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HEADER CELL ADHESION/BLOOD CLOTTING 15-JUN-10 3NID
TITLE THE CLOSED HEADPIECE OF INTEGRIN ALPHAIIB BETA3 AND ITS COMPLEX WITH
TITLE 2 AN ALPAHIIB BETA3 -SPECIFIC ANTAGONIST THAT DOES NOT INDUCE OPENING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: INTEGRIN ALPHA-IIB, RESIDUES 32-488;
COMPND 5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,
COMPND 6 INTEGRIN ALPHA-IIB HEAVY CHAIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTEGRIN BETA-3;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: INTEGRIN BETA-3, RESIDUES 27-497;
COMPND 12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: MMONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;
COMPND 16 CHAIN: E, H;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: MMONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;
COMPND 20 CHAIN: F, L;
COMPND 21 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, GP2B, ITGAB;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;
SOURCE 10 EXPRESSION_SYSTEM_CELL: CHO;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: ITGB3, GP3A;
SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 19 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;
SOURCE 22 EXPRESSION_SYSTEM_CELL: CHO;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;
SOURCE 25 MOL_ID: 3;
SOURCE 26 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 27 ORGANISM_COMMON: MOUSE;
SOURCE 28 ORGANISM_TAXID: 10090;
SOURCE 29 STRAIN: BALB/C;
SOURCE 30 CELL_LINE: 10E5 HYBRIDOMA;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 33 ORGANISM_COMMON: MOUSE;
SOURCE 34 ORGANISM_TAXID: 10090;
SOURCE 35 STRAIN: BALB/C;
SOURCE 36 CELL_LINE: 10E5 HYBRIDOMA
KEYWDS INTEGRIN, HEADPIECE, ALPHAIIB, BETA3, CELL ADHESION-BLOOD CLOTTING
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.ZHU,J.Q.ZHU,T.A.SPRINGER
REVDAT 1 22-DEC-10 3NID 0
JRNL AUTH J.H.ZHU,J.Q.ZHU,A.NEGRI,D.PROVASI,M.FILIZOLA,B.S.COLLER,
JRNL AUTH 2 T.A.SPRINGER
JRNL TITL CLOSED HEADPIECE OF INTEGRIN {ALPHA}IIB{BETA}3 AND ITS
JRNL TITL 2 COMPLEX WITH AN {ALPHA}IIB{BETA}3-SPECIFIC ANTAGONIST THAT
JRNL TITL 3 DOES NOT INDUCE OPENING.
JRNL REF BLOOD V. 116 5050 2010
JRNL REFN ISSN 0006-4971
JRNL PMID 20679525
JRNL DOI 10.1182/BLOOD-2010-04-281154
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 168819
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1029
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12241
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20715
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 302
REMARK 3 SOLVENT ATOMS : 1059
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.05000
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): 0.217
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.963
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21579 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 14427 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 29409 ; 1.068 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35078 ; 0.780 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2712 ; 5.713 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 930 ;32.897 ;24.355
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3360 ;12.463 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;14.191 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3263 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 24094 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4269 ; 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): 13454 ; 1.845 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5484 ; 0.391 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21723 ; 3.327 ;10.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8125 ; 6.419 ;20.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7676 ; 8.437 ;20.000
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 : 9
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
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 1 A 454 6
REMARK 3 1 C 1 C 454 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 5857 ; 0.300 ;10.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 5857 ; 3.150 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
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 1 B 57 6
REMARK 3 1 D 1 D 57 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 2 B (A): 719 ; 0.510 ;10.000
REMARK 3 LOOSE THERMAL 2 B (A**2): 719 ; 2.820 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 3 B (A): 1651 ; 0.440 ;10.000
REMARK 3 LOOSE THERMAL 3 B (A**2): 1651 ; 2.740 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
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 6
REMARK 3 1 D 109 D 352 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 4 B (A): 3151 ; 0.260 ;10.000
REMARK 3 LOOSE THERMAL 4 B (A**2): 3151 ; 2.750 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
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 433 B 466 6
REMARK 3 1 D 433 D 466 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 5 B (A): 418 ; 0.550 ;10.000
REMARK 3 LOOSE THERMAL 5 B (A**2): 418 ; 2.960 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : H E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 1 H 119 6
REMARK 3 1 E 1 E 119 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 6 H (A): 1555 ; 0.270 ;10.000
REMARK 3 LOOSE THERMAL 6 H (A**2): 1555 ; 2.050 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : H E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 120 H 221 6
REMARK 3 1 E 120 E 221 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 7 H (A): 1166 ; 0.430 ;10.000
REMARK 3 LOOSE THERMAL 7 H (A**2): 1166 ; 2.110 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : L F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 1 L 108 6
REMARK 3 1 F 1 F 108 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 8 L (A): 1358 ; 0.220 ;10.000
REMARK 3 LOOSE THERMAL 8 L (A**2): 1358 ; 2.180 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : L F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 109 L 214 6
REMARK 3 1 F 109 F 214 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 9 L (A): 1388 ; 0.610 ;10.000
REMARK 3 LOOSE THERMAL 9 L (A**2): 1388 ; 3.850 ;20.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 52
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5300 91.1560 38.8290
REMARK 3 T TENSOR
REMARK 3 T11: 0.1115 T22: 0.0930
REMARK 3 T33: 0.0973 T12: 0.0063
REMARK 3 T13: -0.0188 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 3.1594 L22: 2.8255
REMARK 3 L33: 2.3799 L12: -1.2771
REMARK 3 L13: -1.1732 L23: 1.0227
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: 0.2277 S13: 0.0685
REMARK 3 S21: -0.2728 S22: -0.0925 S23: 0.3246
REMARK 3 S31: -0.0798 S32: -0.3807 S33: 0.0627
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 74 A 274
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0020 95.4830 62.6300
REMARK 3 T TENSOR
REMARK 3 T11: 0.1108 T22: 0.0793
REMARK 3 T33: 0.1222 T12: -0.0129
REMARK 3 T13: 0.0715 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.7983 L22: 0.8745
REMARK 3 L33: 0.9889 L12: -0.1062
REMARK 3 L13: -0.0237 L23: 0.3816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.0601 S13: -0.0227
REMARK 3 S21: 0.1712 S22: -0.0750 S23: 0.2380
REMARK 3 S31: 0.0990 S32: -0.2620 S33: 0.0902
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 275 A 334
REMARK 3 ORIGIN FOR THE GROUP (A): 66.4820 86.1120 60.3930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1207 T22: 0.0472
REMARK 3 T33: 0.0894 T12: 0.0523
REMARK 3 T13: -0.0028 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 1.1272 L22: 4.3203
REMARK 3 L33: 2.0267 L12: 0.5630
REMARK 3 L13: -0.2273 L23: -0.0188
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.1472 S13: -0.1364
REMARK 3 S21: 0.2839 S22: 0.0395 S23: -0.4313
REMARK 3 S31: 0.1664 S32: 0.1514 S33: -0.0447
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 335 A 454
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6750 82.8310 45.0520
REMARK 3 T TENSOR
REMARK 3 T11: 0.1086 T22: 0.0163
REMARK 3 T33: 0.0714 T12: 0.0355
REMARK 3 T13: 0.0482 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.5288 L22: 2.4086
REMARK 3 L33: 1.6093 L12: 0.1475
REMARK 3 L13: 0.2345 L23: 0.4449
REMARK 3 S TENSOR
REMARK 3 S11: -0.0505 S12: 0.0057 S13: -0.1365
REMARK 3 S21: 0.0878 S22: 0.0957 S23: -0.1448
REMARK 3 S31: 0.1334 S32: 0.0865 S33: -0.0452
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 25
REMARK 3 ORIGIN FOR THE GROUP (A): 117.7490 84.8540 37.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.5513 T22: 0.8971
REMARK 3 T33: 0.6934 T12: 0.4608
REMARK 3 T13: -0.0002 T23: -0.1273
REMARK 3 L TENSOR
REMARK 3 L11: 7.3065 L22: 7.9984
REMARK 3 L33: 20.4155 L12: 3.4987
REMARK 3 L13: -0.5618 L23: 0.5429
REMARK 3 S TENSOR
REMARK 3 S11: -0.4309 S12: -0.4759 S13: -1.3949
REMARK 3 S21: 0.3153 S22: 0.0177 S23: -0.4621
REMARK 3 S31: 1.8949 S32: 0.8260 S33: 0.4132
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 26 B 60
REMARK 3 ORIGIN FOR THE GROUP (A): 126.5140 91.0210 34.4370
REMARK 3 T TENSOR
REMARK 3 T11: 0.3202 T22: 2.0489
REMARK 3 T33: 0.9612 T12: 0.3624
REMARK 3 T13: -0.0737 T23: -0.3760
REMARK 3 L TENSOR
REMARK 3 L11: 9.8713 L22: 3.9784
REMARK 3 L33: 7.4353 L12: -1.1401
REMARK 3 L13: -2.8208 L23: 1.5980
REMARK 3 S TENSOR
REMARK 3 S11: -0.1840 S12: -0.2316 S13: 0.5221
REMARK 3 S21: 0.1200 S22: 0.9776 S23: -1.5618
REMARK 3 S31: 0.4601 S32: 3.2698 S33: -0.7936
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 : B 61 B 108
REMARK 3 ORIGIN FOR THE GROUP (A): 103.7180 113.1850 51.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1523 T22: 0.6441
REMARK 3 T33: 0.6635 T12: -0.0577
REMARK 3 T13: 0.0373 T23: -0.1897
REMARK 3 L TENSOR
REMARK 3 L11: 5.4651 L22: 7.5702
REMARK 3 L33: 8.6167 L12: -4.2968
REMARK 3 L13: -4.0426 L23: 7.1996
REMARK 3 S TENSOR
REMARK 3 S11: 0.1963 S12: -0.1214 S13: 0.8312
REMARK 3 S21: -0.2965 S22: 0.6433 S23: -0.5552
REMARK 3 S31: -0.3503 S32: 1.0157 S33: -0.8396
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 : B 109 B 177
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3760 123.0290 66.2230
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.0487
REMARK 3 T33: 0.1443 T12: 0.0264
REMARK 3 T13: 0.0396 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 4.0013 L22: 2.7139
REMARK 3 L33: 1.4119 L12: 1.4921
REMARK 3 L13: -0.0728 L23: 0.5756
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: -0.3498 S13: 0.3114
REMARK 3 S21: 0.1224 S22: 0.0150 S23: -0.1198
REMARK 3 S31: -0.2215 S32: 0.0491 S33: -0.0517
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 178 B 354
REMARK 3 ORIGIN FOR THE GROUP (A): 68.6710 116.0720 61.9200
REMARK 3 T TENSOR
REMARK 3 T11: 0.1034 T22: 0.0220
REMARK 3 T33: 0.1216 T12: 0.0096
REMARK 3 T13: 0.0430 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.9379 L22: 2.5530
REMARK 3 L33: 1.3835 L12: 0.6905
REMARK 3 L13: 0.2629 L23: 0.7715
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.0313 S13: 0.1056
REMARK 3 S21: -0.0135 S22: 0.1094 S23: -0.1932
REMARK 3 S31: -0.1230 S32: 0.1081 S33: -0.0941
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 355 B 383
REMARK 3 ORIGIN FOR THE GROUP (A): 98.8810 101.7180 57.3860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1934 T22: 0.2895
REMARK 3 T33: 0.4470 T12: 0.0854
REMARK 3 T13: 0.0480 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 5.6166 L22: 5.9118
REMARK 3 L33: 14.1401 L12: -0.9835
REMARK 3 L13: 1.0837 L23: 3.0343
REMARK 3 S TENSOR
REMARK 3 S11: -0.2167 S12: -0.2775 S13: -0.0252
REMARK 3 S21: 0.6746 S22: 0.2820 S23: 0.1867
REMARK 3 S31: 0.8229 S32: 0.9027 S33: -0.0653
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 384 B 432
REMARK 3 ORIGIN FOR THE GROUP (A): 99.3080 104.7860 50.8060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1403 T22: 0.4096
REMARK 3 T33: 0.4504 T12: 0.0233
REMARK 3 T13: -0.0222 T23: -0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 3.7586 L22: 3.6432
REMARK 3 L33: 9.3908 L12: -2.5965
REMARK 3 L13: -3.3303 L23: 4.7398
REMARK 3 S TENSOR
REMARK 3 S11: -0.1181 S12: 0.0651 S13: -0.1498
REMARK 3 S21: 0.2147 S22: 0.1659 S23: 0.0628
REMARK 3 S31: 0.3205 S32: 0.4981 S33: -0.0478
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 433 B 466
REMARK 3 ORIGIN FOR THE GROUP (A): 115.9970 88.5430 19.2060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2302 T22: 0.7523
REMARK 3 T33: 0.5872 T12: 0.1606
REMARK 3 T13: 0.0907 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 8.9120 L22: 1.5651
REMARK 3 L33: 15.0908 L12: 0.8385
REMARK 3 L13: 0.2888 L23: -1.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.2017 S12: 0.2711 S13: 0.2249
REMARK 3 S21: -0.2492 S22: 0.4248 S23: -0.2408
REMARK 3 S31: 0.2436 S32: 1.1079 S33: -0.2231
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 : C 1 C 73
REMARK 3 ORIGIN FOR THE GROUP (A): 88.8060 95.1680 130.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: 0.3573
REMARK 3 T33: 0.1313 T12: -0.0136
REMARK 3 T13: 0.0211 T23: -0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 3.4122 L22: 1.8398
REMARK 3 L33: 3.2922 L12: 0.6674
REMARK 3 L13: -0.7807 L23: -0.5998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: -0.3999 S13: 0.1188
REMARK 3 S21: 0.1329 S22: -0.0347 S23: -0.2733
REMARK 3 S31: -0.0960 S32: 0.5939 S33: 0.0838
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 : C 74 C 274
REMARK 3 ORIGIN FOR THE GROUP (A): 91.9610 89.7630 106.6780
REMARK 3 T TENSOR
REMARK 3 T11: 0.1494 T22: 0.2888
REMARK 3 T33: 0.1192 T12: 0.0380
REMARK 3 T13: 0.1105 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.9501 L22: 1.1475
REMARK 3 L33: 1.2238 L12: 0.5561
REMARK 3 L13: 0.0046 L23: -0.0870
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: 0.1170 S13: -0.0402
REMARK 3 S21: -0.2008 S22: 0.0095 S23: -0.2401
REMARK 3 S31: 0.1749 S32: 0.5002 S33: 0.0586
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 : C 275 C 334
REMARK 3 ORIGIN FOR THE GROUP (A): 71.2280 75.8330 114.6080
REMARK 3 T TENSOR
REMARK 3 T11: 0.2253 T22: 0.0386
REMARK 3 T33: 0.1296 T12: -0.0352
REMARK 3 T13: 0.0592 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 2.9155 L22: 3.7696
REMARK 3 L33: 3.3858 L12: -1.8993
REMARK 3 L13: 0.0732 L23: -0.6202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0751 S12: 0.0883 S13: -0.5233
REMARK 3 S21: -0.1409 S22: 0.0189 S23: 0.1801
REMARK 3 S31: 0.5204 S32: -0.0389 S33: 0.0562
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 : C 335 C 453
REMARK 3 ORIGIN FOR THE GROUP (A): 75.3360 80.3710 129.4100
REMARK 3 T TENSOR
REMARK 3 T11: 0.1849 T22: 0.1582
REMARK 3 T33: 0.0865 T12: 0.0427
REMARK 3 T13: 0.0620 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 2.7348 L22: 1.8903
REMARK 3 L33: 2.4722 L12: 0.2485
REMARK 3 L13: 0.1388 L23: -0.1158
REMARK 3 S TENSOR
REMARK 3 S11: -0.0253 S12: -0.2804 S13: -0.3915
REMARK 3 S21: -0.0138 S22: 0.0276 S23: -0.0861
REMARK 3 S31: 0.4329 S32: 0.1906 S33: -0.0023
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 : D 1 D 25
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9070 68.5850 139.4080
REMARK 3 T TENSOR
REMARK 3 T11: 0.6905 T22: 0.5196
REMARK 3 T33: 0.4753 T12: -0.3349
REMARK 3 T13: 0.0918 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 7.2185 L22: 11.1172
REMARK 3 L33: 14.8679 L12: -2.1740
REMARK 3 L13: -3.3589 L23: 5.5865
REMARK 3 S TENSOR
REMARK 3 S11: -0.2106 S12: 0.0546 S13: -1.1613
REMARK 3 S21: 0.1127 S22: -0.3101 S23: -0.2709
REMARK 3 S31: 1.7333 S32: -0.2125 S33: 0.5206
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 26 D 59
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2060 71.5570 140.3510
REMARK 3 T TENSOR
REMARK 3 T11: 0.3918 T22: 0.9015
REMARK 3 T33: 0.5799 T12: -0.4741
REMARK 3 T13: 0.0732 T23: -0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 4.1918 L22: 6.1559
REMARK 3 L33: 16.0777 L12: -1.1716
REMARK 3 L13: -4.5425 L23: -1.9464
REMARK 3 S TENSOR
REMARK 3 S11: -0.4013 S12: 0.2205 S13: -0.1430
REMARK 3 S21: 0.2550 S22: 0.2696 S23: 1.0402
REMARK 3 S31: 1.1969 S32: -2.2618 S33: 0.1317
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 : D 60 D 91
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5090 95.7760 113.4460
REMARK 3 T TENSOR
REMARK 3 T11: 0.1176 T22: 0.4740
REMARK 3 T33: 0.2297 T12: 0.0219
REMARK 3 T13: 0.0360 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 2.4013 L22: 6.4555
REMARK 3 L33: 15.7556 L12: 2.1587
REMARK 3 L13: -2.9066 L23: -7.2854
REMARK 3 S TENSOR
REMARK 3 S11: 0.2520 S12: 0.2154 S13: 0.2759
REMARK 3 S21: 0.4152 S22: 0.2600 S23: 0.2600
REMARK 3 S31: -0.8639 S32: -0.8008 S33: -0.5120
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 92 D 176
REMARK 3 ORIGIN FOR THE GROUP (A): 54.3170 100.9320 98.9110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1994 T22: 0.1584
REMARK 3 T33: 0.0995 T12: -0.0262
REMARK 3 T13: 0.0350 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 1.2741 L22: 0.8109
REMARK 3 L33: 2.2242 L12: 0.1440
REMARK 3 L13: -0.2795 L23: -0.5615
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: 0.3508 S13: 0.2523
REMARK 3 S21: -0.0595 S22: 0.0647 S23: 0.0714
REMARK 3 S31: -0.0198 S32: -0.3251 S33: -0.0238
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 : D 177 D 353
REMARK 3 ORIGIN FOR THE GROUP (A): 60.7540 100.6150 101.1800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.0805
REMARK 3 T33: 0.0704 T12: -0.0232
REMARK 3 T13: 0.0470 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 2.0520 L22: 0.9116
REMARK 3 L33: 2.5049 L12: -0.3463
REMARK 3 L13: 0.7335 L23: -0.2510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0637 S12: 0.0303 S13: 0.2430
REMARK 3 S21: -0.0536 S22: 0.0527 S23: 0.0221
REMARK 3 S31: -0.1443 S32: -0.1603 S33: 0.0110
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 354 D 383
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1000 81.4900 112.5570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1935 T22: 0.2131
REMARK 3 T33: 0.2391 T12: -0.0545
REMARK 3 T13: 0.0829 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 4.1774 L22: 3.0294
REMARK 3 L33: 14.1530 L12: 0.0599
REMARK 3 L13: 0.7932 L23: -0.7923
REMARK 3 S TENSOR
REMARK 3 S11: -0.1612 S12: 0.1808 S13: -0.4332
REMARK 3 S21: -0.2711 S22: -0.0301 S23: -0.1754
REMARK 3 S31: 1.0689 S32: 0.0750 S33: 0.1913
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 : D 384 D 436
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2280 86.0160 119.2990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.2799
REMARK 3 T33: 0.1934 T12: -0.0789
REMARK 3 T13: 0.0154 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.3754 L22: 1.5444
REMARK 3 L33: 10.7579 L12: 0.3480
REMARK 3 L13: -1.5533 L23: -1.8194
REMARK 3 S TENSOR
REMARK 3 S11: -0.1497 S12: -0.0034 S13: -0.1563
REMARK 3 S21: -0.0377 S22: -0.0123 S23: -0.1307
REMARK 3 S31: 0.5029 S32: -0.3852 S33: 0.1620
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 437 D 468
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2560 79.3570 155.4240
REMARK 3 T TENSOR
REMARK 3 T11: 0.2066 T22: 0.1992
REMARK 3 T33: 0.2185 T12: -0.1422
REMARK 3 T13: 0.0818 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 13.6134 L22: 6.3151
REMARK 3 L33: 5.7472 L12: 2.1181
REMARK 3 L13: -1.0434 L23: 4.7914
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: -0.5614 S13: -0.2457
REMARK 3 S21: 0.1347 S22: -0.1648 S23: 0.2339
REMARK 3 S31: 0.4225 S32: -0.4836 S33: 0.2270
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 33
REMARK 3 ORIGIN FOR THE GROUP (A): 115.5550 83.4160 86.1720
REMARK 3 T TENSOR
REMARK 3 T11: 0.8949 T22: 0.6580
REMARK 3 T33: 0.4725 T12: -0.0916
REMARK 3 T13: 0.2336 T23: -0.1793
REMARK 3 L TENSOR
REMARK 3 L11: 7.0473 L22: 7.0426
REMARK 3 L33: 6.3586 L12: -3.9841
REMARK 3 L13: -1.7571 L23: -1.8413
REMARK 3 S TENSOR
REMARK 3 S11: -0.1489 S12: 0.5040 S13: -1.0838
REMARK 3 S21: -1.2615 S22: -0.2810 S23: -0.1046
REMARK 3 S31: 1.8576 S32: -0.0193 S33: 0.4299
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 34 E 64
REMARK 3 ORIGIN FOR THE GROUP (A): 114.5390 96.0790 85.7030
REMARK 3 T TENSOR
REMARK 3 T11: 0.4977 T22: 0.6027
REMARK 3 T33: 0.2677 T12: -0.0330
REMARK 3 T13: 0.2822 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 5.5617 L22: 6.0202
REMARK 3 L33: 3.5678 L12: -1.5463
REMARK 3 L13: 2.5836 L23: 0.6792
REMARK 3 S TENSOR
REMARK 3 S11: 0.2424 S12: 0.5647 S13: 0.3448
REMARK 3 S21: -0.8975 S22: -0.3096 S23: -0.3449
REMARK 3 S31: 0.3533 S32: 0.2415 S33: 0.0672
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 65 E 113
REMARK 3 ORIGIN FOR THE GROUP (A): 114.8370 89.8840 87.1680
REMARK 3 T TENSOR
REMARK 3 T11: 0.8965 T22: 0.5976
REMARK 3 T33: 0.4264 T12: -0.0403
REMARK 3 T13: 0.3039 T23: -0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 5.0754 L22: 2.0659
REMARK 3 L33: 5.1073 L12: -1.6493
REMARK 3 L13: -1.1414 L23: 0.2777
REMARK 3 S TENSOR
REMARK 3 S11: 0.1918 S12: 0.5580 S13: -0.2263
REMARK 3 S21: -1.1457 S22: -0.1956 S23: -0.2878
REMARK 3 S31: 0.6934 S32: 0.0586 S33: 0.0038
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 114 E 151
REMARK 3 ORIGIN FOR THE GROUP (A): 149.5190 86.4050 76.1280
REMARK 3 T TENSOR
REMARK 3 T11: 0.9088 T22: 0.6942
REMARK 3 T33: 1.1397 T12: 0.0452
REMARK 3 T13: 0.1180 T23: 0.2867
REMARK 3 L TENSOR
REMARK 3 L11: 13.1808 L22: 2.3431
REMARK 3 L33: 5.9808 L12: -0.9336
REMARK 3 L13: 1.3470 L23: 3.2778
REMARK 3 S TENSOR
REMARK 3 S11: 0.4694 S12: 1.4765 S13: -0.5733
REMARK 3 S21: 0.0201 S22: -0.1497 S23: -0.6087
REMARK 3 S31: -0.2834 S32: 0.3701 S33: -0.3196
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 152 E 170
REMARK 3 ORIGIN FOR THE GROUP (A): 147.3350 80.2460 83.8380
REMARK 3 T TENSOR
REMARK 3 T11: 1.1217 T22: 1.1826
REMARK 3 T33: 1.4926 T12: -0.1927
REMARK 3 T13: 0.3052 T23: 0.3546
REMARK 3 L TENSOR
REMARK 3 L11: 7.1384 L22: 5.9246
REMARK 3 L33: 3.3796 L12: -3.5521
REMARK 3 L13: -3.7111 L23: 3.8414
REMARK 3 S TENSOR
REMARK 3 S11: 0.4233 S12: -0.5207 S13: -0.7275
REMARK 3 S21: -0.5386 S22: -0.4339 S23: -1.1229
REMARK 3 S31: 0.0858 S32: -0.5943 S33: 0.0106
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 171 E 187
REMARK 3 ORIGIN FOR THE GROUP (A): 143.4700 89.4790 78.2920
REMARK 3 T TENSOR
REMARK 3 T11: 0.4721 T22: 0.9190
REMARK 3 T33: 1.0173 T12: -0.0207
REMARK 3 T13: 0.4009 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 8.2637 L22: 6.8748
REMARK 3 L33: 19.2779 L12: 2.7161
REMARK 3 L13: 11.7626 L23: 7.5373
REMARK 3 S TENSOR
REMARK 3 S11: -0.9976 S12: 0.5687 S13: 0.6440
REMARK 3 S21: -0.6600 S22: 0.1354 S23: -0.5555
REMARK 3 S31: -1.4391 S32: 0.4445 S33: 0.8622
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 188 E 221
REMARK 3 ORIGIN FOR THE GROUP (A): 157.5460 79.0120 79.3050
REMARK 3 T TENSOR
REMARK 3 T11: 1.2121 T22: 1.4939
REMARK 3 T33: 2.0502 T12: 0.1568
REMARK 3 T13: 0.5145 T23: 0.3286
REMARK 3 L TENSOR
REMARK 3 L11: 9.9500 L22: 10.2443
REMARK 3 L33: 1.4262 L12: 3.2571
REMARK 3 L13: 3.2935 L23: 2.4491
REMARK 3 S TENSOR
REMARK 3 S11: -0.2994 S12: 0.4432 S13: -0.2461
REMARK 3 S21: -0.9657 S22: 0.1153 S23: -1.0512
REMARK 3 S31: 0.0742 S32: 0.2364 S33: 0.1841
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 24
REMARK 3 ORIGIN FOR THE GROUP (A): 130.3090 104.7950 101.4090
REMARK 3 T TENSOR
REMARK 3 T11: 0.3135 T22: 1.0993
REMARK 3 T33: 1.3404 T12: -0.1379
REMARK 3 T13: 0.0273 T23: -0.0833
REMARK 3 L TENSOR
REMARK 3 L11: 8.8368 L22: 7.3534
REMARK 3 L33: 4.0285 L12: -2.0225
REMARK 3 L13: 4.9589 L23: -1.7291
REMARK 3 S TENSOR
REMARK 3 S11: -0.5260 S12: -0.5582 S13: 2.3774
REMARK 3 S21: 0.1594 S22: -0.4667 S23: -1.8319
REMARK 3 S31: -0.2669 S32: 0.3516 S33: 0.9927
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 25 F 79
REMARK 3 ORIGIN FOR THE GROUP (A): 122.6370 98.0100 104.4680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1326 T22: 0.6446
REMARK 3 T33: 0.5106 T12: -0.0830
REMARK 3 T13: 0.1228 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 6.3495 L22: 6.0006
REMARK 3 L33: 4.4816 L12: -1.3387
REMARK 3 L13: -0.2635 L23: -1.5372
REMARK 3 S TENSOR
REMARK 3 S11: -0.2463 S12: -0.3472 S13: 0.2154
REMARK 3 S21: 0.2289 S22: -0.2145 S23: -0.8449
REMARK 3 S31: 0.0714 S32: 0.5001 S33: 0.4608
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 80 F 105
REMARK 3 ORIGIN FOR THE GROUP (A): 125.0060 99.1510 97.2840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2000 T22: 0.5856
REMARK 3 T33: 0.5284 T12: -0.0583
REMARK 3 T13: 0.2627 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 7.3458 L22: 4.9615
REMARK 3 L33: 6.1076 L12: -2.1204
REMARK 3 L13: 3.7655 L23: -2.2088
REMARK 3 S TENSOR
REMARK 3 S11: 0.1143 S12: 0.3031 S13: 0.1959
REMARK 3 S21: -0.2770 S22: -0.3825 S23: -0.9986
REMARK 3 S31: 0.2975 S32: 0.8305 S33: 0.2681
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 106 F 156
REMARK 3 ORIGIN FOR THE GROUP (A): 153.5350 98.3150 82.2190
REMARK 3 T TENSOR
REMARK 3 T11: 0.6052 T22: 0.8077
REMARK 3 T33: 1.1422 T12: -0.0280
REMARK 3 T13: 0.2247 T23: 0.2827
REMARK 3 L TENSOR
REMARK 3 L11: 4.7729 L22: 2.8893
REMARK 3 L33: 14.1616 L12: -0.6448
REMARK 3 L13: -1.6771 L23: 2.7838
REMARK 3 S TENSOR
REMARK 3 S11: -0.0506 S12: 0.0835 S13: 0.1119
REMARK 3 S21: -0.9791 S22: 0.0554 S23: -0.1527
REMARK 3 S31: -0.4362 S32: 0.7617 S33: -0.0048
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 157 F 187
REMARK 3 ORIGIN FOR THE GROUP (A): 149.2860 95.4150 80.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.6977 T22: 1.1272
REMARK 3 T33: 1.2476 T12: 0.0048
REMARK 3 T13: 0.3617 T23: 0.3056
REMARK 3 L TENSOR
REMARK 3 L11: 5.3162 L22: 5.9235
REMARK 3 L33: 4.3775 L12: -2.8918
REMARK 3 L13: -3.2028 L23: 4.9875
REMARK 3 S TENSOR
REMARK 3 S11: -0.1091 S12: 0.2323 S13: -0.1549
REMARK 3 S21: -0.7247 S22: 0.0938 S23: -0.1504
REMARK 3 S31: -0.4169 S32: -0.0413 S33: 0.0153
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 188 F 207
REMARK 3 ORIGIN FOR THE GROUP (A): 158.3360 104.9050 81.4030
REMARK 3 T TENSOR
REMARK 3 T11: 1.0097 T22: 1.6619
REMARK 3 T33: 1.7196 T12: -0.4104
REMARK 3 T13: 0.4766 T23: 0.3526
REMARK 3 L TENSOR
REMARK 3 L11: 1.3958 L22: 6.0300
REMARK 3 L33: 0.7594 L12: 0.3513
REMARK 3 L13: -0.0553 L23: -2.1301
REMARK 3 S TENSOR
REMARK 3 S11: -0.2207 S12: -0.3857 S13: 0.5428
REMARK 3 S21: -1.0653 S22: -0.3512 S23: -1.6841
REMARK 3 S31: 0.3469 S32: 0.0642 S33: 0.5719
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 208 F 214
REMARK 3 ORIGIN FOR THE GROUP (A): 166.3040 96.9150 70.8070
REMARK 3 T TENSOR
REMARK 3 T11: 1.0456 T22: 1.4972
REMARK 3 T33: 1.0203 T12: 0.0212
REMARK 3 T13: 0.3525 T23: -0.1357
REMARK 3 L TENSOR
REMARK 3 L11: 44.1430 L22: 13.6955
REMARK 3 L33: 9.2115 L12: -21.9259
REMARK 3 L13: 17.8488 L23: -11.2243
REMARK 3 S TENSOR
REMARK 3 S11: 2.3192 S12: 0.5650 S13: -0.6625
REMARK 3 S21: -1.1311 S22: -1.1721 S23: 1.4226
REMARK 3 S31: 0.9529 S32: 1.0966 S33: -1.1471
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 29
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4420 90.4760 86.4800
REMARK 3 T TENSOR
REMARK 3 T11: 0.7230 T22: 0.4835
REMARK 3 T33: 0.2774 T12: -0.0819
REMARK 3 T13: 0.0573 T23: 0.0836
REMARK 3 L TENSOR
REMARK 3 L11: 8.4421 L22: 4.9074
REMARK 3 L33: 9.4900 L12: -2.2063
REMARK 3 L13: -4.4083 L23: 2.5934
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.6526 S13: -0.6141
REMARK 3 S21: 1.3577 S22: -0.0481 S23: 0.1229
REMARK 3 S31: 0.8025 S32: -0.4273 S33: 0.0475
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 30 H 64
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6210 101.6070 79.3020
REMARK 3 T TENSOR
REMARK 3 T11: 0.2573 T22: 0.2711
REMARK 3 T33: 0.1896 T12: -0.0389
REMARK 3 T13: 0.1251 T23: -0.0756
REMARK 3 L TENSOR
REMARK 3 L11: 3.5058 L22: 5.8414
REMARK 3 L33: 4.7140 L12: 1.2379
REMARK 3 L13: 0.4547 L23: 0.8878
REMARK 3 S TENSOR
REMARK 3 S11: 0.2772 S12: -0.3664 S13: 0.3054
REMARK 3 S21: 0.7872 S22: -0.2669 S23: 0.2445
REMARK 3 S31: 0.0234 S32: -0.2016 S33: -0.0103
REMARK 3
REMARK 3 TLS GROUP : 41
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 65 H 113
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7650 96.4560 81.0740
REMARK 3 T TENSOR
REMARK 3 T11: 0.4876 T22: 0.3933
REMARK 3 T33: 0.2620 T12: -0.0674
REMARK 3 T13: 0.1175 T23: -0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 3.4228 L22: 3.1673
REMARK 3 L33: 4.3151 L12: 0.3805
REMARK 3 L13: -1.4033 L23: -0.3649
REMARK 3 S TENSOR
REMARK 3 S11: 0.1169 S12: -0.6294 S13: 0.1044
REMARK 3 S21: 1.1309 S22: -0.1606 S23: 0.1737
REMARK 3 S31: 0.1264 S32: -0.2841 S33: 0.0437
REMARK 3
REMARK 3 TLS GROUP : 42
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 114 H 151
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5770 86.3960 94.3470
REMARK 3 T TENSOR
REMARK 3 T11: 0.5139 T22: 0.4228
REMARK 3 T33: 1.1514 T12: 0.1050
REMARK 3 T13: 0.3021 T23: 0.2278
REMARK 3 L TENSOR
REMARK 3 L11: 5.1089 L22: 2.1977
REMARK 3 L33: 7.8077 L12: 0.8922
REMARK 3 L13: -1.4439 L23: 1.5510
REMARK 3 S TENSOR
REMARK 3 S11: -0.2221 S12: -1.0240 S13: -1.6111
REMARK 3 S21: -0.0861 S22: -0.1157 S23: 0.3833
REMARK 3 S31: 0.3682 S32: 0.1569 S33: 0.3378
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 152 H 167
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5750 78.8010 91.0110
REMARK 3 T TENSOR
REMARK 3 T11: 0.8367 T22: 1.0006
REMARK 3 T33: 1.8325 T12: 0.4864
REMARK 3 T13: 0.2135 T23: -0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 12.0298 L22: 11.0024
REMARK 3 L33: 8.4779 L12: 9.0199
REMARK 3 L13: 5.2961 L23: 8.6085
REMARK 3 S TENSOR
REMARK 3 S11: -0.4634 S12: 0.4561 S13: -1.6308
REMARK 3 S21: 1.2359 S22: 0.6632 S23: -0.3802
REMARK 3 S31: 1.9723 S32: 1.5274 S33: -0.1998
REMARK 3
REMARK 3 TLS GROUP : 44
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 168 H 187
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6460 88.7930 89.4260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1258 T22: 0.2331
REMARK 3 T33: 0.6491 T12: 0.0848
REMARK 3 T13: 0.2204 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 15.9637 L22: 2.9829
REMARK 3 L33: 15.3038 L12: 6.6449
REMARK 3 L13: 7.6945 L23: 1.6799
REMARK 3 S TENSOR
REMARK 3 S11: -0.3152 S12: 0.1509 S13: -0.0891
REMARK 3 S21: -0.0965 S22: 0.0117 S23: 0.0210
REMARK 3 S31: -0.1250 S32: 0.4580 S33: 0.3034
REMARK 3
REMARK 3 TLS GROUP : 45
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 188 H 221
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9690 75.9880 94.8420
REMARK 3 T TENSOR
REMARK 3 T11: 1.5538 T22: 0.6313
REMARK 3 T33: 2.2721 T12: 0.1611
REMARK 3 T13: 0.9088 T23: 0.2280
REMARK 3 L TENSOR
REMARK 3 L11: 8.5146 L22: 4.1876
REMARK 3 L33: 11.8299 L12: 0.8562
REMARK 3 L13: 5.6161 L23: -0.0166
REMARK 3 S TENSOR
REMARK 3 S11: -0.6136 S12: -0.9507 S13: -2.2469
REMARK 3 S21: 0.5743 S22: -0.1721 S23: 0.0002
REMARK 3 S31: 2.8046 S32: -0.3033 S33: 0.7857
REMARK 3
REMARK 3 TLS GROUP : 46
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 24
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9010 98.9090 62.9830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1109 T22: 0.9721
REMARK 3 T33: 1.0959 T12: 0.0983
REMARK 3 T13: -0.0047 T23: -0.4176
REMARK 3 L TENSOR
REMARK 3 L11: 3.4143 L22: 6.3342
REMARK 3 L33: 1.1736 L12: -3.0312
REMARK 3 L13: -1.8567 L23: 0.9399
REMARK 3 S TENSOR
REMARK 3 S11: 0.1034 S12: 1.0981 S13: -0.6141
REMARK 3 S21: -0.0828 S22: -0.3566 S23: 1.6337
REMARK 3 S31: -0.0641 S32: -0.8012 S33: 0.2533
REMARK 3
REMARK 3 TLS GROUP : 47
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 25 L 79
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3230 94.1550 62.4660
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: 0.4200
REMARK 3 T33: 0.3517 T12: -0.0065
REMARK 3 T13: 0.0528 T23: -0.1279
REMARK 3 L TENSOR
REMARK 3 L11: 5.0210 L22: 4.4476
REMARK 3 L33: 3.2407 L12: 0.2183
REMARK 3 L13: -0.0224 L23: 0.6706
REMARK 3 S TENSOR
REMARK 3 S11: 0.0141 S12: 0.2329 S13: -0.2732
REMARK 3 S21: -0.0620 S22: -0.3474 S23: 0.6008
REMARK 3 S31: 0.1106 S32: -0.6833 S33: 0.3334
REMARK 3
REMARK 3 TLS GROUP : 48
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 80 L 105
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0870 97.1740 68.6610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0823 T22: 0.4548
REMARK 3 T33: 0.3829 T12: 0.0153
REMARK 3 T13: 0.1464 T23: -0.1419
REMARK 3 L TENSOR
REMARK 3 L11: 8.4661 L22: 6.3780
REMARK 3 L33: 3.6912 L12: 3.8122
REMARK 3 L13: 0.7484 L23: 2.6891
REMARK 3 S TENSOR
REMARK 3 S11: 0.0996 S12: -0.1175 S13: -0.1480
REMARK 3 S21: 0.3958 S22: -0.5178 S23: 0.8518
REMARK 3 S31: 0.2220 S32: -0.7033 S33: 0.4182
REMARK 3
REMARK 3 TLS GROUP : 49
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 106 L 128
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5480 87.8660 85.6180
REMARK 3 T TENSOR
REMARK 3 T11: 0.2215 T22: 0.4457
REMARK 3 T33: 1.3103 T12: -0.0883
REMARK 3 T13: 0.3127 T23: -0.1886
REMARK 3 L TENSOR
REMARK 3 L11: 8.9369 L22: 3.2043
REMARK 3 L33: 0.3946 L12: 0.0206
REMARK 3 L13: -1.0753 L23: 0.9142
REMARK 3 S TENSOR
REMARK 3 S11: -0.5104 S12: 0.6409 S13: -2.1763
REMARK 3 S21: 0.5073 S22: 0.1394 S23: 0.3552
REMARK 3 S31: 0.2171 S32: -0.0707 S33: 0.3710
REMARK 3
REMARK 3 TLS GROUP : 50
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 129 L 155
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3370 95.7460 83.2450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.4965
REMARK 3 T33: 0.7063 T12: -0.0077
REMARK 3 T13: 0.0893 T23: -0.0856
REMARK 3 L TENSOR
REMARK 3 L11: 4.2898 L22: 3.4806
REMARK 3 L33: 5.2664 L12: -2.1659
REMARK 3 L13: -0.9969 L23: 3.6427
REMARK 3 S TENSOR
REMARK 3 S11: -0.0923 S12: 0.5072 S13: -0.8182
REMARK 3 S21: -0.0632 S22: -0.0516 S23: 0.3048
REMARK 3 S31: -0.3547 S32: -0.2589 S33: 0.1438
REMARK 3
REMARK 3 TLS GROUP : 51
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 156 L 209
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1250 94.2290 85.2580
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.3340
REMARK 3 T33: 0.7181 T12: -0.0511
REMARK 3 T13: 0.1064 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 5.3016 L22: 3.0125
REMARK 3 L33: 10.7474 L12: -1.5180
REMARK 3 L13: -3.6114 L23: 2.7050
REMARK 3 S TENSOR
REMARK 3 S11: -0.3816 S12: 0.3285 S13: -0.9363
REMARK 3 S21: 0.1765 S22: -0.0394 S23: 0.3482
REMARK 3 S31: -0.0577 S32: -0.3191 S33: 0.4211
REMARK 3
REMARK 3 TLS GROUP : 52
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 210 L 214
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4500 91.1550 97.2780
REMARK 3 T TENSOR
REMARK 3 T11: 2.5565 T22: 1.5270
REMARK 3 T33: 0.9033 T12: 0.0446
REMARK 3 T13: 0.4700 T23: -0.3487
REMARK 3 L TENSOR
REMARK 3 L11: 76.2091 L22: 191.5262
REMARK 3 L33: 12.2154 L12: 120.0856
REMARK 3 L13: 23.8164 L23: 34.2220
REMARK 3 S TENSOR
REMARK 3 S11: 4.0626 S12: -1.7034 S13: -3.4924
REMARK 3 S21: 4.2853 S22: -3.5156 S23: -5.8307
REMARK 3 S31: 4.4528 S32: 0.4618 S33: -0.5470
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 3NID COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00695
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 169848
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.01000
REMARK 200 R SYM (I) : 0.01000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.83900
REMARK 200 R SYM FOR SHELL (I) : 0.83900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2VDR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM SULFATE,
REMARK 280 0.1 M TRIS-HCL, PH 8.9, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 129.48500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 129.48500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.24500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
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 LYS A 455
REMARK 465 ALA A 456
REMARK 465 SER A 457
REMARK 465 LEU B 467
REMARK 465 GLY B 468
REMARK 465 SER B 469
REMARK 465 GLN B 470
REMARK 465 CYS B 471
REMARK 465 VAL C 454
REMARK 465 LYS C 455
REMARK 465 ALA C 456
REMARK 465 SER C 457
REMARK 465 GLY E 135
REMARK 465 ASP E 136
REMARK 465 THR E 137
REMARK 465 THR E 138
REMARK 465 GLY E 139
REMARK 465 GLY E 220
REMARK 465 PRO E 221
REMARK 465 GLY H 135
REMARK 465 ASP H 136
REMARK 465 THR H 137
REMARK 465 GLY H 220
REMARK 465 PRO H 221
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 174 CG CD OE1 OE2
REMARK 480 LYS D 350 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 987 O HOH A 989 1.93
REMARK 500 O HOH A 988 O HOH A 989 1.96
REMARK 500 O HOH D 488 O HOH D 984 2.06
REMARK 500 O HOH A 865 O HOH B 585 2.06
REMARK 500 O HOH A 705 O HOH A 814 2.08
REMARK 500 O HOH B 496 O HOH B 572 2.09
REMARK 500 O HOH A 1048 O HOH B 608 2.09
REMARK 500 O HOH A 607 O HOH B 700 2.13
REMARK 500 O HOH A 985 O HOH A 987 2.14
REMARK 500 O HOH A 717 O HOH A 772 2.15
REMARK 500 O HOH A 987 O HOH A 988 2.15
REMARK 500 O HOH A 717 O HOH A 721 2.18
REMARK 500 O HOH B 495 O HOH B 572 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 -130.07 49.73
REMARK 500 LYS A 118 -119.41 55.74
REMARK 500 GLU A 123 137.11 95.56
REMARK 500 LEU A 212 -46.73 74.11
REMARK 500 SER A 222 -169.47 -71.51
REMARK 500 SER A 261 70.52 53.87
REMARK 500 ASP A 319 37.13 71.50
REMARK 500 PRO B 2 101.29 -55.37
REMARK 500 PRO B 32 162.26 -48.79
REMARK 500 LEU B 33 -72.96 -40.56
REMARK 500 PHE B 56 83.98 -154.06
REMARK 500 ASP B 66 55.93 -148.79
REMARK 500 ASP B 76 -174.36 61.12
REMARK 500 SER B 77 65.35 -156.55
REMARK 500 VAL B 157 -85.12 -122.71
REMARK 500 SER B 213 -160.84 -120.95
REMARK 500 ASP B 241 75.23 -107.13
REMARK 500 LEU B 258 -7.68 87.94
REMARK 500 LEU B 375 -84.34 60.03
REMARK 500 ASP B 432 79.24 -100.82
REMARK 500 SER C 101 -130.53 52.56
REMARK 500 LYS C 118 -115.47 52.79
REMARK 500 GLU C 123 138.28 92.31
REMARK 500 LEU C 212 -43.76 72.98
REMARK 500 ALA C 424 5.85 83.36
REMARK 500 ASP D 47 35.31 -95.50
REMARK 500 VAL D 157 -82.01 -127.30
REMARK 500 LYS D 181 59.59 -100.57
REMARK 500 SER D 213 -161.31 -118.05
REMARK 500 ASP D 241 68.40 -110.63
REMARK 500 LEU D 258 -12.49 88.05
REMARK 500 SER D 337 17.61 58.74
REMARK 500 CYS D 374 -92.37 -106.90
REMARK 500 ASN D 376 -112.32 53.78
REMARK 500 SER E 85 70.05 55.26
REMARK 500 LEU E 100 -74.46 -82.07
REMARK 500 TYR E 101 -61.35 -108.90
REMARK 500 THR E 122 89.23 -68.77
REMARK 500 SER E 178 70.66 50.80
REMARK 500 SER F 77 79.98 60.21
REMARK 500 SER F 127 42.49 -92.91
REMARK 500 ALA F 130 124.78 -178.52
REMARK 500 ALA F 196 117.21 -160.59
REMARK 500 LEU H 100 -70.79 -85.67
REMARK 500 ASP H 179 -15.99 71.22
REMARK 500 SER L 30 54.77 38.95
REMARK 500 SER L 77 80.36 68.14
REMARK 500 ASN L 212 -43.00 68.65
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 MG D2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 488 O
REMARK 620 2 HOH D 483 O 73.6
REMARK 620 3 HOH D 482 O 175.4 107.8
REMARK 620 4 GLU D 220 OE2 81.4 148.6 98.6
REMARK 620 5 HOH D 481 O 96.0 116.8 79.5 83.9
REMARK 620 6 SER D 121 OG 115.7 78.8 68.9 95.8 148.0
REMARK 620 N 1 2 3 4 5
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 HOH B 493 O
REMARK 620 2 HOH B 492 O 93.6
REMARK 620 3 HOH B 495 O 169.3 94.2
REMARK 620 4 GLU B 220 OE2 118.9 97.5 67.3
REMARK 620 5 SER B 121 OG 69.5 163.0 102.5 92.1
REMARK 620 6 HOH B 494 O 107.9 110.5 62.4 123.1 75.0
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 C 464 O
REMARK 620 2 ASP C 367 OD1 96.4
REMARK 620 3 TYR C 371 O 100.5 157.7
REMARK 620 4 ASP C 365 OD2 148.7 78.8 79.1
REMARK 620 5 ASP C 373 OD1 117.6 87.0 97.9 93.2
REMARK 620 6 ASP C 373 OD2 72.5 116.5 82.8 137.4 51.7
REMARK 620 7 ASP C 369 OD1 71.4 81.0 90.6 77.3 165.9 141.3
REMARK 620 N 1 2 3 4 5 6
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 THR C 250 O
REMARK 620 2 ASP C 245 OD2 165.1
REMARK 620 3 ASP C 247 O 86.5 96.4
REMARK 620 4 THR C 250 OG1 77.1 89.1 78.9
REMARK 620 5 GLU C 243 OE1 74.1 120.8 74.3 141.4
REMARK 620 6 GLU C 252 OE2 90.4 80.6 154.4 75.7 129.0
REMARK 620 7 GLU C 252 OE1 106.2 77.0 154.4 125.1 87.7 49.9
REMARK 620 8 GLU C 243 OE2 124.0 70.9 78.6 147.8 49.9 123.2 75.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 217 OD1
REMARK 620 2 GLU B 220 OE1 173.9
REMARK 620 3 ASN B 215 OD1 87.9 90.3
REMARK 620 4 PRO B 219 O 100.7 81.2 171.3
REMARK 620 5 ASP B 158 OD2 94.9 91.1 96.7 82.0
REMARK 620 6 ASP B 217 O 76.8 97.5 93.6 89.1 166.6
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 ASN C 299 OD1
REMARK 620 2 ASP C 297 OD1 86.4
REMARK 620 3 ARG C 303 O 163.1 78.3
REMARK 620 4 HOH C 466 O 87.1 156.8 104.1
REMARK 620 5 ASP C 305 OD1 111.4 134.0 84.8 68.9
REMARK 620 6 ASP C 305 OD2 85.2 91.0 102.1 110.6 51.2
REMARK 620 7 ASP C 301 OD1 83.3 76.6 86.1 80.6 144.8 163.6
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 ASN A 299 OD1
REMARK 620 2 ARG A 303 O 159.1
REMARK 620 3 ASP A 297 OD1 83.8 75.3
REMARK 620 4 HOH A 471 O 86.8 111.7 154.7
REMARK 620 5 ASP A 305 OD1 111.2 83.3 128.3 77.1
REMARK 620 6 ASP A 301 OD1 86.5 86.9 74.8 81.2 150.8
REMARK 620 7 ASP A 305 OD2 81.8 97.4 85.5 116.4 51.0 158.1
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 D 476 O
REMARK 620 2 ASP D 127 OD1 176.1
REMARK 620 3 MET D 335 O 90.5 90.1
REMARK 620 4 HOH D 475 O 84.1 99.8 77.1
REMARK 620 5 SER D 123 O 84.5 96.2 160.5 83.6
REMARK 620 6 ASP D 126 OD1 93.5 83.0 127.4 155.5 71.9
REMARK 620 7 ASP D 126 OD2 92.5 83.9 77.3 154.1 121.7 50.1
REMARK 620 N 1 2 3 4 5 6
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 THR A 250 O
REMARK 620 2 ASP A 245 OD2 159.2
REMARK 620 3 GLU A 243 OE1 75.8 124.7
REMARK 620 4 THR A 250 OG1 76.2 83.6 143.1
REMARK 620 5 ASP A 247 O 86.5 93.2 80.6 74.1
REMARK 620 6 GLU A 243 OE2 128.4 72.0 52.7 144.9 82.2
REMARK 620 7 GLU A 252 OE2 81.9 86.6 127.0 71.5 145.4 129.8
REMARK 620 8 GLU A 252 OE1 100.6 85.4 86.6 122.0 163.4 81.6 51.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 470 O
REMARK 620 2 TYR A 371 O 97.5
REMARK 620 3 ASP A 367 OD1 97.4 164.2
REMARK 620 4 ASP A 365 OD2 151.6 75.7 88.7
REMARK 620 5 ASP A 373 OD2 70.9 77.5 112.6 131.8
REMARK 620 6 ASP A 369 OD1 76.4 90.3 88.1 76.1 143.0
REMARK 620 7 ASP A 373 OD1 117.5 92.7 85.1 90.6 51.6 165.2
REMARK 620 N 1 2 3 4 5 6
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 217 OD1
REMARK 620 2 ASN D 215 OD1 93.4
REMARK 620 3 PRO D 219 O 99.4 166.3
REMARK 620 4 GLU D 220 OE1 162.9 85.9 80.4
REMARK 620 5 ASP D 158 OD2 96.7 99.5 83.9 100.3
REMARK 620 6 ASP D 217 O 75.7 91.8 86.7 87.2 166.8
REMARK 620 N 1 2 3 4 5
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 428 OD1
REMARK 620 2 ASP A 426 OD1 75.4
REMARK 620 3 TYR A 432 O 156.9 81.9
REMARK 620 4 ASN A 430 OD1 89.2 85.6 84.7
REMARK 620 5 HOH A 472 O 72.8 144.6 127.5 79.0
REMARK 620 6 ASP A 434 OD2 116.1 136.2 83.5 133.7 73.3
REMARK 620 7 ASP A 434 OD1 87.2 89.2 96.8 174.4 104.1 52.0
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 C 465 O
REMARK 620 2 ASP C 428 OD1 77.2
REMARK 620 3 TYR C 432 O 124.5 153.8
REMARK 620 4 ASN C 430 OD1 78.6 90.9 80.6
REMARK 620 5 ASP C 426 OD1 149.3 77.5 77.0 84.6
REMARK 620 6 ASP C 434 OD1 104.4 85.8 100.6 174.9 90.8
REMARK 620 7 ASP C 434 OD2 71.0 114.4 88.7 133.8 136.4 51.3
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 ASP B 127 OD1
REMARK 620 2 MET B 335 O 88.2
REMARK 620 3 HOH B 474 O 167.9 99.1
REMARK 620 4 HOH B 475 O 95.7 80.1 95.0
REMARK 620 5 SER B 123 O 96.1 167.0 78.8 87.3
REMARK 620 6 ASP B 126 OD1 77.7 120.1 90.3 158.1 72.9
REMARK 620 7 ASP B 126 OD2 92.0 74.7 80.8 153.4 117.3 48.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 459
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 462
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 463
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3323
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3324
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 458
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 459
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 461
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 462
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 463
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VDR RELATED DB: PDB
REMARK 900 RELATED ID: 3NID RELATED DB: PDB
REMARK 900 RELATED ID: 3NIF RELATED DB: PDB
REMARK 900 RELATED ID: 3NIG RELATED DB: PDB
DBREF 3NID A 1 457 UNP P08514 ITA2B_HUMAN 32 488
DBREF 3NID B 1 471 UNP P05106 ITB3_HUMAN 27 497
DBREF 3NID C 1 457 UNP P08514 ITA2B_HUMAN 32 488
DBREF 3NID D 1 471 UNP P05106 ITB3_HUMAN 27 497
DBREF 3NID E 1 221 PDB 3NID 3NID 1 221
DBREF 3NID H 1 221 PDB 3NID 3NID 1 221
DBREF 3NID F 1 214 PDB 3NID 3NID 1 214
DBREF 3NID L 1 214 PDB 3NID 3NID 1 214
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 471 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 471 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 471 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 471 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 471 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 471 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 471 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 471 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 471 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 471 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 471 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 471 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 471 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 471 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 471 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 471 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 471 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 471 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 471 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 471 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 471 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 471 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 471 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 471 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 471 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 471 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 471 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 471 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 471 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 471 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 471 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 471 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 471 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 471 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 B 471 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 B 471 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 B 471 SER GLN CYS
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 471 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 D 471 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 D 471 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 D 471 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 D 471 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 D 471 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 D 471 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 D 471 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 D 471 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 D 471 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 D 471 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 D 471 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 D 471 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 D 471 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 D 471 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 D 471 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 D 471 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 D 471 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 D 471 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 D 471 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 D 471 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 D 471 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 D 471 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 D 471 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 D 471 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 D 471 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 D 471 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 D 471 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 D 471 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 D 471 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 D 471 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 D 471 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 D 471 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 D 471 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 D 471 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 D 471 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 D 471 SER GLN CYS
SEQRES 1 E 221 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 E 221 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 E 221 PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN
SEQRES 4 E 221 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 E 221 PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN
SEQRES 6 E 221 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 E 221 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR
SEQRES 8 E 221 ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR
SEQRES 9 E 221 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL
SEQRES 10 E 221 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU
SEQRES 11 E 221 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR
SEQRES 12 E 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 E 221 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 E 221 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 E 221 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO
SEQRES 16 E 221 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 E 221 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO
SEQRES 1 F 214 ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL
SEQRES 2 F 214 SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER
SEQRES 3 F 214 GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS
SEQRES 4 F 214 PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR
SEQRES 5 F 214 ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 F 214 GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU
SEQRES 7 F 214 ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR
SEQRES 8 F 214 ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 F 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 F 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 F 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 F 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 F 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 F 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 F 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 F 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 F 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 221 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 H 221 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 H 221 PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN
SEQRES 4 H 221 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 H 221 PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN
SEQRES 6 H 221 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 H 221 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR
SEQRES 8 H 221 ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR
SEQRES 9 H 221 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL
SEQRES 10 H 221 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU
SEQRES 11 H 221 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR
SEQRES 12 H 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 H 221 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 H 221 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 H 221 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO
SEQRES 16 H 221 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 H 221 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO
SEQRES 1 L 214 ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL
SEQRES 2 L 214 SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER
SEQRES 3 L 214 GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR
SEQRES 5 L 214 ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU
SEQRES 7 L 214 ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR
SEQRES 8 L 214 ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
MODRES 3NID ASN B 371 ASN GLYCOSYLATION SITE
MODRES 3NID ASN D 371 ASN GLYCOSYLATION SITE
MODRES 3NID ASN B 99 ASN GLYCOSYLATION SITE
MODRES 3NID ASN D 99 ASN GLYCOSYLATION SITE
MODRES 3NID ASN D 320 ASN GLYCOSYLATION SITE
MODRES 3NID ASN B 320 ASN GLYCOSYLATION SITE
HET CA A2004 1
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET GOL A 458 6
HET GOL A 459 6
HET GOL A 460 6
HET GOL A 461 6
HET GOL A 462 6
HET GOL A 463 6
HET SO4 A 464 5
HET MG B2001 1
HET CA B2002 1
HET CA B2003 1
HET NAG B3099 14
HET NAG B3320 14
HET NAG B3321 14
HET MAN B3322 11
HET MAN B3323 11
HET MAN B3324 11
HET NAG B3371 14
HET NAG B3372 14
HET GOL B 472 6
HET SO4 B 473 5
HET CA C2004 1
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET GOL C 458 6
HET GOL C 459 6
HET SO4 C 460 5
HET SO4 C 461 5
HET SO4 C 462 5
HET SO4 C 463 5
HET MG D2001 1
HET CA D2002 1
HET CA D2003 1
HET NAG D3099 14
HET NAG D3320 14
HET NAG D3321 14
HET MAN D3322 11
HET NAG D3371 14
HET NAG D3372 14
HET SO4 D 472 5
HET SO4 D 473 5
HET SO4 H 222 5
HET SO4 L 215 5
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 CA 12(CA 2+)
FORMUL 13 GOL 9(C3 H8 O3)
FORMUL 19 SO4 10(O4 S 2-)
FORMUL 20 MG 2(MG 2+)
FORMUL 23 NAG 10(C8 H15 N O6)
FORMUL 24 MAN 4(C6 H12 O6)
FORMUL 48 HOH *1059(H2 O)
HELIX 1 1 LEU A 151 ASN A 158 1 8
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 TYR A 440 ALA A 442 5 3
HELIX 7 7 ASN B 3 ARG B 8 1 6
HELIX 8 8 SER B 12 ALA B 18 1 7
HELIX 9 9 LYS B 41 ASP B 47 1 7
HELIX 10 10 ALA B 50 GLU B 52 5 3
HELIX 11 11 SER B 121 SER B 123 5 3
HELIX 12 12 MET B 124 ILE B 131 1 8
HELIX 13 13 ASN B 133 ARG B 143 1 11
HELIX 14 14 PRO B 169 ASN B 175 1 7
HELIX 15 15 VAL B 200 GLN B 210 1 11
HELIX 16 16 GLY B 221 CYS B 232 1 12
HELIX 17 17 CYS B 232 GLY B 237 1 6
HELIX 18 18 LEU B 258 GLY B 264 5 7
HELIX 19 19 SER B 291 LYS B 302 1 12
HELIX 20 20 VAL B 314 ILE B 325 1 12
HELIX 21 21 ASN B 339 ARG B 352 1 14
HELIX 22 22 CYS B 435 ALA B 441 5 7
HELIX 23 23 LEU C 151 ASN C 158 1 8
HELIX 24 24 GLY C 187 LEU C 192 1 6
HELIX 25 25 VAL C 200 TYR C 207 1 8
HELIX 26 26 ASN C 227 PHE C 231 5 5
HELIX 27 27 THR C 259 LEU C 264 1 6
HELIX 28 28 TYR C 440 ALA C 442 5 3
HELIX 29 29 ASN D 3 GLY D 9 1 7
HELIX 30 30 SER D 12 SER D 20 1 9
HELIX 31 31 LYS D 41 ASP D 47 1 7
HELIX 32 32 ALA D 50 GLU D 52 5 3
HELIX 33 33 SER D 121 SER D 123 5 3
HELIX 34 34 MET D 124 ILE D 131 1 8
HELIX 35 35 ASN D 133 ARG D 143 1 11
HELIX 36 36 PRO D 169 ASN D 175 1 7
HELIX 37 37 GLN D 199 GLN D 210 1 12
HELIX 38 38 GLY D 221 CYS D 232 1 12
HELIX 39 39 CYS D 232 GLY D 237 1 6
HELIX 40 40 LEU D 258 GLY D 264 5 7
HELIX 41 41 SER D 291 ASN D 303 1 13
HELIX 42 42 VAL D 314 GLU D 323 1 10
HELIX 43 43 ASN D 339 ARG D 352 1 14
HELIX 44 44 CYS D 435 ALA D 441 5 7
HELIX 45 45 ASN E 28 THR E 32 5 5
HELIX 46 46 PRO E 62 GLN E 65 5 4
HELIX 47 47 THR E 87 THR E 91 5 5
HELIX 48 48 ASP F 79 PHE F 83 5 5
HELIX 49 49 SER F 121 SER F 127 1 7
HELIX 50 50 THR F 182 GLU F 187 1 6
HELIX 51 51 ASN H 28 THR H 32 5 5
HELIX 52 52 PRO H 62 GLN H 65 5 4
HELIX 53 53 THR H 87 THR H 91 5 5
HELIX 54 54 ASP L 79 PHE L 83 5 5
HELIX 55 55 SER L 121 GLY L 128 1 8
HELIX 56 56 LYS L 183 GLU L 187 1 5
SHEET 1 A 4 THR A 9 ALA A 12 0
SHEET 2 A 4 GLN A 444 TYR A 448 -1 O VAL A 447 N THR A 9
SHEET 3 A 4 ASP A 434 ALA A 439 -1 N LEU A 435 O TYR A 448
SHEET 4 A 4 SER A 420 VAL A 425 -1 N ARG A 422 O ILE A 436
SHEET 1 B 3 LEU A 23 LYS A 27 0
SHEET 2 B 3 VAL A 33 ALA A 39 -1 O ALA A 34 N HIS A 26
SHEET 3 B 3 GLY A 52 PRO A 57 -1 O CYS A 56 N ILE A 35
SHEET 1 C 4 THR A 76 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 LEU A 116 N THR A 83
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 ALA A 133 -1 O SER A 129 N ALA A 108
SHEET 4 D 4 ARG A 140 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 280 N VAL A 267
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 LYS A 321 N ARG A 317
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 LEU A 363
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 LEU B 40 0
SHEET 2 K 3 CYS B 23 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 ALA B 89 N ARG B 62
SHEET 3 L 6 LEU B 425 PHE B 431 1 O GLN B 428 N LEU B 90
SHEET 4 L 6 GLU B 411 PRO B 418 -1 N ILE B 416 O LEU B 425
SHEET 5 L 6 VAL B 355 ARG B 360 -1 N GLU B 358 O LYS B 417
SHEET 6 L 6 SER B 385 CYS B 386 -1 O CYS B 386 N VAL B 355
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 CYS B 374 -1 N SER B 367 O LYS B 402
SHEET 5 M 5 GLU B 378 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 PHE B 153 O LEU B 194
SHEET 3 N 6 VAL B 112 ASP B 119 1 N TYR B 116 O GLY B 152
SHEET 4 N 6 SER B 243 THR B 250 1 O SER B 243 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 THR B 329 N PHE B 308
SHEET 1 O 2 GLY B 453 GLU B 456 0
SHEET 2 O 2 VAL B 459 CYS B 462 -1 O ARG B 461 N THR B 454
SHEET 1 P 4 THR C 9 ALA C 12 0
SHEET 2 P 4 GLN C 444 TYR C 448 -1 O VAL C 447 N THR C 9
SHEET 3 P 4 ASP C 434 ALA C 439 -1 N LEU C 435 O TYR C 448
SHEET 4 P 4 SER C 420 VAL C 425 -1 N ARG C 422 O ILE C 436
SHEET 1 Q 3 LEU C 23 LYS C 27 0
SHEET 2 Q 3 VAL C 33 GLY C 38 -1 O ALA C 34 N HIS C 26
SHEET 3 Q 3 VAL C 53 PRO C 57 -1 O CYS C 56 N ILE C 35
SHEET 1 R 4 THR C 76 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 ASN C 114 N GLN C 85
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 GLN C 134 -1 O SER C 129 N ALA C 108
SHEET 4 S 4 ARG C 139 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 VAL C 182 N VAL C 174
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 LEU C 270 -1 O LEU C 270 N TYR C 253
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 LYS C 321 N ARG C 317
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 LEU C 363
SHEET 3 X 4 GLN C 388 PHE C 392 -1 O LEU C 390 N VAL C 376
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 LEU D 40 0
SHEET 2 Z 3 CYS D 23 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 GLU D 411 PRO D 418 -1 N PHE D 414 O VAL D 427
SHEET 5 AA 6 VAL D 355 ARG D 360 -1 N GLU D 358 O LYS D 417
SHEET 6 AA 6 SER D 385 CYS D 386 -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 ILE D 399 N PHE D 100
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 PHE D 153 O LEU D 194
SHEET 3 AC 6 VAL D 112 ASP D 119 1 N TYR D 116 O GLY D 152
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 THR D 311 1 O ALA D 309 N PHE D 248
SHEET 6 AC 6 THR D 329 LEU D 333 1 O THR D 329 N PHE D 308
SHEET 1 AD 2 THR D 454 GLU D 456 0
SHEET 2 AD 2 VAL D 459 ARG D 461 -1 O ARG D 461 N THR D 454
SHEET 1 AE 4 GLN E 3 GLN E 6 0
SHEET 2 AE 4 VAL E 18 SER E 25 -1 O THR E 23 N GLN E 5
SHEET 3 AE 4 THR E 78 LEU E 83 -1 O LEU E 83 N VAL E 18
SHEET 4 AE 4 ALA E 68 ASP E 73 -1 N THR E 71 O TYR E 80
SHEET 1 AF 6 GLU E 10 VAL E 12 0
SHEET 2 AF 6 THR E 113 VAL E 117 1 O SER E 114 N GLU E 10
SHEET 3 AF 6 ALA E 92 ARG E 98 -1 N TYR E 94 O THR E 113
SHEET 4 AF 6 VAL E 34 ARG E 40 -1 N VAL E 37 O TYR E 95
SHEET 5 AF 6 GLY E 44 ILE E 51 -1 O GLU E 46 N LYS E 38
SHEET 6 AF 6 THR E 58 TYR E 60 -1 O LYS E 59 N ARG E 50
SHEET 1 AG 4 GLU E 10 VAL E 12 0
SHEET 2 AG 4 THR E 113 VAL E 117 1 O SER E 114 N GLU E 10
SHEET 3 AG 4 ALA E 92 ARG E 98 -1 N TYR E 94 O THR E 113
SHEET 4 AG 4 TYR E 108 TRP E 109 -1 O TYR E 108 N ARG E 98
SHEET 1 AH 4 SER E 126 LEU E 130 0
SHEET 2 AH 4 SER E 141 TYR E 151 -1 O GLY E 145 N LEU E 130
SHEET 3 AH 4 TYR E 181 THR E 190 -1 O LEU E 183 N VAL E 148
SHEET 4 AH 4 VAL E 169 THR E 171 -1 N HIS E 170 O SER E 186
SHEET 1 AI 4 SER E 126 LEU E 130 0
SHEET 2 AI 4 SER E 141 TYR E 151 -1 O GLY E 145 N LEU E 130
SHEET 3 AI 4 TYR E 181 THR E 190 -1 O LEU E 183 N VAL E 148
SHEET 4 AI 4 VAL E 175 LEU E 176 -1 N VAL E 175 O THR E 182
SHEET 1 AJ 3 THR E 157 TRP E 160 0
SHEET 2 AJ 3 THR E 200 ALA E 204 -1 O ASN E 202 N THR E 159
SHEET 3 AJ 3 ASP E 213 LYS E 215 -1 O LYS E 214 N CYS E 201
SHEET 1 AK 4 MET F 4 SER F 7 0
SHEET 2 AK 4 VAL F 19 ALA F 25 -1 O HIS F 24 N THR F 5
SHEET 3 AK 4 ASP F 70 ILE F 75 -1 O LEU F 73 N ILE F 21
SHEET 4 AK 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74
SHEET 1 AL 6 SER F 10 VAL F 13 0
SHEET 2 AL 6 THR F 102 ILE F 106 1 O GLU F 105 N VAL F 13
SHEET 3 AL 6 ASP F 85 GLN F 90 -1 N TYR F 86 O THR F 102
SHEET 4 AL 6 ILE F 33 GLN F 38 -1 N GLY F 34 O VAL F 89
SHEET 5 AL 6 PHE F 44 TYR F 49 -1 O LEU F 47 N TRP F 35
SHEET 6 AL 6 ASN F 53 LEU F 54 -1 O ASN F 53 N TYR F 49
SHEET 1 AM 4 SER F 10 VAL F 13 0
SHEET 2 AM 4 THR F 102 ILE F 106 1 O GLU F 105 N VAL F 13
SHEET 3 AM 4 ASP F 85 GLN F 90 -1 N TYR F 86 O THR F 102
SHEET 4 AM 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90
SHEET 1 AN 4 THR F 114 PHE F 118 0
SHEET 2 AN 4 ALA F 130 PHE F 139 -1 O VAL F 133 N PHE F 118
SHEET 3 AN 4 TYR F 173 LEU F 181 -1 O MET F 175 N LEU F 136
SHEET 4 AN 4 VAL F 159 TRP F 163 -1 N SER F 162 O SER F 176
SHEET 1 AO 3 SER F 153 ARG F 155 0
SHEET 2 AO 3 ASN F 145 ILE F 150 -1 N ILE F 150 O SER F 153
SHEET 3 AO 3 TYR F 192 THR F 197 -1 O GLU F 195 N LYS F 147
SHEET 1 AP 4 GLN H 3 GLN H 6 0
SHEET 2 AP 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5
SHEET 3 AP 4 THR H 78 LEU H 83 -1 O LEU H 81 N LEU H 20
SHEET 4 AP 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80
SHEET 1 AQ 6 GLU H 10 VAL H 12 0
SHEET 2 AQ 6 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10
SHEET 3 AQ 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113
SHEET 4 AQ 6 VAL H 34 ARG H 40 -1 N HIS H 35 O VAL H 97
SHEET 5 AQ 6 GLY H 44 ILE H 51 -1 O GLU H 46 N LYS H 38
SHEET 6 AQ 6 THR H 58 TYR H 60 -1 O LYS H 59 N ARG H 50
SHEET 1 AR 4 GLU H 10 VAL H 12 0
SHEET 2 AR 4 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10
SHEET 3 AR 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113
SHEET 4 AR 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98
SHEET 1 AS 4 SER H 126 LEU H 130 0
SHEET 2 AS 4 SER H 141 TYR H 151 -1 O LYS H 149 N SER H 126
SHEET 3 AS 4 LEU H 180 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 AS 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186
SHEET 1 AT 4 SER H 126 LEU H 130 0
SHEET 2 AT 4 SER H 141 TYR H 151 -1 O LYS H 149 N SER H 126
SHEET 3 AT 4 LEU H 180 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 AT 4 VAL H 175 GLN H 177 -1 N VAL H 175 O THR H 182
SHEET 1 AU 3 THR H 157 TRP H 160 0
SHEET 2 AU 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159
SHEET 3 AU 3 THR H 210 LYS H 215 -1 O LYS H 214 N CYS H 201
SHEET 1 AV 4 MET L 4 SER L 7 0
SHEET 2 AV 4 THR L 18 ALA L 25 -1 O HIS L 24 N THR L 5
SHEET 3 AV 4 ASP L 70 SER L 76 -1 O LEU L 73 N ILE L 21
SHEET 4 AV 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 AW 6 SER L 10 VAL L 13 0
SHEET 2 AW 6 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11
SHEET 3 AW 6 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AW 6 ILE L 33 GLN L 38 -1 N GLN L 38 O ASP L 85
SHEET 5 AW 6 PHE L 44 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 AW 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49
SHEET 1 AX 4 SER L 10 VAL L 13 0
SHEET 2 AX 4 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11
SHEET 3 AX 4 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AX 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 AY 4 THR L 114 PHE L 118 0
SHEET 2 AY 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AY 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132
SHEET 4 AY 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 AZ 4 SER L 153 ARG L 155 0
SHEET 2 AZ 4 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 AZ 4 SER L 191 HIS L 198 -1 O THR L 197 N ASN L 145
SHEET 4 AZ 4 SER L 201 ASN L 210 -1 O LYS L 207 N CYS L 194
SSBOND 1 CYS A 56 CYS A 65 1555 1555 2.08
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.07
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.06
SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.04
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 2.10
SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.09
SSBOND 10 CYS B 374 CYS B 386 1555 1555 2.05
SSBOND 11 CYS B 406 CYS B 433 1555 1555 2.03
SSBOND 12 CYS B 437 CYS B 457 1555 1555 2.04
SSBOND 13 CYS B 448 CYS B 460 1555 1555 2.04
SSBOND 14 CYS C 56 CYS C 65 1555 1555 2.05
SSBOND 15 CYS C 107 CYS C 130 1555 1555 2.07
SSBOND 16 CYS C 146 CYS C 167 1555 1555 2.04
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 2.09
SSBOND 22 CYS D 232 CYS D 273 1555 1555 2.08
SSBOND 23 CYS D 374 CYS D 386 1555 1555 2.04
SSBOND 24 CYS D 406 CYS D 433 1555 1555 2.04
SSBOND 25 CYS D 437 CYS D 457 1555 1555 2.05
SSBOND 26 CYS D 448 CYS D 460 1555 1555 2.06
SSBOND 27 CYS D 462 CYS D 471 1555 1555 2.04
SSBOND 28 CYS E 22 CYS E 96 1555 1555 2.04
SSBOND 29 CYS E 134 CYS F 214 1555 1555 2.04
SSBOND 30 CYS E 146 CYS E 201 1555 1555 2.04
SSBOND 31 CYS F 23 CYS F 88 1555 1555 2.06
SSBOND 32 CYS F 134 CYS F 194 1555 1555 2.04
SSBOND 33 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 34 CYS H 134 CYS L 214 1555 1555 2.04
SSBOND 35 CYS H 146 CYS H 201 1555 1555 2.03
SSBOND 36 CYS L 23 CYS L 88 1555 1555 2.07
SSBOND 37 CYS L 134 CYS L 194 1555 1555 2.03
LINK ND2 ASN B 371 C1 NAG B3371 1555 1555 1.44
LINK ND2 ASN D 371 C1 NAG D3371 1555 1555 1.44
LINK ND2 ASN B 99 C1 NAG B3099 1555 1555 1.44
LINK ND2 ASN D 99 C1 NAG D3099 1555 1555 1.44
LINK O4 NAG B3371 C1 NAG B3372 1555 1555 1.44
LINK O4 NAG B3320 C1 NAG B3321 1555 1555 1.44
LINK ND2 ASN D 320 C1 NAG D3320 1555 1555 1.44
LINK O4 NAG D3371 C1 NAG D3372 1555 1555 1.44
LINK O4 NAG D3320 C1 NAG D3321 1555 1555 1.44
LINK ND2 ASN B 320 C1 NAG B3320 1555 1555 1.44
LINK O4 NAG B3321 C1 MAN B3322 1555 1555 1.45
LINK O6 MAN B3322 C1 MAN B3324 1555 1555 1.45
LINK O3 MAN B3322 C1 MAN B3323 1555 1555 1.45
LINK O4 NAG D3321 C1 MAN D3322 1555 1555 1.45
LINK MG MG D2001 O HOH D 488 1555 1555 1.88
LINK MG MG B2001 O HOH B 493 1555 1555 2.07
LINK CA CA C2006 O HOH C 464 1555 1555 2.11
LINK MG MG D2001 O HOH D 483 1555 1555 2.13
LINK O THR C 250 CA CA C2004 1555 1555 2.14
LINK MG MG D2001 O HOH D 482 1555 1555 2.14
LINK OD1 ASP B 217 CA CA B2003 1555 1555 2.18
LINK OD1 ASN C 299 CA CA C2005 1555 1555 2.19
LINK OD1 ASN A 299 CA CA A2005 1555 1555 2.19
LINK CA CA D2002 O HOH D 476 1555 1555 2.20
LINK OE2 GLU D 220 MG MG D2001 1555 1555 2.21
LINK MG MG B2001 O HOH B 492 1555 1555 2.22
LINK OD1 ASP C 297 CA CA C2005 1555 1555 2.22
LINK O THR A 250 CA CA A2004 1555 1555 2.22
LINK CA CA A2006 O HOH A 470 1555 1555 2.23
LINK OE1 GLU B 220 CA CA B2003 1555 1555 2.24
LINK OD2 ASP A 245 CA CA A2004 1555 1555 2.24
LINK OD1 ASP D 217 CA CA D2003 1555 1555 2.25
LINK O TYR A 371 CA CA A2006 1555 1555 2.26
LINK OD1 ASP C 367 CA CA C2006 1555 1555 2.26
LINK OD2 ASP C 245 CA CA C2004 1555 1555 2.26
LINK OD1 ASP A 428 CA CA A2007 1555 1555 2.28
LINK OD1 ASN D 215 CA CA D2003 1555 1555 2.29
LINK OD1 ASP D 127 CA CA D2002 1555 1555 2.29
LINK OD1 ASP A 426 CA CA A2007 1555 1555 2.29
LINK OD1 ASN B 215 CA CA B2003 1555 1555 2.29
LINK O ARG A 303 CA CA A2005 1555 1555 2.30
LINK O PRO D 219 CA CA D2003 1555 1555 2.30
LINK O TYR C 371 CA CA C2006 1555 1555 2.30
LINK OD1 ASP A 367 CA CA A2006 1555 1555 2.31
LINK CA CA C2007 O HOH C 465 1555 1555 2.32
LINK O TYR A 432 CA CA A2007 1555 1555 2.32
LINK O MET D 335 CA CA D2002 1555 1555 2.32
LINK OD1 ASP C 428 CA CA C2007 1555 1555 2.33
LINK O PRO B 219 CA CA B2003 1555 1555 2.34
LINK OD2 ASP A 365 CA CA A2006 1555 1555 2.34
LINK MG MG B2001 O HOH B 495 1555 1555 2.34
LINK O TYR C 432 CA CA C2007 1555 1555 2.35
LINK OD2 ASP B 158 CA CA B2003 1555 1555 2.35
LINK OD1 ASP A 297 CA CA A2005 1555 1555 2.35
LINK OE1 GLU D 220 CA CA D2003 1555 1555 2.36
LINK OD1 ASP B 127 CA CA B2002 1555 1555 2.36
LINK O MET B 335 CA CA B2002 1555 1555 2.37
LINK O ARG C 303 CA CA C2005 1555 1555 2.37
LINK CA CA B2002 O HOH B 474 1555 1555 2.38
LINK OD2 ASP D 158 CA CA D2003 1555 1555 2.38
LINK CA CA D2002 O HOH D 475 1555 1555 2.39
LINK OD1 ASN A 430 CA CA A2007 1555 1555 2.39
LINK O SER D 123 CA CA D2002 1555 1555 2.40
LINK O ASP B 217 CA CA B2003 1555 1555 2.40
LINK OE1 GLU A 243 CA CA A2004 1555 1555 2.40
LINK CA CA B2002 O HOH B 475 1555 1555 2.40
LINK MG MG D2001 O HOH D 481 1555 1555 2.40
LINK OD1 ASN C 430 CA CA C2007 1555 1555 2.41
LINK OD1 ASP C 426 CA CA C2007 1555 1555 2.41
LINK OG SER D 121 MG MG D2001 1555 1555 2.42
LINK OG1 THR A 250 CA CA A2004 1555 1555 2.43
LINK OD2 ASP C 365 CA CA C2006 1555 1555 2.43
LINK CA CA A2005 O HOH A 471 1555 1555 2.43
LINK O ASP C 247 CA CA C2004 1555 1555 2.43
LINK O SER B 123 CA CA B2002 1555 1555 2.43
LINK OE2 GLU B 220 MG MG B2001 1555 1555 2.45
LINK O ASP A 247 CA CA A2004 1555 1555 2.45
LINK O ASP D 217 CA CA D2003 1555 1555 2.45
LINK CA CA C2005 O HOH C 466 1555 1555 2.46
LINK CA CA A2007 O HOH A 472 1555 1555 2.47
LINK OD2 ASP A 434 CA CA A2007 1555 1555 2.48
LINK OG1 THR C 250 CA CA C2004 1555 1555 2.48
LINK OD2 ASP A 373 CA CA A2006 1555 1555 2.48
LINK OE1 GLU C 243 CA CA C2004 1555 1555 2.49
LINK OD1 ASP A 305 CA CA A2005 1555 1555 2.49
LINK OD1 ASP C 373 CA CA C2006 1555 1555 2.50
LINK OE2 GLU A 243 CA CA A2004 1555 1555 2.51
LINK OE2 GLU C 252 CA CA C2004 1555 1555 2.52
LINK OD1 ASP C 434 CA CA C2007 1555 1555 2.53
LINK OD1 ASP A 434 CA CA A2007 1555 1555 2.53
LINK OD1 ASP C 305 CA CA C2005 1555 1555 2.53
LINK OE2 GLU A 252 CA CA A2004 1555 1555 2.54
LINK OD1 ASP A 369 CA CA A2006 1555 1555 2.54
LINK OD2 ASP C 373 CA CA C2006 1555 1555 2.55
LINK OD1 ASP D 126 CA CA D2002 1555 1555 2.55
LINK OD2 ASP C 305 CA CA C2005 1555 1555 2.56
LINK OE1 GLU A 252 CA CA A2004 1555 1555 2.56
LINK OD1 ASP A 373 CA CA A2006 1555 1555 2.57
LINK OD2 ASP C 434 CA CA C2007 1555 1555 2.57
LINK OD1 ASP C 369 CA CA C2006 1555 1555 2.58
LINK OD1 ASP B 126 CA CA B2002 1555 1555 2.58
LINK OD1 ASP C 301 CA CA C2005 1555 1555 2.59
LINK OD2 ASP D 126 CA CA D2002 1555 1555 2.59
LINK OD1 ASP A 301 CA CA A2005 1555 1555 2.60
LINK OD2 ASP A 305 CA CA A2005 1555 1555 2.63
LINK OG SER B 121 MG MG B2001 1555 1555 2.66
LINK OE1 GLU C 252 CA CA C2004 1555 1555 2.68
LINK OE2 GLU C 243 CA CA C2004 1555 1555 2.69
LINK MG MG B2001 O HOH B 494 1555 1555 2.73
LINK OD2 ASP B 126 CA CA B2002 1555 1555 2.74
CISPEP 1 SER B 77 SER B 78 0 -1.75
CISPEP 2 SER B 84 PRO B 85 0 -6.60
CISPEP 3 SER B 162 PRO B 163 0 7.94
CISPEP 4 SER B 168 PRO B 169 0 -12.56
CISPEP 5 PRO B 464 GLY B 465 0 -9.33
CISPEP 6 SER D 77 SER D 78 0 3.69
CISPEP 7 SER D 84 PRO D 85 0 -7.23
CISPEP 8 SER D 162 PRO D 163 0 6.28
CISPEP 9 SER D 168 PRO D 169 0 -7.50
CISPEP 10 PHE E 152 PRO E 153 0 -5.50
CISPEP 11 GLU E 154 PRO E 155 0 0.96
CISPEP 12 TRP E 194 PRO E 195 0 2.37
CISPEP 13 SER F 7 PRO F 8 0 -9.46
CISPEP 14 LEU F 94 PRO F 95 0 -3.24
CISPEP 15 TYR F 140 PRO F 141 0 2.52
CISPEP 16 PHE H 152 PRO H 153 0 -4.89
CISPEP 17 GLU H 154 PRO H 155 0 -2.84
CISPEP 18 TRP H 194 PRO H 195 0 2.06
CISPEP 19 SER L 7 PRO L 8 0 -8.15
CISPEP 20 LEU L 94 PRO L 95 0 -2.81
CISPEP 21 TYR L 140 PRO L 141 0 0.56
SITE 1 AC1 5 GLU A 243 ASP A 245 ASP A 247 THR A 250
SITE 2 AC1 5 GLU A 252
SITE 1 AC2 6 ASP A 297 ASN A 299 ASP A 301 ARG A 303
SITE 2 AC2 6 ASP A 305 HOH A 471
SITE 1 AC3 6 ASP A 365 ASP A 367 ASP A 369 TYR A 371
SITE 2 AC3 6 ASP A 373 HOH A 470
SITE 1 AC4 6 ASP A 426 ASP A 428 ASN A 430 TYR A 432
SITE 2 AC4 6 ASP A 434 HOH A 472
SITE 1 AC5 5 GLN A 395 SER A 401 ARG A 402 HOH A 595
SITE 2 AC5 5 HOH A 632
SITE 1 AC6 6 PHE A 160 TYR A 190 GOL A 462 HOH A 644
SITE 2 AC6 6 HOH A 874 HOH A 875
SITE 1 AC7 5 LEU A 1 LEU A 3 GLN A 405 PRO C 403
SITE 2 AC7 5 HOH C 635
SITE 1 AC8 6 ALA A 89 ARG A 90 HIS A 112 LYS A 124
SITE 2 AC8 6 HOH A 643 HOH A 845
SITE 1 AC9 9 TYR A 190 LEU A 192 PHE A 231 GOL A 459
SITE 2 AC9 9 HOH A 487 HOH A 489 HOH A 575 HOH A 644
SITE 3 AC9 9 HOH A 874
SITE 1 BC1 5 PRO A 403 HOH A 697 LEU C 1 ASN C 2
SITE 2 BC1 5 LEU C 3
SITE 1 BC2 4 ILE A 154 TYR A 155 ASN A 158 SER A 161
SITE 1 BC3 6 SER B 121 GLU B 220 HOH B 492 HOH B 493
SITE 2 BC3 6 HOH B 494 HOH B 495
SITE 1 BC4 6 SER B 123 ASP B 126 ASP B 127 MET B 335
SITE 2 BC4 6 HOH B 474 HOH B 475
SITE 1 BC5 5 ASP B 158 ASN B 215 ASP B 217 PRO B 219
SITE 2 BC5 5 GLU B 220
SITE 1 BC6 4 LYS B 98 ASN B 99 PHE B 100 HOH B 539
SITE 1 BC7 9 MET A 285 LEU B 317 ASN B 320 HOH B 509
SITE 2 BC7 9 HOH B 547 HOH B 575 HOH B 763 HOH B 950
SITE 3 BC7 9 NAG B3321
SITE 1 BC8 7 ARG A 281 HOH B 950 HOH B 951 HOH B 952
SITE 2 BC8 7 NAG B3320 MAN B3322 MAN B3323
SITE 1 BC9 3 NAG B3321 MAN B3323 MAN B3324
SITE 1 CC1 3 ARG A 281 NAG B3321 MAN B3322
SITE 1 CC2 1 MAN B3322
SITE 1 CC3 5 SER B 369 ASN B 371 SER B 398 GLU B 400
SITE 2 CC3 5 NAG B3372
SITE 1 CC4 1 NAG B3371
SITE 1 CC5 5 SER B 300 ASN B 303 ILE B 304 PRO B 326
SITE 2 CC5 5 HOH B 783
SITE 1 CC6 6 GLN B 82 GLN B 106 SER B 243 ARG B 352
SITE 2 CC6 6 GLY B 420 PHE B 421
SITE 1 CC7 5 GLU C 243 ASP C 245 ASP C 247 THR C 250
SITE 2 CC7 5 GLU C 252
SITE 1 CC8 6 ASP C 297 ASN C 299 ASP C 301 ARG C 303
SITE 2 CC8 6 ASP C 305 HOH C 466
SITE 1 CC9 6 ASP C 365 ASP C 367 ASP C 369 TYR C 371
SITE 2 CC9 6 ASP C 373 HOH C 464
SITE 1 DC1 6 ASP C 426 ASP C 428 ASN C 430 TYR C 432
SITE 2 DC1 6 ASP C 434 HOH C 465
SITE 1 DC2 6 ARG C 90 TRP C 110 HOH C 850 HOH C 941
SITE 2 DC2 6 SER D 162 ALA D 263
SITE 1 DC3 4 PHE C 160 HOH C 489 HOH C 870 HOH C 871
SITE 1 DC4 4 PHE A 10 PHE A 411 GLN A 444 PRO C 383
SITE 1 DC5 6 ARG C 281 GLY C 282 GLU C 283 TYR C 329
SITE 2 DC5 6 PHE C 331 PRO C 343
SITE 1 DC6 2 ARG C 279 ARG C 281
SITE 1 DC7 4 ASN C 227 TYR C 230 ARG C 276 ARG C 279
SITE 1 DC8 6 SER D 121 GLU D 220 HOH D 481 HOH D 482
SITE 2 DC8 6 HOH D 483 HOH D 488
SITE 1 DC9 6 SER D 123 ASP D 126 ASP D 127 MET D 335
SITE 2 DC9 6 HOH D 475 HOH D 476
SITE 1 EC1 5 ASP D 158 ASN D 215 ASP D 217 PRO D 219
SITE 2 EC1 5 GLU D 220
SITE 1 EC2 3 ASN D 99 SER D 101 NAG D3372
SITE 1 EC3 10 MET C 285 LEU D 317 ASN D 320 HOH D 509
SITE 2 EC3 10 HOH D 517 HOH D 543 HOH D 552 HOH D 553
SITE 3 EC3 10 HOH D 554 NAG D3321
SITE 1 EC4 4 ARG C 281 HOH D 532 NAG D3320 MAN D3322
SITE 1 EC5 1 NAG D3321
SITE 1 EC6 5 SER D 369 ASN D 371 SER D 398 GLU D 400
SITE 2 EC6 5 NAG D3372
SITE 1 EC7 2 NAG D3099 NAG D3371
SITE 1 EC8 6 GLN D 82 GLN D 106 TYR D 110 SER D 243
SITE 2 EC8 6 ARG D 352 PHE D 421
SITE 1 EC9 4 GLN A 134 SER A 137 ARG D 461 CYS D 462
SITE 1 FC1 4 LYS H 38 ARG H 40 GLU H 46 PHE H 64
SITE 1 FC2 5 GLN L 37 LYS L 39 LEU L 47 PRO L 59
SITE 2 FC2 5 PHE L 62
CRYST1 258.970 144.490 104.200 90.00 90.00 90.00 P 21 21 2 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 0.003861 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006921 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END