ; 0.180 ; 0.500
REMARK 3 MEDIUM THERMAL 11 B (A**2): 554 ; 0.070 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 601 A 609 5
REMARK 3 1 C 601 C 609 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 12 A (A): 53 ; 0.070 ; 0.500
REMARK 3 LOOSE POSITIONAL 12 A (A): 47 ; 0.110 ; 5.000
REMARK 3 MEDIUM THERMAL 12 A (A**2): 53 ; 0.080 ; 2.000
REMARK 3 LOOSE THERMAL 12 A (A**2): 47 ; 0.130 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
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 2007
REMARK 3 ORIGIN FOR THE GROUP (A): -82.6220 -53.3398 -79.4693
REMARK 3 T TENSOR
REMARK 3 T11: -0.2536 T22: -0.0294
REMARK 3 T33: -0.0934 T12: 0.0012
REMARK 3 T13: -0.0395 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.6690 L22: 1.7658
REMARK 3 L33: 1.9983 L12: -0.2091
REMARK 3 L13: 0.3571 L23: 0.4368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.1589 S13: 0.0807
REMARK 3 S21: -0.3133 S22: -0.1161 S23: -0.0579
REMARK 3 S31: -0.0381 S32: -0.1443 S33: 0.0921
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 2007
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7863 34.0230 9.4560
REMARK 3 T TENSOR
REMARK 3 T11: -0.1907 T22: -0.3062
REMARK 3 T33: -0.2377 T12: -0.0161
REMARK 3 T13: 0.0440 T23: -0.0659
REMARK 3 L TENSOR
REMARK 3 L11: 1.6977 L22: 1.5980
REMARK 3 L33: 2.0005 L12: -0.0706
REMARK 3 L13: 0.4183 L23: 0.4365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0925 S12: -0.1413 S13: 0.0029
REMARK 3 S21: 0.0161 S22: 0.0148 S23: 0.0564
REMARK 3 S31: -0.2180 S32: 0.0690 S33: 0.0776
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 453 A 600
REMARK 3 ORIGIN FOR THE GROUP (A): -47.4587 -31.6025 -42.6473
REMARK 3 T TENSOR
REMARK 3 T11: -0.0568 T22: -0.2487
REMARK 3 T33: -0.0129 T12: -0.0079
REMARK 3 T13: -0.0074 T23: -0.2422
REMARK 3 L TENSOR
REMARK 3 L11: 5.3148 L22: 2.3188
REMARK 3 L33: 5.4415 L12: 1.4954
REMARK 3 L13: 2.1381 L23: 0.4958
REMARK 3 S TENSOR
REMARK 3 S11: 0.1148 S12: -0.3685 S13: -0.0966
REMARK 3 S21: 0.0685 S22: 0.1690 S23: 0.2735
REMARK 3 S31: -0.3069 S32: -0.1493 S33: -0.2838
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 453 C 600
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0567 -1.0633 -27.2439
REMARK 3 T TENSOR
REMARK 3 T11: -0.1904 T22: -0.1838
REMARK 3 T33: -0.0730 T12: 0.0027
REMARK 3 T13: -0.2075 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 2.2549 L22: 5.4267
REMARK 3 L33: 5.4763 L12: 1.8080
REMARK 3 L13: 0.6760 L23: 2.5660
REMARK 3 S TENSOR
REMARK 3 S11: 0.1526 S12: 0.0046 S13: 0.1531
REMARK 3 S21: -0.3714 S22: 0.1093 S23: -0.0469
REMARK 3 S31: -0.0290 S32: -0.3162 S33: -0.2619
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 : A 601 A 746
REMARK 3 RESIDUE RANGE : A 2008 A 2008
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5079 -40.0846 -69.5152
REMARK 3 T TENSOR
REMARK 3 T11: -0.0614 T22: 0.0632
REMARK 3 T33: 0.0108 T12: -0.0075
REMARK 3 T13: -0.0255 T23: -0.2509
REMARK 3 L TENSOR
REMARK 3 L11: 2.6400 L22: 3.2304
REMARK 3 L33: 7.8315 L12: 0.6586
REMARK 3 L13: 2.7043 L23: 3.2151
REMARK 3 S TENSOR
REMARK 3 S11: -0.0959 S12: 0.0111 S13: -0.1684
REMARK 3 S21: -0.5900 S22: 0.1266 S23: 0.1128
REMARK 3 S31: -0.6464 S32: -0.2333 S33: -0.0307
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 : C 601 C 746
REMARK 3 RESIDUE RANGE : C 2008 C 2008
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5684 -15.1015 -0.2543
REMARK 3 T TENSOR
REMARK 3 T11: 0.1661 T22: -0.1807
REMARK 3 T33: 0.0788 T12: 0.0329
REMARK 3 T13: -0.1624 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 3.4101 L22: 2.8449
REMARK 3 L33: 8.4651 L12: 0.4864
REMARK 3 L13: 3.1575 L23: 2.8071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0809 S12: -0.5502 S13: 0.1277
REMARK 3 S21: 0.0614 S22: 0.0350 S23: -0.1708
REMARK 3 S31: -0.4495 S32: -0.6480 S33: -0.1159
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 747 A 959
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4014 -69.7992-114.9065
REMARK 3 T TENSOR
REMARK 3 T11: -0.1336 T22: -0.0461
REMARK 3 T33: -0.2978 T12: -0.0842
REMARK 3 T13: -0.1262 T23: -0.1501
REMARK 3 L TENSOR
REMARK 3 L11: 1.5071 L22: 5.3303
REMARK 3 L33: 7.4174 L12: -0.3289
REMARK 3 L13: 0.1689 L23: 3.8160
REMARK 3 S TENSOR
REMARK 3 S11: -0.1320 S12: -0.2677 S13: 0.1466
REMARK 3 S21: 0.1535 S22: 0.1325 S23: -0.2849
REMARK 3 S31: -0.1266 S32: 0.0819 S33: -0.0005
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 747 C 959
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0292 -7.5729 44.5094
REMARK 3 T TENSOR
REMARK 3 T11: 0.7356 T22: 0.9487
REMARK 3 T33: 0.2250 T12: 0.0093
REMARK 3 T13: -0.3013 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 2.4053 L22: 0.7691
REMARK 3 L33: 2.9958 L12: -1.2308
REMARK 3 L13: 1.3404 L23: -0.1264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: -1.5190 S13: -0.6034
REMARK 3 S21: 0.3089 S22: 0.3201 S23: -0.0778
REMARK 3 S31: 0.0290 S32: -0.7361 S33: -0.3974
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 : B 1 B 57
REMARK 3 RESIDUE RANGE : B 434 B 436
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5571 -73.4332 -42.1754
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: -0.1409
REMARK 3 T33: -0.1827 T12: 0.0591
REMARK 3 T13: -0.0546 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 8.1591 L22: 3.3539
REMARK 3 L33: 3.8761 L12: -1.5525
REMARK 3 L13: 2.4936 L23: -2.0083
REMARK 3 S TENSOR
REMARK 3 S11: 0.1368 S12: 0.0249 S13: 0.6087
REMARK 3 S21: 0.2090 S22: -0.1143 S23: -0.4263
REMARK 3 S31: -0.6482 S32: 0.0285 S33: -0.0226
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 : D 1 D 57
REMARK 3 RESIDUE RANGE : D 434 D 436
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7938 -17.1445 -27.7742
REMARK 3 T TENSOR
REMARK 3 T11: -0.0962 T22: 0.0323
REMARK 3 T33: -0.1150 T12: 0.0716
REMARK 3 T13: 0.0062 T23: -0.1133
REMARK 3 L TENSOR
REMARK 3 L11: 4.1362 L22: 8.1329
REMARK 3 L33: 3.5169 L12: -0.8401
REMARK 3 L13: -0.6825 L23: 3.1997
REMARK 3 S TENSOR
REMARK 3 S11: -0.2129 S12: 0.2341 S13: -0.1440
REMARK 3 S21: -0.4366 S22: 0.2354 S23: 0.6762
REMARK 3 S31: 0.0488 S32: -0.7095 S33: -0.0225
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 : B 58 B 108
REMARK 3 RESIDUE RANGE : B 353 B 433
REMARK 3 ORIGIN FOR THE GROUP (A): -52.3761 -87.7205 -63.8100
REMARK 3 T TENSOR
REMARK 3 T11: 0.3266 T22: -0.5543
REMARK 3 T33: -0.0483 T12: 0.1416
REMARK 3 T13: -0.1422 T23: 0.1004
REMARK 3 L TENSOR
REMARK 3 L11: 4.9949 L22: 2.4481
REMARK 3 L33: 4.7672 L12: 1.5713
REMARK 3 L13: 2.4641 L23: 2.9640
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: -0.2050 S13: -0.6048
REMARK 3 S21: 0.0743 S22: 0.0089 S23: 0.1976
REMARK 3 S31: 0.7687 S32: 0.2044 S33: -0.0216
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 : D 58 D 108
REMARK 3 RESIDUE RANGE : D 353 D 433
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2056 3.7133 -6.2380
REMARK 3 T TENSOR
REMARK 3 T11: -0.6604 T22: 0.3088
REMARK 3 T33: -0.0366 T12: 0.1884
REMARK 3 T13: 0.1573 T23: -0.2235
REMARK 3 L TENSOR
REMARK 3 L11: 3.3879 L22: 6.2464
REMARK 3 L33: 6.3162 L12: 1.5258
REMARK 3 L13: 4.1094 L23: 1.7135
REMARK 3 S TENSOR
REMARK 3 S11: 0.1903 S12: 0.1258 S13: -0.1564
REMARK 3 S21: -0.1709 S22: 0.0780 S23: -0.7849
REMARK 3 S31: 0.3308 S32: 0.6615 S33: -0.2683
REMARK 3
REMARK 3 TLS GROUP : 13
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): -80.6029 -87.0349 -83.1536
REMARK 3 T TENSOR
REMARK 3 T11: 0.3006 T22: -0.2293
REMARK 3 T33: 0.1094 T12: -0.0992
REMARK 3 T13: -0.1085 T23: -0.1892
REMARK 3 L TENSOR
REMARK 3 L11: 1.9253 L22: 2.1482
REMARK 3 L33: 0.7364 L12: -0.7382
REMARK 3 L13: -0.4231 L23: 0.2485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1690 S12: 0.4181 S13: -0.5928
REMARK 3 S21: -0.0205 S22: -0.1549 S23: 0.3545
REMARK 3 S31: 0.6881 S32: -0.2861 S33: -0.0141
REMARK 3
REMARK 3 TLS GROUP : 14
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): 38.5322 31.8298 13.0841
REMARK 3 T TENSOR
REMARK 3 T11: -0.4633 T22: 0.2965
REMARK 3 T33: -0.0209 T12: -0.0869
REMARK 3 T13: -0.0771 T23: -0.1614
REMARK 3 L TENSOR
REMARK 3 L11: 2.2660 L22: 1.7838
REMARK 3 L33: 0.5997 L12: -0.2705
REMARK 3 L13: 0.0287 L23: -0.6392
REMARK 3 S TENSOR
REMARK 3 S11: -0.1109 S12: 0.0469 S13: 0.1405
REMARK 3 S21: 0.2387 S22: 0.1108 S23: -0.5378
REMARK 3 S31: -0.3197 S32: 0.7132 S33: 0.0002
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 : B 437 B 472
REMARK 3 ORIGIN FOR THE GROUP (A): -39.2518 -64.8909 -28.2604
REMARK 3 T TENSOR
REMARK 3 T11: -0.2024 T22: 0.2486
REMARK 3 T33: -0.2543 T12: 0.1281
REMARK 3 T13: 0.0000 T23: -0.1832
REMARK 3 L TENSOR
REMARK 3 L11: 2.6914 L22: 9.0510
REMARK 3 L33: 3.9345 L12: -1.3749
REMARK 3 L13: -3.0657 L23: -0.3558
REMARK 3 S TENSOR
REMARK 3 S11: -0.0750 S12: -0.9920 S13: 0.4062
REMARK 3 S21: 0.2852 S22: -0.0983 S23: 0.5756
REMARK 3 S31: 0.1899 S32: -0.6163 S33: 0.1733
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 437 D 472
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2263 -9.3829 -41.7377
REMARK 3 T TENSOR
REMARK 3 T11: 0.2535 T22: -0.1291
REMARK 3 T33: -0.1918 T12: 0.0924
REMARK 3 T13: -0.2294 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 2.7855 L22: 2.6103
REMARK 3 L33: 9.3659 L12: 1.0639
REMARK 3 L13: -0.1640 L23: 3.6656
REMARK 3 S TENSOR
REMARK 3 S11: 0.1380 S12: 0.5513 S13: 0.4349
REMARK 3 S21: -1.1430 S22: -0.2722 S23: 0.1319
REMARK 3 S31: -0.7323 S32: -0.0913 S33: 0.1342
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 473 B 522
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6151 -51.2952 -44.1610
REMARK 3 T TENSOR
REMARK 3 T11: -0.0282 T22: -0.2974
REMARK 3 T33: 0.0050 T12: 0.1950
REMARK 3 T13: -0.0913 T23: -0.2338
REMARK 3 L TENSOR
REMARK 3 L11: 9.1837 L22: 5.7373
REMARK 3 L33: 7.9206 L12: 2.9781
REMARK 3 L13: 1.6035 L23: -0.4844
REMARK 3 S TENSOR
REMARK 3 S11: -0.2606 S12: -0.1007 S13: 0.3085
REMARK 3 S21: 0.0753 S22: -0.1167 S23: -0.1295
REMARK 3 S31: 0.1489 S32: 0.2269 S33: 0.3773
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 473 D 522
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6108 -16.0107 -25.8379
REMARK 3 T TENSOR
REMARK 3 T11: -0.2428 T22: -0.0823
REMARK 3 T33: 0.0810 T12: 0.1658
REMARK 3 T13: -0.2171 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 3.3956 L22: 8.9434
REMARK 3 L33: 6.4364 L12: 1.0215
REMARK 3 L13: -0.7020 L23: -0.9011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: -0.0647 S13: -0.0109
REMARK 3 S21: -0.0982 S22: -0.1751 S23: -0.0452
REMARK 3 S31: 0.6239 S32: -0.0030 S33: 0.2248
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 523 B 559
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5219 -61.8840 -63.7301
REMARK 3 T TENSOR
REMARK 3 T11: 0.2148 T22: -0.4884
REMARK 3 T33: -0.0519 T12: 0.0522
REMARK 3 T13: -0.0408 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 7.7967 L22: 7.1888
REMARK 3 L33: 9.3594 L12: 4.2165
REMARK 3 L13: 5.0677 L23: 5.4206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0016 S12: -0.1388 S13: 0.9855
REMARK 3 S21: -0.3198 S22: -0.1430 S23: -0.1647
REMARK 3 S31: -0.3356 S32: -0.6620 S33: 0.1414
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 523 D 559
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1921 -4.1175 -6.2051
REMARK 3 T TENSOR
REMARK 3 T11: -0.2786 T22: 0.2574
REMARK 3 T33: 0.0422 T12: 0.0926
REMARK 3 T13: -0.0521 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 4.3993 L22: 5.6015
REMARK 3 L33: 6.1860 L12: 4.3050
REMARK 3 L13: 2.8353 L23: 1.3158
REMARK 3 S TENSOR
REMARK 3 S11: 0.1729 S12: -0.2882 S13: -0.2051
REMARK 3 S21: 0.0164 S22: 0.0657 S23: 1.0438
REMARK 3 S31: -0.6047 S32: -0.1218 S33: -0.2386
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 560 B 612
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0747 -76.7271 -89.5359
REMARK 3 T TENSOR
REMARK 3 T11: 0.0353 T22: 0.2095
REMARK 3 T33: -0.2329 T12: 0.0667
REMARK 3 T13: -0.0698 T23: -0.1093
REMARK 3 L TENSOR
REMARK 3 L11: 0.7873 L22: 3.4245
REMARK 3 L33: 9.8085 L12: 0.0399
REMARK 3 L13: -2.7694 L23: 0.3367
REMARK 3 S TENSOR
REMARK 3 S11: -0.3219 S12: 0.3554 S13: -0.0970
REMARK 3 S21: 0.1850 S22: -0.1038 S23: 0.1055
REMARK 3 S31: 0.3470 S32: -0.1211 S33: 0.4257
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 560 D 612
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6652 -4.5346 19.7967
REMARK 3 T TENSOR
REMARK 3 T11: 0.5140 T22: 0.1586
REMARK 3 T33: 0.0095 T12: 0.0000
REMARK 3 T13: -0.2423 T23: -0.1647
REMARK 3 L TENSOR
REMARK 3 L11: 8.5751 L22: 2.0675
REMARK 3 L33: 7.2795 L12: -0.9910
REMARK 3 L13: 1.1539 L23: -3.8634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0954 S12: -0.0441 S13: 0.0533
REMARK 3 S21: 0.7884 S22: -0.5623 S23: -0.6457
REMARK 3 S31: 0.0450 S32: 1.0880 S33: 0.4669
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 613 B 690
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3353 -95.3977-102.1487
REMARK 3 T TENSOR
REMARK 3 T11: 0.4678 T22: 0.4976
REMARK 3 T33: 0.6048 T12: 0.0381
REMARK 3 T13: 0.0082 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.2241 L22: 1.1316
REMARK 3 L33: 2.6345 L12: 0.2408
REMARK 3 L13: -0.7174 L23: -0.2270
REMARK 3 S TENSOR
REMARK 3 S11: 0.4013 S12: -0.2037 S13: 0.9018
REMARK 3 S21: 0.1321 S22: -0.4006 S23: -0.1023
REMARK 3 S31: 1.1710 S32: 0.1712 S33: -0.0008
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3FCS 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_1000050430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 135066
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.550
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.15
REMARK 200 R MERGE FOR SHELL (I) : 0.56600
REMARK 200 R SYM FOR SHELL (I) : 0.56600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.130
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: COMBINATION OF PDB ENTRY 1JV2 AND 1TXV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 50 MM MAGNESIUM ACETATE,
REMARK 280 AND 0.1 M IMIDAZOLE, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 327.31150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 163.65575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 490.96725
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: HETERO-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: 11070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, G, H, 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 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: 10610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J, K, L, M, N
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 GLU A 764
REMARK 465 GLU A 765
REMARK 465 GLY A 766
REMARK 465 GLU A 767
REMARK 465 ARG A 768
REMARK 465 GLU A 769
REMARK 465 GLN A 770
REMARK 465 ASN A 771
REMARK 465 SER A 772
REMARK 465 LEU A 773
REMARK 465 ASP A 774
REMARK 465 GLY A 840
REMARK 465 LEU A 841
REMARK 465 PRO A 842
REMARK 465 ILE A 843
REMARK 465 PRO A 844
REMARK 465 SER A 845
REMARK 465 PRO A 846
REMARK 465 SER A 847
REMARK 465 PRO A 848
REMARK 465 ILE A 849
REMARK 465 HIS A 850
REMARK 465 PRO A 851
REMARK 465 ALA A 852
REMARK 465 HIS A 853
REMARK 465 HIS A 854
REMARK 465 LYS A 855
REMARK 465 ARG A 856
REMARK 465 ASP A 857
REMARK 465 ARG A 858
REMARK 465 ARG A 859
REMARK 465 GLN A 860
REMARK 465 ILE A 861
REMARK 465 PHE A 862
REMARK 465 LEU A 863
REMARK 465 PRO A 864
REMARK 465 GLU A 865
REMARK 465 PRO A 866
REMARK 465 GLU A 867
REMARK 465 GLN A 868
REMARK 465 PRO A 869
REMARK 465 SER A 870
REMARK 465 ARG A 871
REMARK 465 LEU A 872
REMARK 465 GLN A 873
REMARK 465 GLY B 75
REMARK 465 ASP B 76
REMARK 465 SER B 77
REMARK 465 SER B 78
REMARK 465 ASP B 477
REMARK 465 TYR B 478
REMARK 465 ARG B 479
REMARK 465 PRO B 480
REMARK 465 SER B 481
REMARK 465 GLN B 482
REMARK 465 SER C 758
REMARK 465 LEU C 759
REMARK 465 VAL C 760
REMARK 465 VAL C 761
REMARK 465 ALA C 762
REMARK 465 ALA C 763
REMARK 465 GLU C 764
REMARK 465 GLU C 765
REMARK 465 GLY C 766
REMARK 465 GLU C 767
REMARK 465 ARG C 768
REMARK 465 GLU C 769
REMARK 465 GLN C 770
REMARK 465 ASN C 771
REMARK 465 SER C 772
REMARK 465 LEU C 773
REMARK 465 ASP C 774
REMARK 465 SER C 775
REMARK 465 TRP C 776
REMARK 465 ASP C 838
REMARK 465 TRP C 839
REMARK 465 GLY C 840
REMARK 465 LEU C 841
REMARK 465 PRO C 842
REMARK 465 ILE C 843
REMARK 465 PRO C 844
REMARK 465 SER C 845
REMARK 465 PRO C 846
REMARK 465 SER C 847
REMARK 465 PRO C 848
REMARK 465 ILE C 849
REMARK 465 HIS C 850
REMARK 465 PRO C 851
REMARK 465 ALA C 852
REMARK 465 HIS C 853
REMARK 465 HIS C 854
REMARK 465 LYS C 855
REMARK 465 ARG C 856
REMARK 465 ASP C 857
REMARK 465 ARG C 858
REMARK 465 ARG C 859
REMARK 465 GLN C 860
REMARK 465 ILE C 861
REMARK 465 PHE C 862
REMARK 465 LEU C 863
REMARK 465 PRO C 864
REMARK 465 GLU C 865
REMARK 465 PRO C 866
REMARK 465 GLU C 867
REMARK 465 GLN C 868
REMARK 465 PRO C 869
REMARK 465 SER C 870
REMARK 465 ARG C 871
REMARK 465 LEU C 872
REMARK 465 GLN C 873
REMARK 465 ASP D 76
REMARK 465 SER D 77
REMARK 465 SER D 78
REMARK 465 ASP D 477
REMARK 465 TYR D 478
REMARK 465 ARG D 479
REMARK 465 PRO D 480
REMARK 465 SER D 481
REMARK 465 GLN D 482
REMARK 465 GLU D 613
REMARK 465 CYS D 614
REMARK 465 VAL D 615
REMARK 465 GLU D 616
REMARK 465 CYS D 617
REMARK 465 LYS D 618
REMARK 465 LYS D 619
REMARK 465 PHE D 620
REMARK 465 ASP D 621
REMARK 465 ARG D 622
REMARK 465 GLY D 623
REMARK 465 ALA D 624
REMARK 465 LEU D 625
REMARK 465 HIS D 626
REMARK 465 ASP D 627
REMARK 465 GLU D 628
REMARK 465 ASN D 629
REMARK 465 THR D 630
REMARK 465 CYS D 631
REMARK 465 ASN D 632
REMARK 465 ARG D 633
REMARK 465 TYR D 634
REMARK 465 CYS D 635
REMARK 465 ARG D 636
REMARK 465 ASP D 637
REMARK 465 GLU D 638
REMARK 465 ILE D 639
REMARK 465 GLU D 640
REMARK 465 SER D 641
REMARK 465 VAL D 642
REMARK 465 LYS D 643
REMARK 465 GLU D 644
REMARK 465 LEU D 645
REMARK 465 LYS D 646
REMARK 465 ASP D 647
REMARK 465 THR D 648
REMARK 465 GLY D 649
REMARK 465 LYS D 650
REMARK 465 ASP D 651
REMARK 465 ALA D 652
REMARK 465 VAL D 653
REMARK 465 ASN D 654
REMARK 465 CYS D 655
REMARK 465 THR D 656
REMARK 465 TYR D 657
REMARK 465 LYS D 658
REMARK 465 ASN D 659
REMARK 465 GLU D 660
REMARK 465 ASP D 661
REMARK 465 ASP D 662
REMARK 465 CYS D 663
REMARK 465 VAL D 664
REMARK 465 VAL D 665
REMARK 465 ARG D 666
REMARK 465 PHE D 667
REMARK 465 GLN D 668
REMARK 465 TYR D 669
REMARK 465 TYR D 670
REMARK 465 GLU D 671
REMARK 465 ASP D 672
REMARK 465 SER D 673
REMARK 465 SER D 674
REMARK 465 GLY D 675
REMARK 465 LYS D 676
REMARK 465 SER D 677
REMARK 465 ILE D 678
REMARK 465 LEU D 679
REMARK 465 TYR D 680
REMARK 465 VAL D 681
REMARK 465 VAL D 682
REMARK 465 GLU D 683
REMARK 465 GLU D 684
REMARK 465 PRO D 685
REMARK 465 GLU D 686
REMARK 465 CYS D 687
REMARK 465 CYS D 688
REMARK 465 LYS D 689
REMARK 465 GLY D 690
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 GLU A 667 C O CB CG CD OE1 OE2
REMARK 470 GLY A 668 N CA
REMARK 470 TRP A 839 C O CB CG CD1 CD2 NE1
REMARK 470 TRP A 839 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 GLU C 667 C O CB CG CD OE1 OE2
REMARK 470 GLY C 668 N
REMARK 470 PHE C 669 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLY C 777 N
REMARK 470 VAL C 837 CA C O CB CG1 CG2
REMARK 470 ASP C 874 N CB CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU D 573 O HOH D 693 2.05
REMARK 500 O ARG C 516 O HOH C 1134 2.08
REMARK 500 O HOH A 1021 O HOH A 1022 2.12
REMARK 500 O HOH C 1029 O HOH C 1226 2.13
REMARK 500 O HOH C 1008 O HOH C 1094 2.17
REMARK 500 O HOH C 984 O HOH D 720 2.17
REMARK 500 O ASP A 881 O HOH A 1183 2.18
REMARK 500 O HOH C 983 O HOH C 1108 2.19
REMARK 500 O HOH A 1003 O HOH B 695 2.19
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 SER A 101 -122.91 50.95
REMARK 500 LYS A 118 -116.09 51.00
REMARK 500 GLU A 123 132.90 73.05
REMARK 500 SER A 144 81.68 -152.74
REMARK 500 SER A 217 -65.70 8.76
REMARK 500 ARG A 320 104.35 -162.42
REMARK 500 VAL A 325 -35.34 -139.16
REMARK 500 GLN A 477 -52.77 71.99
REMARK 500 MET A 580 -164.75 65.28
REMARK 500 ALA A 581 80.85 99.64
REMARK 500 ASP A 628 58.52 -107.95
REMARK 500 MET A 660 -62.50 -106.75
REMARK 500 ASN A 665 57.95 -105.41
REMARK 500 PHE A 669 85.84 -175.60
REMARK 500 ASN A 833 72.49 49.74
REMARK 500 LYS A 836 -107.33 -74.92
REMARK 500 VAL A 837 151.66 70.18
REMARK 500 ARG A 917 67.49 72.02
REMARK 500 ALA A 938 -71.30 -66.29
REMARK 500 PRO A 940 70.14 -114.38
REMARK 500 LEU A 942 -90.86 -130.49
REMARK 500 THR B 7 49.21 -93.06
REMARK 500 ARG B 8 -95.81 -152.78
REMARK 500 VAL B 157 -78.39 -128.31
REMARK 500 CYS B 177 49.45 -97.93
REMARK 500 VAL B 193 -59.30 -125.20
REMARK 500 GLN B 199 94.66 -69.99
REMARK 500 ASP B 241 77.67 -100.79
REMARK 500 LEU B 258 -9.16 88.93
REMARK 500 CYS B 374 -133.54 -98.35
REMARK 500 ASN B 376 -151.45 58.79
REMARK 500 GLN B 440 39.91 -94.90
REMARK 500 CYS B 448 66.34 -106.32
REMARK 500 GLU B 472 -75.02 -76.98
REMARK 500 GLU B 475 -71.08 -149.51
REMARK 500 GLN B 505 117.79 -169.89
REMARK 500 PHE B 526 23.26 -162.67
REMARK 500 TYR B 531 -61.04 -107.11
REMARK 500 SER B 576 -109.59 45.91
REMARK 500 CYS B 601 86.31 -161.45
REMARK 500 THR B 609 -78.22 -164.46
REMARK 500 GLU B 616 -51.70 -142.92
REMARK 500 THR B 630 38.17 -160.47
REMARK 500 ARG B 636 48.31 -152.27
REMARK 500 GLU B 644 74.18 60.41
REMARK 500 ASP B 647 59.64 -167.64
REMARK 500 LYS B 650 -56.45 -159.57
REMARK 500 ASP B 651 32.91 -99.80
REMARK 500 ALA B 652 -151.18 -177.99
REMARK 500 ASN B 659 -169.39 -77.20
REMARK 500
REMARK 500 THIS ENTRY HAS 94 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 ASP A 245 OD1 96.9
REMARK 620 3 ASP A 247 O 84.3 81.0
REMARK 620 4 THR A 250 O 93.1 169.2 95.9
REMARK 620 5 THR A 250 OG1 167.9 88.0 85.5 81.4
REMARK 620 6 GLU A 252 OE1 75.7 73.1 144.8 113.6 116.4
REMARK 620 7 GLU A 252 OE2 121.8 78.3 148.2 99.9 70.0 47.1
REMARK 620 N 1 2 3 4 5 6
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 73.2
REMARK 620 3 ASP A 301 OD1 73.1 76.6
REMARK 620 4 ARG A 303 O 82.2 155.5 97.5
REMARK 620 5 ASP A 305 OD1 130.2 106.1 156.6 88.8
REMARK 620 6 ASP A 305 OD2 85.9 72.5 146.5 105.3 49.6
REMARK 620 7 HOH A 960 O 145.2 79.7 79.7 123.2 78.0 106.6
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 OD1
REMARK 620 2 ASP A 367 OD1 95.6
REMARK 620 3 ASP A 369 OD1 87.0 93.8
REMARK 620 4 TYR A 371 O 78.1 172.5 90.1
REMARK 620 5 ASP A 373 OD1 131.3 111.3 128.5 70.8
REMARK 620 6 ASP A 373 OD2 99.6 83.1 172.9 93.7 48.0
REMARK 620 7 HOH A 961 O 148.3 105.7 68.7 81.7 61.6 106.0
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 77.5
REMARK 620 3 ASN A 430 OD1 85.8 85.0
REMARK 620 4 TYR A 432 O 83.8 160.4 87.7
REMARK 620 5 ASP A 434 OD1 134.5 117.1 135.5 80.5
REMARK 620 6 ASP A 434 OD2 91.3 86.2 171.1 100.3 50.7
REMARK 620 7 HOH A 962 O 148.4 73.4 79.7 123.1 71.8 98.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2008 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 602 O
REMARK 620 2 ASP A 605 OD1 78.1
REMARK 620 3 VAL A 607 O 94.5 102.3
REMARK 620 4 GLU A 642 OE1 94.8 172.9 77.1
REMARK 620 5 GLU A 642 OE2 67.3 128.9 116.3 47.2
REMARK 620 6 HOH A1044 O 169.1 95.0 78.6 91.8 123.2
REMARK 620 7 HOH A1045 O 88.3 64.3 165.5 116.9 77.9 96.3
REMARK 620 N 1 2 3 4 5 6
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 GLU B 220 OE2 110.7
REMARK 620 3 HOH B 692 O 91.1 139.7
REMARK 620 4 HOH B 756 O 116.3 93.5 106.9
REMARK 620 5 HOH B 757 O 87.5 72.3 75.4 155.8
REMARK 620 6 HOH B 761 O 160.9 68.8 79.7 82.5 74.1
REMARK 620 N 1 2 3 4 5
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 SER B 123 O
REMARK 620 2 ASP B 126 OD1 73.4
REMARK 620 3 ASP B 127 OD1 101.1 64.4
REMARK 620 4 MET B 335 O 173.4 110.1 76.1
REMARK 620 5 HOH B 693 O 114.0 139.4 75.1 59.6
REMARK 620 6 HOH B 694 O 96.5 163.9 130.9 81.2 56.0
REMARK 620 N 1 2 3 4 5
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 118.3
REMARK 620 3 ASP B 217 O 155.7 85.4
REMARK 620 4 ASP B 217 OD1 98.9 116.9 72.4
REMARK 620 5 PRO B 219 O 78.3 135.4 80.7 98.9
REMARK 620 6 GLU B 220 OE1 84.3 70.2 100.4 168.7 71.0
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 46.1
REMARK 620 3 ASP C 245 OD1 105.1 59.3
REMARK 620 4 ASP C 247 O 78.5 71.2 84.7
REMARK 620 5 THR C 250 O 84.2 129.1 168.9 91.5
REMARK 620 6 THR C 250 OG1 155.9 137.5 86.7 81.8 82.5
REMARK 620 7 GLU C 252 OE1 79.7 70.8 70.9 141.5 117.3 124.4
REMARK 620 8 GLU C 252 OE2 122.8 119.8 86.1 158.5 93.9 78.3 50.9
REMARK 620 N 1 2 3 4 5 6 7
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 ASP C 297 OD1
REMARK 620 2 ASN C 299 OD1 82.5
REMARK 620 3 ASP C 301 OD1 80.4 76.1
REMARK 620 4 ARG C 303 O 89.1 171.3 104.5
REMARK 620 5 ASP C 305 OD1 128.5 103.2 151.0 80.5
REMARK 620 6 ASP C 305 OD2 85.2 77.2 151.1 100.1 48.3
REMARK 620 7 HOH C 961 O 152.6 78.7 75.8 109.9 75.7 109.6
REMARK 620 N 1 2 3 4 5 6
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 ASP C 365 OD1
REMARK 620 2 ASP C 367 OD1 81.7
REMARK 620 3 ASP C 369 OD1 79.6 83.1
REMARK 620 4 TYR C 371 O 83.1 164.5 91.3
REMARK 620 5 ASP C 373 OD1 139.2 115.1 136.6 78.8
REMARK 620 6 ASP C 373 OD2 100.0 83.8 166.9 101.8 49.7
REMARK 620 7 HOH C1012 O 151.1 99.2 71.9 92.7 66.6 108.8
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 ASP C 426 OD1
REMARK 620 2 ASP C 428 OD1 76.9
REMARK 620 3 ASN C 430 OD1 86.7 80.4
REMARK 620 4 TYR C 432 O 79.8 155.1 89.8
REMARK 620 5 ASP C 434 OD1 128.8 122.3 139.3 79.6
REMARK 620 6 ASP C 434 OD2 84.3 94.0 170.3 92.2 50.3
REMARK 620 7 HOH C 962 O 148.9 72.2 85.1 130.0 72.9 100.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2008 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 602 O
REMARK 620 2 ASP C 605 OD1 76.0
REMARK 620 3 VAL C 607 O 92.7 94.6
REMARK 620 4 GLU C 642 OE1 96.9 165.4 72.7
REMARK 620 5 GLU C 642 OE2 71.1 135.7 115.5 49.7
REMARK 620 6 HOH C1007 O 173.6 104.6 80.9 81.0 111.4
REMARK 620 7 HOH C1056 O 85.8 60.8 154.9 132.3 87.7 100.1
REMARK 620 N 1 2 3 4 5 6
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 SER D 121 OG
REMARK 620 2 GLU D 220 OE2 91.0
REMARK 620 3 HOH D 692 O 71.7 84.8
REMARK 620 4 HOH D 781 O 80.3 157.9 73.2
REMARK 620 5 HOH D 782 O 157.1 99.3 88.8 82.6
REMARK 620 6 HOH D 787 O 76.7 119.2 140.5 78.7 114.7
REMARK 620 N 1 2 3 4 5
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 SER D 123 O
REMARK 620 2 ASP D 126 OD1 90.2
REMARK 620 3 ASP D 127 OD1 98.8 69.1
REMARK 620 4 MET D 335 O 146.9 118.4 78.3
REMARK 620 5 HOH D 694 O 80.0 160.0 94.9 67.5
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 109.9
REMARK 620 3 ASP D 217 O 167.1 82.6
REMARK 620 4 ASP D 217 OD1 105.4 97.3 68.8
REMARK 620 5 PRO D 219 O 81.4 157.1 88.0 98.6
REMARK 620 6 GLU D 220 OE1 87.2 81.1 98.2 167.0 79.7
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FCU RELATED DB: PDB
DBREF 3FCS A 1 958 UNP Q17R67 Q17R67_HUMAN 32 989
DBREF 3FCS B 1 690 UNP P05106 ITB3_HUMAN 27 716
DBREF 3FCS C 1 958 UNP Q17R67 Q17R67_HUMAN 32 989
DBREF 3FCS D 1 690 UNP P05106 ITB3_HUMAN 27 716
SEQADV 3FCS CYS A 959 UNP Q17R67 EXPRESSION TAG
SEQADV 3FCS CYS B 688 UNP P05106 PRO 714 ENGINEERED MUTATION
SEQADV 3FCS CYS C 959 UNP Q17R67 EXPRESSION TAG
SEQADV 3FCS CYS D 688 UNP P05106 PRO 714 ENGINEERED MUTATION
SEQRES 1 A 959 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 A 959 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 A 959 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 A 959 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 A 959 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 A 959 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 A 959 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 A 959 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 A 959 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 A 959 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 A 959 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 A 959 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 A 959 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 A 959 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 A 959 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 A 959 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 A 959 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 A 959 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 A 959 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 A 959 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 A 959 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 A 959 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 A 959 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 A 959 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 A 959 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 A 959 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 A 959 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 A 959 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 A 959 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 A 959 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 A 959 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 A 959 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 A 959 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 A 959 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 A 959 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 A 959 ALA SER VAL GLN LEU LEU VAL GLN ASP SER LEU ASN PRO
SEQRES 37 A 959 ALA VAL LYS SER CYS VAL LEU PRO GLN THR LYS THR PRO
SEQRES 38 A 959 VAL SER CYS PHE ASN ILE GLN MET CYS VAL GLY ALA THR
SEQRES 39 A 959 GLY HIS ASN ILE PRO GLN LYS LEU SER LEU ASN ALA GLU
SEQRES 40 A 959 LEU GLN LEU ASP ARG GLN LYS PRO ARG GLN GLY ARG ARG
SEQRES 41 A 959 VAL LEU LEU LEU GLY SER GLN GLN ALA GLY THR THR LEU
SEQRES 42 A 959 ASN LEU ASP LEU GLY GLY LYS HIS SER PRO ILE CYS HIS
SEQRES 43 A 959 THR THR MET ALA PHE LEU ARG ASP GLU ALA ASP PHE ARG
SEQRES 44 A 959 ASP LYS LEU SER PRO ILE VAL LEU SER LEU ASN VAL SER
SEQRES 45 A 959 LEU PRO PRO THR GLU ALA GLY MET ALA PRO ALA VAL VAL
SEQRES 46 A 959 LEU HIS GLY ASP THR HIS VAL GLN GLU GLN THR ARG ILE
SEQRES 47 A 959 VAL LEU ASP CYS GLY GLU ASP ASP VAL CYS VAL PRO GLN
SEQRES 48 A 959 LEU GLN LEU THR ALA SER VAL THR GLY SER PRO LEU LEU
SEQRES 49 A 959 VAL GLY ALA ASP ASN VAL LEU GLU LEU GLN MET ASP ALA
SEQRES 50 A 959 ALA ASN GLU GLY GLU GLY ALA TYR GLU ALA GLU LEU ALA
SEQRES 51 A 959 VAL HIS LEU PRO GLN GLY ALA HIS TYR MET ARG ALA LEU
SEQRES 52 A 959 SER ASN VAL GLU GLY PHE GLU ARG LEU ILE CYS ASN GLN
SEQRES 53 A 959 LYS LYS GLU ASN GLU THR ARG VAL VAL LEU CYS GLU LEU
SEQRES 54 A 959 GLY ASN PRO MET LYS LYS ASN ALA GLN ILE GLY ILE ALA
SEQRES 55 A 959 MET LEU VAL SER VAL GLY ASN LEU GLU GLU ALA GLY GLU
SEQRES 56 A 959 SER VAL SER PHE GLN LEU GLN ILE ARG SER LYS ASN SER
SEQRES 57 A 959 GLN ASN PRO ASN SER LYS ILE VAL LEU LEU ASP VAL PRO
SEQRES 58 A 959 VAL ARG ALA GLU ALA GLN VAL GLU LEU ARG GLY ASN SER
SEQRES 59 A 959 PHE PRO ALA SER LEU VAL VAL ALA ALA GLU GLU GLY GLU
SEQRES 60 A 959 ARG GLU GLN ASN SER LEU ASP SER TRP GLY PRO LYS VAL
SEQRES 61 A 959 GLU HIS THR TYR GLU LEU HIS ASN ASN GLY PRO GLY THR
SEQRES 62 A 959 VAL ASN GLY LEU HIS LEU SER ILE HIS LEU PRO GLY GLN
SEQRES 63 A 959 SER GLN PRO SER ASP LEU LEU TYR ILE LEU ASP ILE GLN
SEQRES 64 A 959 PRO GLN GLY GLY LEU GLN CYS PHE PRO GLN PRO PRO VAL
SEQRES 65 A 959 ASN PRO LEU LYS VAL ASP TRP GLY LEU PRO ILE PRO SER
SEQRES 66 A 959 PRO SER PRO ILE HIS PRO ALA HIS HIS LYS ARG ASP ARG
SEQRES 67 A 959 ARG GLN ILE PHE LEU PRO GLU PRO GLU GLN PRO SER ARG
SEQRES 68 A 959 LEU GLN ASP PRO VAL LEU VAL SER CYS ASP SER ALA PRO
SEQRES 69 A 959 CYS THR VAL VAL GLN CYS ASP LEU GLN GLU MET ALA ARG
SEQRES 70 A 959 GLY GLN ARG ALA MET VAL THR VAL LEU ALA PHE LEU TRP
SEQRES 71 A 959 LEU PRO SER LEU TYR GLN ARG PRO LEU ASP GLN PHE VAL
SEQRES 72 A 959 LEU GLN SER HIS ALA TRP PHE ASN VAL SER SER LEU PRO
SEQRES 73 A 959 TYR ALA VAL PRO PRO LEU SER LEU PRO ARG GLY GLU ALA
SEQRES 74 A 959 GLN VAL TRP THR GLN LEU LEU ARG ALA CYS
SEQRES 1 B 690 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 690 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 690 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 690 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 690 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 690 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 690 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 690 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 690 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 690 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 690 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 690 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 690 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 690 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 690 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 690 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 690 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 690 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 690 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 690 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 690 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 690 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 690 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 690 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 690 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 690 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 690 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 690 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 690 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 690 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 690 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 690 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 690 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 690 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 B 690 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 B 690 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 B 690 SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER
SEQRES 38 B 690 GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL
SEQRES 39 B 690 CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL
SEQRES 40 B 690 CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR
SEQRES 41 B 690 CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY
SEQRES 42 B 690 GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP
SEQRES 43 B 690 CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN
SEQRES 44 B 690 CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY
SEQRES 45 B 690 LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER
SEQRES 46 B 690 CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS
SEQRES 47 B 690 GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS
SEQRES 48 B 690 LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA
SEQRES 49 B 690 LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP
SEQRES 50 B 690 GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS
SEQRES 51 B 690 ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS
SEQRES 52 B 690 VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS
SEQRES 53 B 690 SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS CYS LYS
SEQRES 54 B 690 GLY
SEQRES 1 C 959 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 C 959 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 C 959 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 C 959 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 C 959 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 C 959 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 C 959 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 C 959 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 C 959 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 C 959 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 C 959 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 C 959 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 C 959 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 C 959 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 C 959 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 C 959 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 C 959 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 C 959 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 C 959 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 C 959 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 C 959 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 C 959 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 C 959 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 C 959 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 C 959 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 C 959 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 C 959 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 C 959 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 C 959 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 C 959 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 C 959 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 C 959 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 C 959 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 C 959 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 C 959 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 C 959 ALA SER VAL GLN LEU LEU VAL GLN ASP SER LEU ASN PRO
SEQRES 37 C 959 ALA VAL LYS SER CYS VAL LEU PRO GLN THR LYS THR PRO
SEQRES 38 C 959 VAL SER CYS PHE ASN ILE GLN MET CYS VAL GLY ALA THR
SEQRES 39 C 959 GLY HIS ASN ILE PRO GLN LYS LEU SER LEU ASN ALA GLU
SEQRES 40 C 959 LEU GLN LEU ASP ARG GLN LYS PRO ARG GLN GLY ARG ARG
SEQRES 41 C 959 VAL LEU LEU LEU GLY SER GLN GLN ALA GLY THR THR LEU
SEQRES 42 C 959 ASN LEU ASP LEU GLY GLY LYS HIS SER PRO ILE CYS HIS
SEQRES 43 C 959 THR THR MET ALA PHE LEU ARG ASP GLU ALA ASP PHE ARG
SEQRES 44 C 959 ASP LYS LEU SER PRO ILE VAL LEU SER LEU ASN VAL SER
SEQRES 45 C 959 LEU PRO PRO THR GLU ALA GLY MET ALA PRO ALA VAL VAL
SEQRES 46 C 959 LEU HIS GLY ASP THR HIS VAL GLN GLU GLN THR ARG ILE
SEQRES 47 C 959 VAL LEU ASP CYS GLY GLU ASP ASP VAL CYS VAL PRO GLN
SEQRES 48 C 959 LEU GLN LEU THR ALA SER VAL THR GLY SER PRO LEU LEU
SEQRES 49 C 959 VAL GLY ALA ASP ASN VAL LEU GLU LEU GLN MET ASP ALA
SEQRES 50 C 959 ALA ASN GLU GLY GLU GLY ALA TYR GLU ALA GLU LEU ALA
SEQRES 51 C 959 VAL HIS LEU PRO GLN GLY ALA HIS TYR MET ARG ALA LEU
SEQRES 52 C 959 SER ASN VAL GLU GLY PHE GLU ARG LEU ILE CYS ASN GLN
SEQRES 53 C 959 LYS LYS GLU ASN GLU THR ARG VAL VAL LEU CYS GLU LEU
SEQRES 54 C 959 GLY ASN PRO MET LYS LYS ASN ALA GLN ILE GLY ILE ALA
SEQRES 55 C 959 MET LEU VAL SER VAL GLY ASN LEU GLU GLU ALA GLY GLU
SEQRES 56 C 959 SER VAL SER PHE GLN LEU GLN ILE ARG SER LYS ASN SER
SEQRES 57 C 959 GLN ASN PRO ASN SER LYS ILE VAL LEU LEU ASP VAL PRO
SEQRES 58 C 959 VAL ARG ALA GLU ALA GLN VAL GLU LEU ARG GLY ASN SER
SEQRES 59 C 959 PHE PRO ALA SER LEU VAL VAL ALA ALA GLU GLU GLY GLU
SEQRES 60 C 959 ARG GLU GLN ASN SER LEU ASP SER TRP GLY PRO LYS VAL
SEQRES 61 C 959 GLU HIS THR TYR GLU LEU HIS ASN ASN GLY PRO GLY THR
SEQRES 62 C 959 VAL ASN GLY LEU HIS LEU SER ILE HIS LEU PRO GLY GLN
SEQRES 63 C 959 SER GLN PRO SER ASP LEU LEU TYR ILE LEU ASP ILE GLN
SEQRES 64 C 959 PRO GLN GLY GLY LEU GLN CYS PHE PRO GLN PRO PRO VAL
SEQRES 65 C 959 ASN PRO LEU LYS VAL ASP TRP GLY LEU PRO ILE PRO SER
SEQRES 66 C 959 PRO SER PRO ILE HIS PRO ALA HIS HIS LYS ARG ASP ARG
SEQRES 67 C 959 ARG GLN ILE PHE LEU PRO GLU PRO GLU GLN PRO SER ARG
SEQRES 68 C 959 LEU GLN ASP PRO VAL LEU VAL SER CYS ASP SER ALA PRO
SEQRES 69 C 959 CYS THR VAL VAL GLN CYS ASP LEU GLN GLU MET ALA ARG
SEQRES 70 C 959 GLY GLN ARG ALA MET VAL THR VAL LEU ALA PHE LEU TRP
SEQRES 71 C 959 LEU PRO SER LEU TYR GLN ARG PRO LEU ASP GLN PHE VAL
SEQRES 72 C 959 LEU GLN SER HIS ALA TRP PHE ASN VAL SER SER LEU PRO
SEQRES 73 C 959 TYR ALA VAL PRO PRO LEU SER LEU PRO ARG GLY GLU ALA
SEQRES 74 C 959 GLN VAL TRP THR GLN LEU LEU ARG ALA CYS
SEQRES 1 D 690 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 D 690 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 D 690 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 D 690 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 D 690 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 D 690 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 D 690 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 D 690 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 D 690 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 D 690 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 D 690 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 D 690 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 D 690 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 D 690 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 D 690 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 D 690 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 D 690 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 D 690 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 D 690 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 D 690 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 D 690 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 D 690 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 D 690 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 D 690 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 D 690 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 D 690 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 D 690 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 D 690 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 D 690 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 D 690 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 D 690 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 D 690 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 D 690 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 D 690 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 D 690 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 D 690 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 D 690 SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER
SEQRES 38 D 690 GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL
SEQRES 39 D 690 CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL
SEQRES 40 D 690 CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR
SEQRES 41 D 690 CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY
SEQRES 42 D 690 GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP
SEQRES 43 D 690 CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN
SEQRES 44 D 690 CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY
SEQRES 45 D 690 LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER
SEQRES 46 D 690 CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS
SEQRES 47 D 690 GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS
SEQRES 48 D 690 LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA
SEQRES 49 D 690 LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP
SEQRES 50 D 690 GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS
SEQRES 51 D 690 ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS
SEQRES 52 D 690 VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS
SEQRES 53 D 690 SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS CYS LYS
SEQRES 54 D 690 GLY
MODRES 3FCS ASN A 15 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN A 570 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN B 99 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN B 320 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN B 371 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN B 452 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN B 559 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN C 15 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN C 249 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN C 570 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN D 99 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN D 320 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN D 371 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN D 452 ASN GLYCOSYLATION SITE
MODRES 3FCS ASN D 559 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET MAN F 3 11
HET MAN F 4 11
HET NAG G 1 14
HET NAG G 2 14
HET MAN G 3 11
HET NAG H 1 14
HET NAG H 2 14
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 NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET CA A2004 1
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET CA A2008 1
HET NAG A3015 14
HET NAG A3570 14
HET IMD A5001 5
HET MG B2001 1
HET CA B2002 1
HET CA B2003 1
HET CA C2004 1
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET CA C2008 1
HET NAG C3015 14
HET NAG C3570 14
HET IMD C5001 5
HET IMD C 960 5
HET IMD C5002 5
HET IMD C5003 5
HET IMD C5004 5
HET MG D2001 1
HET CA D2002 1
HET CA D2003 1
HET NAG D3099 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM IMD IMIDAZOLE
HETNAM MG MAGNESIUM 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
FORMUL 5 NAG 25(C8 H15 N O6)
FORMUL 6 MAN 6(C6 H12 O6)
FORMUL 15 CA 14(CA 2+)
FORMUL 22 IMD 6(C3 H5 N2 1+)
FORMUL 23 MG 2(MG 2+)
FORMUL 42 HOH *678(H2 O)
HELIX 1 1 SER A 152 GLU A 157 1 6
HELIX 2 2 GLY A 188 PHE A 191 1 4
HELIX 3 3 VAL A 200 SER A 206 1 7
HELIX 4 4 PRO A 228 TYR A 230 1 3
HELIX 5 5 TRP A 260 THR A 263 1 4
HELIX 6 6 TYR A 440 ALA A 442 1 3
HELIX 7 7 ARG A 516 GLY A 518 1 3
HELIX 8 8 GLU A 555 ASP A 557 1 3
HELIX 9 9 LEU A 911 LEU A 914 1 4
HELIX 10 10 CYS B 13 VAL B 19 1 7
HELIX 11 11 LYS B 41 LYS B 46 1 6
HELIX 12 12 PRO B 51 SER B 53 1 3
HELIX 13 13 TYR B 122 SER B 130 1 9
HELIX 14 14 THR B 136 LEU B 145 1 10
HELIX 15 15 VAL B 200 VAL B 207 1 8
HELIX 16 16 GLY B 222 VAL B 231 1 10
HELIX 17 17 ASP B 233 ILE B 236 1 4
HELIX 18 18 ASP B 259 ALA B 263 1 5
HELIX 19 19 SER B 282 THR B 285 1 4
HELIX 20 20 LEU B 292 GLN B 301 1 10
HELIX 21 21 GLU B 312 LEU B 324 1 13
HELIX 22 22 VAL B 340 ILE B 351 1 12
HELIX 23 23 ALA B 436 GLN B 438 1 3
HELIX 24 24 VAL B 494 GLN B 497 1 4
HELIX 25 25 CYS B 536 GLY B 538 1 3
HELIX 26 26 GLU B 613 VAL B 615 1 3
HELIX 27 27 SER C 152 GLU C 157 1 6
HELIX 28 28 GLY C 188 PHE C 191 1 4
HELIX 29 29 VAL C 200 SER C 206 1 7
HELIX 30 30 PRO C 228 TYR C 230 1 3
HELIX 31 31 TRP C 260 THR C 263 1 4
HELIX 32 32 TYR C 440 ALA C 442 1 3
HELIX 33 33 ARG C 516 GLY C 518 1 3
HELIX 34 34 GLU C 555 ASP C 557 1 3
HELIX 35 35 LEU C 911 LEU C 914 1 4
HELIX 36 36 CYS D 13 VAL D 19 1 7
HELIX 37 37 LYS D 41 LYS D 46 1 6
HELIX 38 38 PRO D 51 SER D 53 1 3
HELIX 39 39 TYR D 122 TRP D 129 1 8
HELIX 40 40 THR D 136 MET D 142 1 7
HELIX 41 41 PRO D 170 GLU D 174 1 5
HELIX 42 42 THR D 201 LYS D 209 1 9
HELIX 43 43 GLY D 222 VAL D 231 1 10
HELIX 44 44 ASP D 233 ILE D 236 1 4
HELIX 45 45 ASP D 259 ALA D 263 1 5
HELIX 46 46 SER D 282 THR D 285 1 4
HELIX 47 47 LEU D 292 GLN D 301 1 10
HELIX 48 48 GLU D 312 LEU D 324 1 13
HELIX 49 49 VAL D 340 ILE D 351 1 12
HELIX 50 50 ALA D 436 GLN D 440 1 5
HELIX 51 51 VAL D 494 GLN D 497 1 4
HELIX 52 52 CYS D 536 GLY D 538 1 3
HELIX 53 53 ALA D 607 PHE D 610 1 4
SHEET 1 1 1 THR A 9 ALA A 12 0
SHEET 1 2 1 SER A 22 LYS A 27 0
SHEET 1 3 1 VAL A 33 ALA A 39 0
SHEET 1 4 1 GLY A 52 PRO A 57 0
SHEET 1 5 1 GLY A 62 GLN A 64 0
SHEET 1 6 1 THR A 76 VAL A 79 0
SHEET 1 7 1 GLN A 82 PHE A 87 0
SHEET 1 8 1 SER A 96 TRP A 100 0
SHEET 1 9 1 VAL A 103 ALA A 108 0
SHEET 1 10 1 HIS A 112 GLU A 117 0
SHEET 1 11 1 GLU A 120 GLU A 121 0
SHEET 1 12 1 SER A 129 GLN A 134 0
SHEET 1 13 1 ARG A 139 TYR A 143 0
SHEET 1 14 1 SER A 172 VAL A 175 0
SHEET 1 15 1 GLU A 180 ALA A 185 0
SHEET 1 16 1 LEU A 194 PRO A 199 0
SHEET 1 17 1 SER A 220 LEU A 221 0
SHEET 1 18 1 SER A 238 GLY A 242 0
SHEET 1 19 1 GLU A 252 ALA A 257 0
SHEET 1 20 1 ALA A 266 LEU A 270 0
SHEET 1 21 1 ARG A 276 ARG A 281 0
SHEET 1 22 1 SER A 292 THR A 296 0
SHEET 1 23 1 ASP A 305 ALA A 310 0
SHEET 1 24 1 MET A 314 ARG A 317 0
SHEET 1 25 1 ARG A 320 GLU A 324 0
SHEET 1 26 1 ARG A 327 PHE A 331 0
SHEET 1 27 1 LEU A 345 THR A 348 0
SHEET 1 28 1 ALA A 359 GLY A 364 0
SHEET 1 29 1 ASP A 373 ALA A 378 0
SHEET 1 30 1 GLN A 388 PHE A 392 0
SHEET 1 31 1 GLY A 394 GLN A 395 0
SHEET 1 32 1 GLY A 398 LEU A 399 0
SHEET 1 33 1 GLN A 405 ASP A 408 0
SHEET 1 34 1 LEU A 421 VAL A 425 0
SHEET 1 35 1 ASP A 434 ALA A 439 0
SHEET 1 36 1 GLN A 444 TYR A 448 0
SHEET 1 37 1 VAL A 453 VAL A 462 0
SHEET 1 38 1 CYS A 473 VAL A 474 0
SHEET 1 39 1 PRO A 481 THR A 494 0
SHEET 1 41 1 SER A 503 LEU A 510 0
SHEET 1 42 1 VAL A 521 LEU A 523 0
SHEET 1 43 1 GLY A 530 ASP A 536 0
SHEET 1 44 1 ILE A 544 LEU A 552 0
SHEET 1 45 1 ILE A 565 SER A 572 0
SHEET 1 46 1 VAL A 585 GLY A 588 0
SHEET 1 47 1 HIS A 591 THR A 596 0
SHEET 1 48 1 LEU A 612 THR A 619 0
SHEET 1 49 1 LEU A 623 LEU A 624 0
SHEET 1 50 1 LEU A 631 ASN A 639 0
SHEET 1 51 1 ALA A 647 HIS A 652 0
SHEET 1 52 1 ALA A 657 SER A 664 0
SHEET 1 53 1 CYS A 674 LYS A 677 0
SHEET 1 54 1 VAL A 684 GLY A 690 0
SHEET 1 55 1 ALA A 697 VAL A 707 0
SHEET 1 56 1 SER A 716 ARG A 724 0
SHEET 1 57 1 VAL A 736 ARG A 743 0
SHEET 1 58 1 VAL A 748 PHE A 755 0
SHEET 1 59 1 SER A 758 VAL A 761 0
SHEET 1 60 1 LYS A 779 ASN A 788 0
SHEET 1 61 1 VAL A 794 PRO A 804 0
SHEET 1 62 1 LEU A 813 GLN A 821 0
SHEET 1 63 1 GLN A 825 GLN A 829 0
SHEET 1 64 1 PRO A 875 VAL A 878 0
SHEET 1 65 1 CYS A 885 MET A 895 0
SHEET 1 66 1 ARG A 900 LEU A 909 0
SHEET 1 67 1 GLN A 921 SER A 934 0
SHEET 1 68 1 ARG A 946 ARG A 957 0
SHEET 1 69 1 ALA B 24 CYS B 26 0
SHEET 1 70 1 CYS B 38 ASP B 39 0
SHEET 1 71 1 ILE B 54 GLU B 55 0
SHEET 1 72 1 GLU B 60 GLU B 65 0
SHEET 1 73 1 VAL B 83 SER B 84 0
SHEET 1 74 1 ARG B 87 LEU B 92 0
SHEET 1 75 1 SER B 97 ARG B 105 0
SHEET 1 76 1 VAL B 112 ASP B 119 0
SHEET 1 77 1 LEU B 149 PHE B 156 0
SHEET 1 78 1 TYR B 190 THR B 197 0
SHEET 1 79 1 SER B 243 THR B 250 0
SHEET 1 80 1 ASN B 305 THR B 311 0
SHEET 1 81 1 THR B 329 LEU B 333 0
SHEET 1 82 1 VAL B 355 ARG B 360 0
SHEET 1 83 1 LEU B 366 THR B 373 0
SHEET 1 84 1 VAL B 379 PRO B 381 0
SHEET 1 85 1 SER B 385 CYS B 386 0
SHEET 1 86 1 THR B 394 VAL B 403 0
SHEET 1 87 1 GLU B 411 PRO B 418 0
SHEET 1 88 1 LEU B 425 PHE B 431 0
SHEET 1 89 1 GLY B 453 GLU B 456 0
SHEET 1 90 1 VAL B 459 CYS B 462 0
SHEET 1 91 1 GLY B 499 CYS B 501 0
SHEET 1 92 1 CYS B 506 CYS B 508 0
SHEET 1 93 1 GLY B 540 SER B 543 0
SHEET 1 94 1 ASP B 546 CYS B 549 0
SHEET 1 95 1 TRP B 553 THR B 554 0
SHEET 1 96 1 CYS B 560 THR B 561 0
SHEET 1 97 1 LYS B 580 GLU B 582 0
SHEET 1 98 1 SER B 585 VAL B 587 0
SHEET 1 99 1 GLU B 638 GLU B 640 0
SHEET 1 100 1 ASN B 654 LYS B 658 0
SHEET 1 101 1 CYS B 663 GLN B 668 0
SHEET 1 102 1 ILE B 678 TYR B 680 0
SHEET 1 103 1 GLU B 686 CYS B 687 0
SHEET 1 104 1 THR C 9 ALA C 12 0
SHEET 1 105 1 SER C 22 LYS C 27 0
SHEET 1 106 1 VAL C 33 ALA C 39 0
SHEET 1 107 1 GLY C 52 PRO C 57 0
SHEET 1 108 1 GLY C 63 GLN C 64 0
SHEET 1 109 1 THR C 76 VAL C 79 0
SHEET 1 110 1 GLN C 82 PHE C 87 0
SHEET 1 111 1 SER C 96 TRP C 100 0
SHEET 1 112 1 VAL C 103 ALA C 108 0
SHEET 1 113 1 HIS C 112 GLU C 117 0
SHEET 1 114 1 GLU C 120 GLU C 121 0
SHEET 1 115 1 SER C 129 GLN C 134 0
SHEET 1 116 1 ARG C 139 TYR C 143 0
SHEET 1 117 1 SER C 172 VAL C 175 0
SHEET 1 118 1 GLU C 180 ALA C 185 0
SHEET 1 119 1 LEU C 194 PRO C 199 0
SHEET 1 120 1 SER C 220 LEU C 221 0
SHEET 1 121 1 SER C 238 GLY C 242 0
SHEET 1 122 1 GLU C 252 ALA C 257 0
SHEET 1 123 1 ALA C 266 LEU C 270 0
SHEET 1 124 1 ARG C 276 ARG C 281 0
SHEET 1 125 1 SER C 292 THR C 296 0
SHEET 1 126 1 ASP C 305 ALA C 310 0
SHEET 1 127 1 MET C 314 ARG C 317 0
SHEET 1 128 1 ARG C 320 GLU C 324 0
SHEET 1 129 1 ARG C 327 PHE C 331 0
SHEET 1 130 1 LEU C 345 THR C 348 0
SHEET 1 131 1 ALA C 359 GLY C 364 0
SHEET 1 132 1 ASP C 373 ALA C 378 0
SHEET 1 133 1 GLN C 388 PHE C 392 0
SHEET 1 134 1 GLY C 394 GLN C 395 0
SHEET 1 135 1 GLY C 398 LEU C 399 0
SHEET 1 136 1 GLN C 405 ASP C 408 0
SHEET 1 137 1 SER C 420 VAL C 425 0
SHEET 1 138 1 ASP C 434 ALA C 439 0
SHEET 1 139 1 GLN C 444 TYR C 448 0
SHEET 1 140 1 VAL C 453 VAL C 462 0
SHEET 1 141 1 CYS C 473 VAL C 474 0
SHEET 1 142 1 PRO C 481 THR C 494 0
SHEET 1 143 1 SER C 503 LEU C 510 0
SHEET 1 144 1 VAL C 521 LEU C 523 0
SHEET 1 145 1 GLY C 530 ASP C 536 0
SHEET 1 146 1 ILE C 544 LEU C 552 0
SHEET 1 147 1 ILE C 565 SER C 572 0
SHEET 1 148 1 VAL C 585 GLY C 588 0
SHEET 1 149 1 HIS C 591 THR C 596 0
SHEET 1 150 1 LEU C 612 THR C 619 0
SHEET 1 151 1 LEU C 623 LEU C 624 0
SHEET 1 152 1 ASN C 629 ASN C 639 0
SHEET 1 153 1 ALA C 647 HIS C 652 0
SHEET 1 154 1 ALA C 657 SER C 664 0
SHEET 1 155 1 CYS C 674 LYS C 677 0
SHEET 1 156 1 VAL C 684 GLY C 690 0
SHEET 1 157 1 ALA C 697 VAL C 707 0
SHEET 1 158 1 SER C 716 ARG C 724 0
SHEET 1 159 1 VAL C 736 ARG C 743 0
SHEET 1 160 1 VAL C 748 PHE C 755 0
SHEET 1 161 1 LYS C 779 ASN C 788 0
SHEET 1 162 1 VAL C 794 PRO C 804 0
SHEET 1 163 1 LEU C 813 GLN C 821 0
SHEET 1 164 1 GLN C 825 GLN C 829 0
SHEET 1 165 1 CYS C 885 MET C 895 0
SHEET 1 166 1 ARG C 900 LEU C 909 0
SHEET 1 167 1 PHE C 922 SER C 934 0
SHEET 1 168 1 ARG C 946 LEU C 955 0
SHEET 1 169 1 CYS D 23 CYS D 26 0
SHEET 1 170 1 CYS D 38 LEU D 40 0
SHEET 1 171 1 ILE D 54 GLU D 55 0
SHEET 1 172 1 GLU D 60 GLU D 65 0
SHEET 1 173 1 VAL D 83 SER D 84 0
SHEET 1 174 1 ARG D 87 LEU D 92 0
SHEET 1 175 1 SER D 97 ARG D 105 0
SHEET 1 176 1 VAL D 112 ASP D 119 0
SHEET 1 177 1 LEU D 149 PHE D 156 0
SHEET 1 178 1 TYR D 190 THR D 197 0
SHEET 1 179 1 SER D 243 THR D 250 0
SHEET 1 180 1 ASN D 305 THR D 311 0
SHEET 1 181 1 THR D 328 LEU D 333 0
SHEET 1 182 1 VAL D 355 ARG D 360 0
SHEET 1 183 1 LEU D 366 SER D 367 0
SHEET 1 184 1 PHE D 370 THR D 373 0
SHEET 1 185 1 VAL D 379 PRO D 381 0
SHEET 1 186 1 SER D 385 CYS D 386 0
SHEET 1 187 1 THR D 394 VAL D 403 0
SHEET 1 188 1 GLU D 411 PRO D 418 0
SHEET 1 189 1 LEU D 425 PHE D 431 0
SHEET 1 190 1 GLY D 453 PHE D 455 0
SHEET 1 191 1 CYS D 460 CYS D 462 0
SHEET 1 192 1 GLY D 499 CYS D 501 0
SHEET 1 193 1 CYS D 506 CYS D 508 0
SHEET 1 194 1 GLY D 540 SER D 543 0
SHEET 1 195 1 ASP D 546 CYS D 549 0
SHEET 1 196 1 TRP D 553 THR D 554 0
SHEET 1 197 1 CYS D 560 THR D 561 0
SHEET 1 198 1 GLY D 579 GLU D 582 0
SHEET 1 199 1 SER D 585 CYS D 588 0
SSBOND 1 CYS A 56 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.04
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.03
SSBOND 4 CYS A 473 CYS A 484 1555 1555 2.03
SSBOND 5 CYS A 490 CYS A 545 1555 1555 2.04
SSBOND 6 CYS A 602 CYS A 608 1555 1555 2.04
SSBOND 7 CYS A 674 CYS A 687 1555 1555 2.04
SSBOND 8 CYS A 826 CYS A 890 1555 1555 2.04
SSBOND 9 CYS A 880 CYS A 885 1555 1555 2.02
SSBOND 10 CYS A 959 CYS B 688 1555 1555 2.03
SSBOND 11 CYS B 5 CYS B 23 1555 1555 2.03
SSBOND 12 CYS B 13 CYS B 435 1555 1555 2.03
SSBOND 13 CYS B 16 CYS B 38 1555 1555 2.03
SSBOND 14 CYS B 26 CYS B 49 1555 1555 2.03
SSBOND 15 CYS B 177 CYS B 184 1555 1555 2.04
SSBOND 16 CYS B 232 CYS B 273 1555 1555 2.03
SSBOND 17 CYS B 374 CYS B 386 1555 1555 2.03
SSBOND 18 CYS B 406 CYS B 433 1555 1555 2.04
SSBOND 19 CYS B 437 CYS B 457 1555 1555 2.03
SSBOND 20 CYS B 448 CYS B 460 1555 1555 2.03
SSBOND 21 CYS B 462 CYS B 471 1555 1555 2.03
SSBOND 22 CYS B 473 CYS B 503 1555 1555 2.04
SSBOND 23 CYS B 486 CYS B 501 1555 1555 2.03
SSBOND 24 CYS B 495 CYS B 506 1555 1555 2.03
SSBOND 25 CYS B 508 CYS B 521 1555 1555 2.04
SSBOND 26 CYS B 523 CYS B 544 1555 1555 2.04
SSBOND 27 CYS B 528 CYS B 542 1555 1555 2.03
SSBOND 28 CYS B 536 CYS B 547 1555 1555 2.03
SSBOND 29 CYS B 549 CYS B 558 1555 1555 2.04
SSBOND 30 CYS B 560 CYS B 583 1555 1555 2.04
SSBOND 31 CYS B 567 CYS B 581 1555 1555 2.03
SSBOND 32 CYS B 575 CYS B 586 1555 1555 2.04
SSBOND 33 CYS B 588 CYS B 598 1555 1555 2.03
SSBOND 34 CYS B 601 CYS B 604 1555 1555 2.03
SSBOND 35 CYS B 608 CYS B 655 1555 1555 2.03
SSBOND 36 CYS B 614 CYS B 635 1555 1555 2.03
SSBOND 37 CYS B 617 CYS B 631 1555 1555 2.03
SSBOND 38 CYS B 663 CYS B 687 1555 1555 2.03
SSBOND 39 CYS C 56 CYS C 65 1555 1555 2.03
SSBOND 40 CYS C 107 CYS C 130 1555 1555 2.04
SSBOND 41 CYS C 146 CYS C 167 1555 1555 2.03
SSBOND 42 CYS C 473 CYS C 484 1555 1555 2.04
SSBOND 43 CYS C 490 CYS C 545 1555 1555 2.04
SSBOND 44 CYS C 602 CYS C 608 1555 1555 2.04
SSBOND 45 CYS C 674 CYS C 687 1555 1555 2.04
SSBOND 46 CYS C 826 CYS C 890 1555 1555 2.03
SSBOND 47 CYS C 880 CYS C 885 1555 1555 2.03
SSBOND 48 CYS D 5 CYS D 23 1555 1555 2.03
SSBOND 49 CYS D 13 CYS D 435 1555 1555 2.03
SSBOND 50 CYS D 16 CYS D 38 1555 1555 2.03
SSBOND 51 CYS D 26 CYS D 49 1555 1555 2.04
SSBOND 52 CYS D 177 CYS D 184 1555 1555 2.04
SSBOND 53 CYS D 232 CYS D 273 1555 1555 2.04
SSBOND 54 CYS D 374 CYS D 386 1555 1555 2.03
SSBOND 55 CYS D 406 CYS D 433 1555 1555 2.03
SSBOND 56 CYS D 437 CYS D 457 1555 1555 2.03
SSBOND 57 CYS D 448 CYS D 460 1555 1555 2.04
SSBOND 58 CYS D 462 CYS D 471 1555 1555 2.03
SSBOND 59 CYS D 473 CYS D 503 1555 1555 2.03
SSBOND 60 CYS D 486 CYS D 501 1555 1555 2.04
SSBOND 61 CYS D 495 CYS D 506 1555 1555 2.04
SSBOND 62 CYS D 508 CYS D 521 1555 1555 2.03
SSBOND 63 CYS D 523 CYS D 544 1555 1555 2.04
SSBOND 64 CYS D 528 CYS D 542 1555 1555 2.03
SSBOND 65 CYS D 536 CYS D 547 1555 1555 2.04
SSBOND 66 CYS D 549 CYS D 558 1555 1555 2.04
SSBOND 67 CYS D 560 CYS D 583 1555 1555 2.04
SSBOND 68 CYS D 567 CYS D 581 1555 1555 2.03
SSBOND 69 CYS D 575 CYS D 586 1555 1555 2.03
SSBOND 70 CYS D 588 CYS D 598 1555 1555 2.03
SSBOND 71 CYS D 601 CYS D 604 1555 1555 2.03
LINK ND2 ASN A 15 C1 NAG A3015 1555 1555 1.45
LINK ND2 ASN A 570 C1 NAG A3570 1555 1555 1.44
LINK ND2 ASN B 99 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 320 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 371 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN B 452 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 559 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN C 15 C1 NAG C3015 1555 1555 1.44
LINK ND2 ASN C 249 C1 NAG J 1 1555 1555 1.43
LINK ND2 ASN C 570 C1 NAG C3570 1555 1555 1.44
LINK ND2 ASN D 99 C1 NAG D3099 1555 1555 1.44
LINK ND2 ASN D 320 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN D 371 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN D 452 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN D 559 C1 NAG N 1 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG F 2 C1 MAN F 3 1555 1555 1.44
LINK O3 MAN F 3 C1 MAN F 4 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 O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
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 1.44
LINK O2 MAN I 4 C1 MAN I 5 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45
LINK OE1 GLU A 243 CA CA A2004 1555 1555 2.37
LINK OD1 ASP A 245 CA CA A2004 1555 1555 2.48
LINK O ASP A 247 CA CA A2004 1555 1555 2.15
LINK O THR A 250 CA CA A2004 1555 1555 2.40
LINK OG1 THR A 250 CA CA A2004 1555 1555 2.66
LINK OE1 GLU A 252 CA CA A2004 1555 1555 2.59
LINK OE2 GLU A 252 CA CA A2004 1555 1555 2.85
LINK OD1 ASP A 297 CA CA A2005 1555 1555 2.51
LINK OD1 ASN A 299 CA CA A2005 1555 1555 2.26
LINK OD1 ASP A 301 CA CA A2005 1555 1555 2.51
LINK O ARG A 303 CA CA A2005 1555 1555 2.21
LINK OD1 ASP A 305 CA CA A2005 1555 1555 2.38
LINK OD2 ASP A 305 CA CA A2005 1555 1555 2.77
LINK OD1 ASP A 365 CA CA A2006 1555 1555 2.23
LINK OD1 ASP A 367 CA CA A2006 1555 1555 2.10
LINK OD1 ASP A 369 CA CA A2006 1555 1555 2.20
LINK O TYR A 371 CA CA A2006 1555 1555 2.48
LINK OD1 ASP A 373 CA CA A2006 1555 1555 2.70
LINK OD2 ASP A 373 CA CA A2006 1555 1555 2.68
LINK OD1 ASP A 426 CA CA A2007 1555 1555 2.32
LINK OD1 ASP A 428 CA CA A2007 1555 1555 2.35
LINK OD1 ASN A 430 CA CA A2007 1555 1555 2.27
LINK O TYR A 432 CA CA A2007 1555 1555 2.37
LINK OD1 ASP A 434 CA CA A2007 1555 1555 2.55
LINK OD2 ASP A 434 CA CA A2007 1555 1555 2.57
LINK O CYS A 602 CA CA A2008 1555 1555 2.21
LINK OD1 ASP A 605 CA CA A2008 1555 1555 2.53
LINK O VAL A 607 CA CA A2008 1555 1555 2.62
LINK OE1 GLU A 642 CA CA A2008 1555 1555 2.56
LINK OE2 GLU A 642 CA CA A2008 1555 1555 2.87
LINK O HOH A 960 CA CA A2005 1555 1555 2.50
LINK O HOH A 961 CA CA A2006 1555 1555 2.26
LINK O HOH A 962 CA CA A2007 1555 1555 2.38
LINK O HOH A1044 CA CA A2008 1555 1555 2.29
LINK O HOH A1045 CA CA A2008 1555 1555 2.16
LINK OG SER B 121 MG MG B2001 1555 1555 2.30
LINK O SER B 123 CA CA B2002 1555 1555 2.48
LINK OD1 ASP B 126 CA CA B2002 1555 1555 2.63
LINK OD1 ASP B 127 CA CA B2002 1555 1555 2.50
LINK OD2 ASP B 158 CA CA B2003 1555 1555 2.44
LINK OD1 ASN B 215 CA CA B2003 1555 1555 2.13
LINK O ASP B 217 CA CA B2003 1555 1555 2.60
LINK OD1 ASP B 217 CA CA B2003 1555 1555 2.25
LINK O PRO B 219 CA CA B2003 1555 1555 2.39
LINK OE2 GLU B 220 MG MG B2001 1555 1555 2.27
LINK OE1 GLU B 220 CA CA B2003 1555 1555 2.69
LINK O MET B 335 CA CA B2002 1555 1555 2.38
LINK O HOH B 692 MG MG B2001 1555 1555 1.84
LINK O HOH B 693 CA CA B2002 1555 1555 2.63
LINK O HOH B 694 CA CA B2002 1555 1555 2.66
LINK O HOH B 756 MG MG B2001 1555 1555 1.76
LINK O HOH B 757 MG MG B2001 1555 1555 2.35
LINK O HOH B 761 MG MG B2001 1555 1555 2.47
LINK OE1 GLU C 243 CA CA C2004 1555 1555 2.47
LINK OE2 GLU C 243 CA CA C2004 1555 1555 2.99
LINK OD1 ASP C 245 CA CA C2004 1555 1555 2.37
LINK O ASP C 247 CA CA C2004 1555 1555 2.28
LINK O THR C 250 CA CA C2004 1555 1555 2.13
LINK OG1 THR C 250 CA CA C2004 1555 1555 2.51
LINK OE1 GLU C 252 CA CA C2004 1555 1555 2.55
LINK OE2 GLU C 252 CA CA C2004 1555 1555 2.54
LINK OD1 ASP C 297 CA CA C2005 1555 1555 2.27
LINK OD1 ASN C 299 CA CA C2005 1555 1555 2.29
LINK OD1 ASP C 301 CA CA C2005 1555 1555 2.42
LINK O ARG C 303 CA CA C2005 1555 1555 2.16
LINK OD1 ASP C 305 CA CA C2005 1555 1555 2.36
LINK OD2 ASP C 305 CA CA C2005 1555 1555 2.87
LINK OD1 ASP C 365 CA CA C2006 1555 1555 2.44
LINK OD1 ASP C 367 CA CA C2006 1555 1555 2.34
LINK OD1 ASP C 369 CA CA C2006 1555 1555 2.18
LINK O TYR C 371 CA CA C2006 1555 1555 2.32
LINK OD1 ASP C 373 CA CA C2006 1555 1555 2.61
LINK OD2 ASP C 373 CA CA C2006 1555 1555 2.59
LINK OD1 ASP C 426 CA CA C2007 1555 1555 2.29
LINK OD1 ASP C 428 CA CA C2007 1555 1555 2.48
LINK OD1 ASN C 430 CA CA C2007 1555 1555 2.20
LINK O TYR C 432 CA CA C2007 1555 1555 2.37
LINK OD1 ASP C 434 CA CA C2007 1555 1555 2.56
LINK OD2 ASP C 434 CA CA C2007 1555 1555 2.56
LINK O CYS C 602 CA CA C2008 1555 1555 2.22
LINK OD1 ASP C 605 CA CA C2008 1555 1555 2.58
LINK O VAL C 607 CA CA C2008 1555 1555 2.77
LINK OE1 GLU C 642 CA CA C2008 1555 1555 2.61
LINK OE2 GLU C 642 CA CA C2008 1555 1555 2.59
LINK O HOH C 961 CA CA C2005 1555 1555 2.04
LINK O HOH C 962 CA CA C2007 1555 1555 2.29
LINK O HOH C1007 CA CA C2008 1555 1555 2.57
LINK O HOH C1012 CA CA C2006 1555 1555 2.60
LINK O HOH C1056 CA CA C2008 1555 1555 2.54
LINK OG SER D 121 MG MG D2001 1555 1555 2.49
LINK O SER D 123 CA CA D2002 1555 1555 2.50
LINK OD1 ASP D 126 CA CA D2002 1555 1555 2.42
LINK OD1 ASP D 127 CA CA D2002 1555 1555 2.44
LINK OD2 ASP D 158 CA CA D2003 1555 1555 2.36
LINK OD1 ASN D 215 CA CA D2003 1555 1555 2.19
LINK O ASP D 217 CA CA D2003 1555 1555 2.57
LINK OD1 ASP D 217 CA CA D2003 1555 1555 2.22
LINK O PRO D 219 CA CA D2003 1555 1555 2.27
LINK OE2 GLU D 220 MG MG D2001 1555 1555 2.12
LINK OE1 GLU D 220 CA CA D2003 1555 1555 2.40
LINK O MET D 335 CA CA D2002 1555 1555 2.51
LINK O HOH D 692 MG MG D2001 1555 1555 2.44
LINK O HOH D 694 CA CA D2002 1555 1555 2.38
LINK O HOH D 781 MG MG D2001 1555 1555 1.95
LINK O HOH D 782 MG MG D2001 1555 1555 2.11
LINK O HOH D 787 MG MG D2001 1555 1555 1.85
CISPEP 1 ASN A 691 PRO A 692 0 0.64
CISPEP 2 PHE A 755 PRO A 756 0 2.07
CISPEP 3 GLN A 829 PRO A 830 0 0.85
CISPEP 4 SER B 84 PRO B 85 0 3.29
CISPEP 5 SER B 162 PRO B 163 0 2.95
CISPEP 6 SER B 168 PRO B 169 0 -2.14
CISPEP 7 ASN C 691 PRO C 692 0 1.96
CISPEP 8 PHE C 755 PRO C 756 0 1.35
CISPEP 9 GLN C 829 PRO C 830 0 2.25
CISPEP 10 SER D 84 PRO D 85 0 4.53
CISPEP 11 SER D 162 PRO D 163 0 0.99
CISPEP 12 SER D 168 PRO D 169 0 -1.84
CRYST1 81.300 81.300 654.623 90.00 90.00 90.00 P 41 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001528 0.00000
(ATOM LINES ARE NOT SHOWN.)
END