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HEADER CELL ADHESION 07-APR-10 2XB6
TITLE REVISITED CRYSTAL STRUCTURE OF NEUREXIN1BETA-NEUROLIGIN4
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-4, X-LINKED;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CHOLINESTERASE-LIKE DOMAIN, RESIDUES 43-619;
COMPND 5 SYNONYM: NEUROLIGIN-4, NEUROLIGIN X, HNLX;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NEUREXIN-1-BETA;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: LNS DOMAIN, RESIDUES 80-258;
COMPND 11 SYNONYM: NEUREXIN I-BETA;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: RAT;
SOURCE 11 ORGANISM_TAXID: 10116;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: ROSETTA
KEYWDS ALPHA-BETA-HYDROLASE FOLD, AUTISM, CONFORMATIONAL REARRANGEMENT,
KEYWDS 2 CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.LEONE,D.COMOLETTI,G.FERRACCI,S.CONROD,S.U.GARCIA,P.TAYLOR,Y.BOURNE,
AUTHOR 2 P.MARCHOT
REVDAT 1 23-JUN-10 2XB6 0
JRNL AUTH P.LEONE,D.COMOLETTI,G.FERRACCI,S.CONROD,S.U.GARCIA,P.TAYLOR,
JRNL AUTH 2 Y.BOURNE,P.MARCHOT
JRNL TITL STRUCTURAL INSIGHTS INTO THE EXQUISITE SELECTIVITY OF
JRNL TITL 2 NEUREXIN-NEUROLIGIN SYNAPTIC INTERACTIONS
JRNL REF EMBO J. 2010
JRNL REFN ESSN 1460-2075
JRNL PMID 20543817
JRNL DOI 10.1038/EMBOJ.2010.123
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.99
REMARK 3 NUMBER OF REFLECTIONS : 68827
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3658
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4984
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 265
REMARK 3 BIN FREE R VALUE : 0.351
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 195
REMARK 3 SOLVENT ATOMS : 349
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.65
REMARK 3 B22 (A**2) : -1.76
REMARK 3 B33 (A**2) : -1.89
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.394
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.258
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.182
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.938
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11634 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7785 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15758 ; 1.526 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18926 ; 1.168 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1411 ; 6.254 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 540 ;36.224 ;24.481
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1804 ;16.316 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;21.426 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1717 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12884 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2326 ; 0.002 ; 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): 7070 ; 0.686 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2889 ; 0.096 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11409 ; 1.258 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4564 ; 2.119 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4349 ; 3.350 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 43 A 62 2
REMARK 3 1 B 43 B 62 2
REMARK 3 2 A 69 A 110 2
REMARK 3 2 B 69 B 110 2
REMARK 3 3 A 143 A 407 2
REMARK 3 3 B 143 B 407 2
REMARK 3 4 A 414 A 598 2
REMARK 3 4 B 414 B 598 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2852 ; 0.04 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3607 ; 0.08 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 3607 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 2852 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2852 ; 0.09 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3607 ; 0.09 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 3607 ; 0.09 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 82 C 101 2
REMARK 3 1 D 82 D 101 2
REMARK 3 2 C 105 C 131 2
REMARK 3 2 D 105 D 131 2
REMARK 3 3 C 137 C 258 2
REMARK 3 3 D 137 D 258 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 812 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 812 ; 0.03 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 C (A): 1026 ; 0.10 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 1026 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 812 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 812 ; 0.08 ; 0.50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 1026 ; 0.07 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 1026 ; 0.07 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 43 A 110
REMARK 3 RESIDUE RANGE : A 143 A 291
REMARK 3 RESIDUE RANGE : A 340 A 373
REMARK 3 RESIDUE RANGE : A 449 A 472
REMARK 3 RESIDUE RANGE : A 561 A 582
REMARK 3 ORIGIN FOR THE GROUP (A): -39.6510 -48.2130 -33.8390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1366 T22: 0.1308
REMARK 3 T33: 0.0513 T12: 0.0788
REMARK 3 T13: 0.0202 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 0.8677 L22: 2.1851
REMARK 3 L33: 1.0805 L12: -0.0293
REMARK 3 L13: -0.1306 L23: 0.0574
REMARK 3 S TENSOR
REMARK 3 S11: -0.1192 S12: 0.1391 S13: -0.1969
REMARK 3 S21: -0.0518 S22: 0.0834 S23: -0.0076
REMARK 3 S31: 0.2347 S32: 0.0694 S33: 0.0358
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 111 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6490 -48.2790 -13.8690
REMARK 3 T TENSOR
REMARK 3 T11: 0.4129 T22: 0.3160
REMARK 3 T33: 0.0665 T12: 0.0488
REMARK 3 T13: -0.0452 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 1.8328 L22: 8.9121
REMARK 3 L33: 2.2703 L12: -3.6763
REMARK 3 L13: -0.8490 L23: 0.3688
REMARK 3 S TENSOR
REMARK 3 S11: -0.2549 S12: -0.3116 S13: 0.0024
REMARK 3 S21: 0.7633 S22: 0.2077 S23: -0.1458
REMARK 3 S31: 0.2486 S32: 0.3539 S33: 0.0472
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 292 A 339
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5160 -49.8200 -21.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.2798 T22: 0.4205
REMARK 3 T33: 0.4133 T12: 0.1487
REMARK 3 T13: -0.2030 T23: 0.0855
REMARK 3 L TENSOR
REMARK 3 L11: 4.8499 L22: 4.2387
REMARK 3 L33: 2.6840 L12: -2.2195
REMARK 3 L13: 0.0437 L23: 1.5424
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: -0.0187 S13: -0.0044
REMARK 3 S21: 0.6717 S22: 0.0700 S23: -0.8997
REMARK 3 S31: 0.1678 S32: 0.5960 S33: -0.0309
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 374 A 448
REMARK 3 RESIDUE RANGE : A 583 A 598
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7100 -20.3850 -17.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1045 T22: 0.0861
REMARK 3 T33: 0.0828 T12: 0.0411
REMARK 3 T13: -0.0616 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.3039 L22: 3.1141
REMARK 3 L33: 3.8428 L12: -0.1031
REMARK 3 L13: -0.5910 L23: -1.0419
REMARK 3 S TENSOR
REMARK 3 S11: 0.0424 S12: -0.0156 S13: 0.0518
REMARK 3 S21: 0.2893 S22: -0.0685 S23: -0.4499
REMARK 3 S31: -0.1581 S32: 0.2895 S33: 0.0260
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 473 A 560
REMARK 3 ORIGIN FOR THE GROUP (A): -53.2040 -39.8760 -23.1820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.0729
REMARK 3 T33: 0.1379 T12: 0.0642
REMARK 3 T13: 0.0514 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.5832 L22: 2.7114
REMARK 3 L33: 1.8373 L12: 0.6813
REMARK 3 L13: -0.1308 L23: 0.6205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0657 S12: 0.0773 S13: -0.1365
REMARK 3 S21: 0.2694 S22: 0.0750 S23: 0.4495
REMARK 3 S31: 0.1682 S32: 0.0103 S33: -0.0093
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 34 B 110
REMARK 3 RESIDUE RANGE : B 143 B 291
REMARK 3 RESIDUE RANGE : B 340 B 373
REMARK 3 RESIDUE RANGE : B 449 B 472
REMARK 3 RESIDUE RANGE : B 561 B 582
REMARK 3 ORIGIN FOR THE GROUP (A): -47.1860 24.9220 -16.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0474 T22: 0.0809
REMARK 3 T33: 0.0315 T12: -0.0403
REMARK 3 T13: 0.0101 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.5307 L22: 2.4984
REMARK 3 L33: 0.8918 L12: -0.4025
REMARK 3 L13: -0.1708 L23: 0.5099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: -0.0703 S13: 0.0026
REMARK 3 S21: 0.1068 S22: 0.0125 S23: 0.1510
REMARK 3 S31: 0.0388 S32: 0.0388 S33: 0.0095
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 111 B 142
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2220 25.1390 -36.3780
REMARK 3 T TENSOR
REMARK 3 T11: 0.5743 T22: 0.2862
REMARK 3 T33: 0.1736 T12: 0.1211
REMARK 3 T13: -0.0779 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.7280 L22: 10.1590
REMARK 3 L33: 3.2198 L12: 1.9833
REMARK 3 L13: 0.8325 L23: 1.2748
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.1130 S13: -0.1108
REMARK 3 S21: -1.2939 S22: -0.1239 S23: -0.0065
REMARK 3 S31: -0.1539 S32: -0.0522 S33: 0.0620
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 292 B 339
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0900 29.7520 -27.4180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1226 T22: 0.2573
REMARK 3 T33: 0.3721 T12: -0.0760
REMARK 3 T13: 0.1745 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 3.2097 L22: 5.8176
REMARK 3 L33: 3.0583 L12: 1.5336
REMARK 3 L13: 0.3729 L23: 1.1735
REMARK 3 S TENSOR
REMARK 3 S11: 0.0866 S12: 0.1897 S13: -0.0174
REMARK 3 S21: -0.5682 S22: 0.2364 S23: -1.3049
REMARK 3 S31: -0.1139 S32: 0.4488 S33: -0.3230
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 374 B 448
REMARK 3 RESIDUE RANGE : B 583 B 598
REMARK 3 ORIGIN FOR THE GROUP (A): -34.7310 -2.3030 -32.9240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0703 T22: 0.0930
REMARK 3 T33: 0.0906 T12: 0.0136
REMARK 3 T13: 0.0495 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.1698 L22: 4.4958
REMARK 3 L33: 2.8292 L12: 0.3234
REMARK 3 L13: 0.4454 L23: 0.1277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0680 S12: 0.1737 S13: -0.0960
REMARK 3 S21: -0.2269 S22: 0.0215 S23: -0.5271
REMARK 3 S31: 0.0868 S32: 0.2318 S33: -0.0895
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 473 B 560
REMARK 3 ORIGIN FOR THE GROUP (A): -57.5500 13.7280 -28.0590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0722 T22: 0.1414
REMARK 3 T33: 0.2123 T12: -0.0314
REMARK 3 T13: -0.0695 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 1.4663 L22: 3.9117
REMARK 3 L33: 2.4171 L12: -1.2081
REMARK 3 L13: -0.7684 L23: 0.1664
REMARK 3 S TENSOR
REMARK 3 S11: 0.1444 S12: 0.1858 S13: -0.1050
REMARK 3 S21: -0.3544 S22: -0.2103 S23: 0.8329
REMARK 3 S31: -0.0628 S32: -0.2349 S33: 0.0659
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 82 C 94
REMARK 3 RESIDUE RANGE : C 226 C 258
REMARK 3 ORIGIN FOR THE GROUP (A): -48.8910 -39.7950 -73.0700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2256 T22: 0.6761
REMARK 3 T33: 0.3293 T12: -0.1249
REMARK 3 T13: -0.1702 T23: -0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 4.5024 L22: 5.2605
REMARK 3 L33: 7.3594 L12: 0.0344
REMARK 3 L13: 1.0783 L23: 1.8325
REMARK 3 S TENSOR
REMARK 3 S11: 0.1586 S12: -0.0104 S13: -0.3051
REMARK 3 S21: -0.6232 S22: -0.4322 S23: 1.2689
REMARK 3 S31: 0.5279 S32: -2.1467 S33: 0.2736
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 : C 95 C 225
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3610 -35.9570 -67.5880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1012 T22: 0.0415
REMARK 3 T33: 0.0153 T12: 0.0516
REMARK 3 T13: 0.0092 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 4.1095 L22: 2.1241
REMARK 3 L33: 5.1635 L12: -0.4755
REMARK 3 L13: 0.4291 L23: 0.9428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: -0.1965 S13: 0.1272
REMARK 3 S21: -0.2889 S22: -0.0966 S23: -0.0130
REMARK 3 S31: -0.2631 S32: -0.2852 S33: 0.1508
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 82 D 94
REMARK 3 RESIDUE RANGE : D 226 D 258
REMARK 3 ORIGIN FOR THE GROUP (A): -53.9330 14.0850 23.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.5329 T22: 0.6732
REMARK 3 T33: 0.2155 T12: 0.0447
REMARK 3 T13: 0.2287 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 5.1556 L22: 3.6317
REMARK 3 L33: 5.2497 L12: 1.1355
REMARK 3 L13: -0.0338 L23: 0.9011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0612 S12: -0.2685 S13: 0.3991
REMARK 3 S21: 0.9896 S22: -0.1412 S23: 0.8523
REMARK 3 S31: 0.1926 S32: -1.3859 S33: 0.2024
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 95 D 225
REMARK 3 ORIGIN FOR THE GROUP (A): -39.1940 13.4850 17.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.3937 T22: 0.1903
REMARK 3 T33: 0.0634 T12: 0.0453
REMARK 3 T13: -0.0309 T23: 0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 2.8800 L22: 2.5722
REMARK 3 L33: 6.3891 L12: 0.8563
REMARK 3 L13: -0.0984 L23: 0.9868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0475 S12: -0.0337 S13: -0.0385
REMARK 3 S21: 0.5652 S22: 0.0663 S23: -0.3119
REMARK 3 S31: 0.2603 S32: -0.1673 S33: -0.0188
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2XB6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9834
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72526
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.00
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.7
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.8
REMARK 200 R MERGE FOR SHELL (I) : 0.55
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WQZ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH6.3,10% PEG 20000,
REMARK 280 2MM CACL2
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 68.15350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 99.38950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.15350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 99.38950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 ASP A -12
REMARK 465 TYR A -11
REMARK 465 LYS A -10
REMARK 465 ASP A -9
REMARK 465 ASP A -8
REMARK 465 ASP A -7
REMARK 465 ASP A -6
REMARK 465 LYS A -5
REMARK 465 LEU A -4
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 PRO A 63
REMARK 465 ASN A 64
REMARK 465 GLU A 65
REMARK 465 ILE A 66
REMARK 465 ASP A 157
REMARK 465 ASP A 158
REMARK 465 ILE A 159
REMARK 465 HIS A 160
REMARK 465 ASP A 161
REMARK 465 GLN A 162
REMARK 465 ASN A 163
REMARK 465 PRO A 541
REMARK 465 GLN A 542
REMARK 465 ASP A 543
REMARK 465 THR A 544
REMARK 465 LYS A 545
REMARK 465 PHE A 546
REMARK 465 ILE A 547
REMARK 465 HIS A 548
REMARK 465 THR A 549
REMARK 465 LYS A 550
REMARK 465 PRO A 551
REMARK 465 ASN A 552
REMARK 465 ARG A 553
REMARK 465 PHE A 554
REMARK 465 GLU A 555
REMARK 465 GLU A 556
REMARK 465 ASN A 599
REMARK 465 LEU A 600
REMARK 465 ASN A 601
REMARK 465 GLU A 602
REMARK 465 ILE A 603
REMARK 465 PHE A 604
REMARK 465 GLN A 605
REMARK 465 TYR A 606
REMARK 465 VAL A 607
REMARK 465 SER A 608
REMARK 465 THR A 609
REMARK 465 THR A 610
REMARK 465 THR A 611
REMARK 465 LYS A 612
REMARK 465 VAL A 613
REMARK 465 PRO A 614
REMARK 465 PRO A 615
REMARK 465 PRO A 616
REMARK 465 ASP A 617
REMARK 465 MET A 618
REMARK 465 THR A 619
REMARK 465 ASP B -12
REMARK 465 TYR B -11
REMARK 465 ASP B 157
REMARK 465 ASP B 158
REMARK 465 ILE B 159
REMARK 465 HIS B 160
REMARK 465 ASP B 161
REMARK 465 GLN B 162
REMARK 465 ASN B 163
REMARK 465 SER B 164
REMARK 465 PRO B 541
REMARK 465 GLN B 542
REMARK 465 ASP B 543
REMARK 465 THR B 544
REMARK 465 LYS B 545
REMARK 465 PHE B 546
REMARK 465 ILE B 547
REMARK 465 HIS B 548
REMARK 465 THR B 549
REMARK 465 LYS B 550
REMARK 465 PRO B 551
REMARK 465 ASN B 552
REMARK 465 ARG B 553
REMARK 465 PHE B 554
REMARK 465 GLU B 555
REMARK 465 GLU B 556
REMARK 465 ASN B 599
REMARK 465 LEU B 600
REMARK 465 ASN B 601
REMARK 465 GLU B 602
REMARK 465 ILE B 603
REMARK 465 PHE B 604
REMARK 465 GLN B 605
REMARK 465 TYR B 606
REMARK 465 VAL B 607
REMARK 465 SER B 608
REMARK 465 THR B 609
REMARK 465 THR B 610
REMARK 465 THR B 611
REMARK 465 LYS B 612
REMARK 465 VAL B 613
REMARK 465 PRO B 614
REMARK 465 PRO B 615
REMARK 465 PRO B 616
REMARK 465 ASP B 617
REMARK 465 MET B 618
REMARK 465 THR B 619
REMARK 465 GLY C 80
REMARK 465 GLY C 81
REMARK 465 GLY D 80
REMARK 465 GLY D 81
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 OE2 GLU B 411 OD1 ASP B 414 1.86
REMARK 500 O6 NAG A 700 O HOH A 2124 1.94
REMARK 500 ND2 ASN B 102 O5 NAG B 700 2.04
REMARK 500 O LEU D 135 O HOH D 2005 2.13
REMARK 500 O LEU B 593 O HIS B 596 2.14
REMARK 500 ND2 ASN A 102 C2 NAG A 700 2.15
REMARK 500 O LEU A 593 O HIS A 596 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A -1 C GLN A 44 N 0.155
REMARK 500 VAL A 238 CB VAL A 238 CG1 -0.171
REMARK 500 VAL A 238 CB VAL A 238 CG2 -0.162
REMARK 500 VAL B 238 CB VAL B 238 CG1 -0.195
REMARK 500 VAL B 238 CB VAL B 238 CG2 -0.195
REMARK 500 ARG C 197 CZ ARG C 197 NH1 -0.214
REMARK 500 ARG D 197 CZ ARG D 197 NH1 -0.207
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 231 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 MET A 501 CB - CG - SD ANGL. DEV. = 30.2 DEGREES
REMARK 500 LEU B 440 CB - CG - CD1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 MET B 501 CB - CG - SD ANGL. DEV. = 31.8 DEGREES
REMARK 500 ARG C 197 NE - CZ - NH1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG C 197 NE - CZ - NH2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG D 197 NE - CZ - NH1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG D 197 NE - CZ - NH2 ANGL. DEV. = 13.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 103 67.45 -119.92
REMARK 500 GLU A 116 120.80 -38.50
REMARK 500 ARG A 117 -24.53 103.42
REMARK 500 CYS A 146 16.45 -143.72
REMARK 500 LYS A 165 114.16 -164.58
REMARK 500 SER A 176 10.74 -140.16
REMARK 500 TYR A 177 -14.55 74.90
REMARK 500 CYS A 306 69.41 -100.87
REMARK 500 GLU A 411 -163.15 -124.69
REMARK 500 ASP A 429 50.14 -164.51
REMARK 500 SER A 487 120.24 -35.61
REMARK 500 LEU A 597 29.96 90.59
REMARK 500 ASP B -9 -42.77 173.99
REMARK 500 ASP B -8 -24.90 -22.61
REMARK 500 ASP B -7 -49.26 94.39
REMARK 500 GLU B 116 -40.84 102.83
REMARK 500 CYS B 146 13.35 -144.22
REMARK 500 TYR B 177 -15.44 74.34
REMARK 500 CYS B 306 69.10 -102.31
REMARK 500 ASP B 347 -60.17 -124.50
REMARK 500 TYR B 407 44.01 -141.13
REMARK 500 GLU B 411 -156.70 -159.89
REMARK 500 ASP B 429 52.98 -162.97
REMARK 500 TRP B 449 -50.78 -121.59
REMARK 500 HIS B 475 153.89 179.85
REMARK 500 SER B 487 121.37 -38.61
REMARK 500 LEU B 597 30.15 95.27
REMARK 500 ASP C 104 34.60 -152.27
REMARK 500 THR C 156 -85.82 -97.82
REMARK 500 ASP C 190 -123.14 51.92
REMARK 500 SER D 132 164.03 -47.72
REMARK 500 THR D 156 -88.17 -93.13
REMARK 500 ASN D 165 -39.74 -131.05
REMARK 500 ASN D 169 57.44 -97.27
REMARK 500 ASP D 190 -120.19 50.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1296 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE C 236 O
REMARK 620 2 ASP C 137 OD2 88.4
REMARK 620 3 ASN C 238 OD1 81.3 80.5
REMARK 620 4 HOH C2012 O 171.6 83.2 97.7
REMARK 620 5 VAL C 154 O 90.0 92.9 169.2 89.8
REMARK 620 6 HOH A2060 O 96.7 167.3 88.8 91.6 98.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D1289 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 238 OD1
REMARK 620 2 ASP D 137 OD2 83.5
REMARK 620 3 HOH B2096 O 92.5 174.0
REMARK 620 4 VAL D 154 O 170.1 91.4 93.2
REMARK 620 5 ILE D 236 O 81.4 86.5 97.4 89.9
REMARK 620 6 HOH D2006 O 101.2 82.6 93.8 86.5 168.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1599
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1599
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1610
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1612
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1613
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1614
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1290
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1291
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1292
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1293
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1295
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C1296
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D1289
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C4R RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE LIGAND-BINDING DOMAIN
REMARK 900 OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN
REMARK 900 FUNCTION BY ALTERNATIVE SPLICING
REMARK 900 RELATED ID: 2VH8 RELATED DB: PDB
REMARK 900 STRUCTURAL ANALYSIS OF THE SYNAPTIC PROTEIN
REMARK 900 NEUROLIGIN AND ITS BETA-NEUREXIN COMPLEX:
REMARK 900 DETERMINANTS FOR FOLDING AND CELL ADHESION
REMARK 900 RELATED ID: 2WQZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN
REMARK 900 NEUROLIGIN-4 IN COMPLEX WITH NEUREXIN-BETA
REMARK 900 1: ALTERNATIVE REFINEMENT
REMARK 999
REMARK 999 R561K IS A SPONTANEOUS MUTAGENESIS OF CDNA CLONE
DBREF 2XB6 A 44 619 UNP Q8N0W4 NLGNX_HUMAN 44 619
DBREF 2XB6 B 44 619 UNP Q8N0W4 NLGNX_HUMAN 44 619
DBREF 2XB6 C 80 288 UNP Q63373 NRX1B_RAT 80 258
DBREF 2XB6 D 80 288 UNP Q63373 NRX1B_RAT 80 258
SEQADV 2XB6 ASP A -12 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 TYR A -11 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 LYS A -10 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP A -9 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP A -8 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP A -7 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP A -6 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 LYS A -5 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 LEU A -4 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ALA A -3 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ALA A -2 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ALA A -1 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP B -12 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 TYR B -11 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 LYS B -10 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP B -9 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP B -8 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP B -7 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ASP B -6 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 LYS B -5 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 LEU B -4 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ALA B -3 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ALA B -2 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ALA B -1 UNP Q8N0W4 EXPRESSION TAG
SEQADV 2XB6 ARG A 561 UNP Q8N0W4 LYS 561 CLONING ARTIFACT
SEQADV 2XB6 ARG B 561 UNP Q8N0W4 LYS 561 CLONING ARTIFACT
SEQRES 1 A 588 ASP TYR LYS ASP ASP ASP ASP LYS LEU ALA ALA ALA GLN
SEQRES 2 A 588 TYR PRO VAL VAL ASN THR ASN TYR GLY LYS ILE ARG GLY
SEQRES 3 A 588 LEU ARG THR PRO LEU PRO ASN GLU ILE LEU GLY PRO VAL
SEQRES 4 A 588 GLU GLN TYR LEU GLY VAL PRO TYR ALA SER PRO PRO THR
SEQRES 5 A 588 GLY GLU ARG ARG PHE GLN PRO PRO GLU PRO PRO SER SER
SEQRES 6 A 588 TRP THR GLY ILE ARG ASN THR THR GLN PHE ALA ALA VAL
SEQRES 7 A 588 CYS PRO GLN HIS LEU ASP GLU ARG SER LEU LEU HIS ASP
SEQRES 8 A 588 MET LEU PRO ILE TRP PHE THR ALA ASN LEU ASP THR LEU
SEQRES 9 A 588 MET THR TYR VAL GLN ASP GLN ASN GLU ASP CYS LEU TYR
SEQRES 10 A 588 LEU ASN ILE TYR VAL PRO THR GLU ASP ASP ILE HIS ASP
SEQRES 11 A 588 GLN ASN SER LYS LYS PRO VAL MET VAL TYR ILE HIS GLY
SEQRES 12 A 588 GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY
SEQRES 13 A 588 SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR
SEQRES 14 A 588 ILE ASN TYR ARG LEU GLY ILE LEU GLY PHE LEU SER THR
SEQRES 15 A 588 GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP
SEQRES 16 A 588 GLN ILE GLN ALA LEU ARG TRP ILE GLU GLU ASN VAL GLY
SEQRES 17 A 588 ALA PHE GLY GLY ASP PRO LYS ARG VAL THR ILE PHE GLY
SEQRES 18 A 588 SER GLY ALA GLY ALA SER CYS VAL SER LEU LEU THR LEU
SEQRES 19 A 588 SER HIS TYR SER GLU GLY LEU PHE GLN LYS ALA ILE ILE
SEQRES 20 A 588 GLN SER GLY THR ALA LEU SER SER TRP ALA VAL ASN TYR
SEQRES 21 A 588 GLN PRO ALA LYS TYR THR ARG ILE LEU ALA ASP LYS VAL
SEQRES 22 A 588 GLY CYS ASN MET LEU ASP THR THR ASP MET VAL GLU CYS
SEQRES 23 A 588 LEU ARG ASN LYS ASN TYR LYS GLU LEU ILE GLN GLN THR
SEQRES 24 A 588 ILE THR PRO ALA THR TYR HIS ILE ALA PHE GLY PRO VAL
SEQRES 25 A 588 ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU
SEQRES 26 A 588 MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU
SEQRES 27 A 588 GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL ASP GLY
SEQRES 28 A 588 ILE VAL ASP ASN GLU ASP GLY VAL THR PRO ASN ASP PHE
SEQRES 29 A 588 ASP PHE SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY
SEQRES 30 A 588 TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS
SEQRES 31 A 588 PHE MET TYR THR ASP TRP ALA ASP LYS GLU ASN PRO GLU
SEQRES 32 A 588 THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS
SEQRES 33 A 588 GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU HIS
SEQRES 34 A 588 ALA GLN TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR
SEQRES 35 A 588 HIS HIS CYS GLN SER GLU MET LYS PRO SER TRP ALA ASP
SEQRES 36 A 588 SER ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY ILE
SEQRES 37 A 588 PRO MET ILE GLY PRO THR GLU LEU PHE SER CYS ASN PHE
SEQRES 38 A 588 SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR
SEQRES 39 A 588 TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN GLN
SEQRES 40 A 588 PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS PRO
SEQRES 41 A 588 ASN ARG PHE GLU GLU VAL ALA TRP SER ARG TYR ASN PRO
SEQRES 42 A 588 LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG
SEQRES 43 A 588 VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP
SEQRES 44 A 588 LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN GLU ILE
SEQRES 45 A 588 PHE GLN TYR VAL SER THR THR THR LYS VAL PRO PRO PRO
SEQRES 46 A 588 ASP MET THR
SEQRES 1 B 588 ASP TYR LYS ASP ASP ASP ASP LYS LEU ALA ALA ALA GLN
SEQRES 2 B 588 TYR PRO VAL VAL ASN THR ASN TYR GLY LYS ILE ARG GLY
SEQRES 3 B 588 LEU ARG THR PRO LEU PRO ASN GLU ILE LEU GLY PRO VAL
SEQRES 4 B 588 GLU GLN TYR LEU GLY VAL PRO TYR ALA SER PRO PRO THR
SEQRES 5 B 588 GLY GLU ARG ARG PHE GLN PRO PRO GLU PRO PRO SER SER
SEQRES 6 B 588 TRP THR GLY ILE ARG ASN THR THR GLN PHE ALA ALA VAL
SEQRES 7 B 588 CYS PRO GLN HIS LEU ASP GLU ARG SER LEU LEU HIS ASP
SEQRES 8 B 588 MET LEU PRO ILE TRP PHE THR ALA ASN LEU ASP THR LEU
SEQRES 9 B 588 MET THR TYR VAL GLN ASP GLN ASN GLU ASP CYS LEU TYR
SEQRES 10 B 588 LEU ASN ILE TYR VAL PRO THR GLU ASP ASP ILE HIS ASP
SEQRES 11 B 588 GLN ASN SER LYS LYS PRO VAL MET VAL TYR ILE HIS GLY
SEQRES 12 B 588 GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY
SEQRES 13 B 588 SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR
SEQRES 14 B 588 ILE ASN TYR ARG LEU GLY ILE LEU GLY PHE LEU SER THR
SEQRES 15 B 588 GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP
SEQRES 16 B 588 GLN ILE GLN ALA LEU ARG TRP ILE GLU GLU ASN VAL GLY
SEQRES 17 B 588 ALA PHE GLY GLY ASP PRO LYS ARG VAL THR ILE PHE GLY
SEQRES 18 B 588 SER GLY ALA GLY ALA SER CYS VAL SER LEU LEU THR LEU
SEQRES 19 B 588 SER HIS TYR SER GLU GLY LEU PHE GLN LYS ALA ILE ILE
SEQRES 20 B 588 GLN SER GLY THR ALA LEU SER SER TRP ALA VAL ASN TYR
SEQRES 21 B 588 GLN PRO ALA LYS TYR THR ARG ILE LEU ALA ASP LYS VAL
SEQRES 22 B 588 GLY CYS ASN MET LEU ASP THR THR ASP MET VAL GLU CYS
SEQRES 23 B 588 LEU ARG ASN LYS ASN TYR LYS GLU LEU ILE GLN GLN THR
SEQRES 24 B 588 ILE THR PRO ALA THR TYR HIS ILE ALA PHE GLY PRO VAL
SEQRES 25 B 588 ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU
SEQRES 26 B 588 MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU
SEQRES 27 B 588 GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL ASP GLY
SEQRES 28 B 588 ILE VAL ASP ASN GLU ASP GLY VAL THR PRO ASN ASP PHE
SEQRES 29 B 588 ASP PHE SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY
SEQRES 30 B 588 TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS
SEQRES 31 B 588 PHE MET TYR THR ASP TRP ALA ASP LYS GLU ASN PRO GLU
SEQRES 32 B 588 THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS
SEQRES 33 B 588 GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU HIS
SEQRES 34 B 588 ALA GLN TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR
SEQRES 35 B 588 HIS HIS CYS GLN SER GLU MET LYS PRO SER TRP ALA ASP
SEQRES 36 B 588 SER ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY ILE
SEQRES 37 B 588 PRO MET ILE GLY PRO THR GLU LEU PHE SER CYS ASN PHE
SEQRES 38 B 588 SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR
SEQRES 39 B 588 TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN GLN
SEQRES 40 B 588 PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS PRO
SEQRES 41 B 588 ASN ARG PHE GLU GLU VAL ALA TRP SER ARG TYR ASN PRO
SEQRES 42 B 588 LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG
SEQRES 43 B 588 VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP
SEQRES 44 B 588 LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN GLU ILE
SEQRES 45 B 588 PHE GLN TYR VAL SER THR THR THR LYS VAL PRO PRO PRO
SEQRES 46 B 588 ASP MET THR
SEQRES 1 C 179 GLY GLY HIS ALA GLY THR THR TYR ILE PHE SER LYS GLY
SEQRES 2 C 179 GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN ASP ARG
SEQRES 3 C 179 PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY PHE SER
SEQRES 4 C 179 THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL ASP SER
SEQRES 5 C 179 SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS ILE HIS
SEQRES 6 C 179 GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY THR ASP
SEQRES 7 C 179 ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE ASN ASP
SEQRES 8 C 179 GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER GLY GLY
SEQRES 9 C 179 ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL ILE GLU
SEQRES 10 C 179 ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE ASN SER
SEQRES 11 C 179 GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN GLY GLN
SEQRES 12 C 179 PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR ASN GLY
SEQRES 13 C 179 LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP ALA ASN
SEQRES 14 C 179 ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL
SEQRES 1 D 179 GLY GLY HIS ALA GLY THR THR TYR ILE PHE SER LYS GLY
SEQRES 2 D 179 GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN ASP ARG
SEQRES 3 D 179 PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY PHE SER
SEQRES 4 D 179 THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL ASP SER
SEQRES 5 D 179 SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS ILE HIS
SEQRES 6 D 179 GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY THR ASP
SEQRES 7 D 179 ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE ASN ASP
SEQRES 8 D 179 GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER GLY GLY
SEQRES 9 D 179 ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL ILE GLU
SEQRES 10 D 179 ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE ASN SER
SEQRES 11 D 179 GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN GLY GLN
SEQRES 12 D 179 PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR ASN GLY
SEQRES 13 D 179 LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP ALA ASN
SEQRES 14 D 179 ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL
HET NAG A 700 14
HET NAG A 701 14
HET EDO A1599 4
HET EDO A1600 4
HET EDO A1601 4
HET EDO A1602 4
HET EDO A1603 4
HET EDO A1604 4
HET EDO A1605 4
HET EDO A1606 4
HET EDO A1607 4
HET EDO A1608 4
HET CL A1609 1
HET CL A1610 1
HET NAG B 700 14
HET NAG B 701 14
HET EDO B1599 4
HET EDO B1600 4
HET EDO B1601 4
HET EDO B1602 4
HET EDO B1603 4
HET EDO B1604 4
HET EDO B1605 4
HET EDO B1606 4
HET EDO B1607 4
HET EDO B1608 4
HET EDO B1609 4
HET EDO B1610 4
HET EDO B1611 4
HET EDO B1612 4
HET CL B1613 1
HET CL B1614 1
HET CL B1615 1
HET MES C1289 12
HET EDO C1290 4
HET EDO C1291 4
HET EDO C1292 4
HET EDO C1293 4
HET EDO C1294 4
HET EDO C1295 4
HET CA C1296 1
HET CA D1289 1
HETNAM CL CHLORIDE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CA CALCIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN NAG NAG
FORMUL 5 CL 5(CL 1-)
FORMUL 8 NAG 4(C8 H15 N O6)
FORMUL 14 CA 2(CA 2+)
FORMUL 16 MES C6 H13 N O4 S
FORMUL 17 EDO 30(C2 H6 O2)
FORMUL 47 HOH *349(H2 O)
HELIX 1 1 THR A 83 ARG A 87 5 5
HELIX 2 2 LEU A 120 LEU A 124 5 5
HELIX 3 3 PRO A 125 ASN A 131 1 7
HELIX 4 4 ASN A 131 GLN A 140 1 10
HELIX 5 5 THR A 181 ILE A 185 5 5
HELIX 6 6 GLY A 187 ASN A 195 1 9
HELIX 7 7 LEU A 205 LEU A 211 1 7
HELIX 8 8 ASN A 221 VAL A 238 1 18
HELIX 9 9 GLY A 239 PHE A 241 5 3
HELIX 10 10 GLY A 254 THR A 264 1 11
HELIX 11 11 LEU A 265 GLU A 270 5 6
HELIX 12 12 GLN A 292 GLY A 305 1 14
HELIX 13 13 ASP A 310 LYS A 321 1 12
HELIX 14 14 ASN A 322 GLN A 328 1 7
HELIX 15 15 ASP A 352 GLN A 359 1 8
HELIX 16 16 GLY A 376 ASP A 381 5 6
HELIX 17 17 THR A 391 TYR A 407 1 17
HELIX 18 18 GLY A 412 TYR A 424 1 13
HELIX 19 19 ASN A 432 TRP A 449 1 18
HELIX 20 20 TRP A 449 TYR A 463 1 15
HELIX 21 21 GLU A 492 PHE A 497 1 6
HELIX 22 22 GLY A 498 ILE A 502 5 5
HELIX 23 23 SER A 513 GLY A 534 1 22
HELIX 24 24 ARG A 583 GLU A 592 1 10
HELIX 25 25 ASP B -6 TYR B 45 1 8
HELIX 26 26 THR B 83 ARG B 87 5 5
HELIX 27 27 LEU B 120 LEU B 124 5 5
HELIX 28 28 PRO B 125 ALA B 130 1 6
HELIX 29 29 ASN B 131 MET B 136 1 6
HELIX 30 30 THR B 181 ILE B 185 5 5
HELIX 31 31 GLY B 187 ASN B 195 1 9
HELIX 32 32 LEU B 205 LEU B 211 1 7
HELIX 33 33 ASN B 221 VAL B 238 1 18
HELIX 34 34 GLY B 239 PHE B 241 5 3
HELIX 35 35 GLY B 254 THR B 264 1 11
HELIX 36 36 LEU B 265 GLU B 270 5 6
HELIX 37 37 GLN B 292 GLY B 305 1 14
HELIX 38 38 ASP B 310 LYS B 321 1 12
HELIX 39 39 ASN B 322 GLN B 328 1 7
HELIX 40 40 ASP B 352 GLN B 359 1 8
HELIX 41 41 GLY B 376 ASP B 381 5 6
HELIX 42 42 THR B 391 TYR B 407 1 17
HELIX 43 43 GLY B 412 TYR B 424 1 13
HELIX 44 44 ASN B 432 TRP B 449 1 18
HELIX 45 45 TRP B 449 TYR B 463 1 15
HELIX 46 46 GLU B 492 PHE B 497 1 6
HELIX 47 47 GLY B 498 ILE B 502 5 5
HELIX 48 48 SER B 513 GLY B 534 1 22
HELIX 49 49 ARG B 583 GLU B 592 1 10
HELIX 50 50 PRO C 101 ARG C 105 5 5
HELIX 51 51 LYS C 267 GLU C 274 1 8
HELIX 52 52 LYS D 267 GLU D 274 1 8
SHEET 1 AA 3 VAL A 47 THR A 50 0
SHEET 2 AA 3 GLY A 53 ARG A 56 -1 O GLY A 53 N THR A 50
SHEET 3 AA 3 ILE A 100 ASN A 102 1 O ARG A 101 N ARG A 56
SHEET 1 AB11 LEU A 58 THR A 60 0
SHEET 2 AB11 VAL A 70 PRO A 77 -1 O VAL A 70 N THR A 60
SHEET 3 AB11 TYR A 148 PRO A 154 -1 O LEU A 149 N VAL A 76
SHEET 4 AB11 ILE A 197 ILE A 201 -1 O VAL A 198 N TYR A 152
SHEET 5 AB11 LYS A 166 ILE A 172 1 O PRO A 167 N ILE A 197
SHEET 6 AB11 GLY A 243 SER A 253 1 N ASP A 244 O LYS A 166
SHEET 7 AB11 LYS A 275 GLN A 279 1 O LYS A 275 N ILE A 250
SHEET 8 AB11 ASP A 366 ASN A 372 1 O ASP A 366 N ALA A 276
SHEET 9 AB11 THR A 467 PHE A 472 1 O TYR A 468 N LEU A 369
SHEET 10 AB11 LEU A 568 ILE A 572 1 O LEU A 570 N ALA A 471
SHEET 11 AB11 ARG A 577 ASP A 580 -1 O ARG A 577 N HIS A 571
SHEET 1 BA 3 VAL B 47 THR B 50 0
SHEET 2 BA 3 GLY B 53 ARG B 56 -1 O GLY B 53 N THR B 50
SHEET 3 BA 3 ILE B 100 ASN B 102 1 O ARG B 101 N ARG B 56
SHEET 1 BB11 LEU B 58 THR B 60 0
SHEET 2 BB11 VAL B 70 PRO B 77 -1 O VAL B 70 N THR B 60
SHEET 3 BB11 TYR B 148 PRO B 154 -1 O LEU B 149 N VAL B 76
SHEET 4 BB11 ILE B 197 ILE B 201 -1 O VAL B 198 N TYR B 152
SHEET 5 BB11 LYS B 166 ILE B 172 1 O PRO B 167 N ILE B 197
SHEET 6 BB11 GLY B 243 SER B 253 1 N ASP B 244 O LYS B 166
SHEET 7 BB11 LYS B 275 GLN B 279 1 O LYS B 275 N ILE B 250
SHEET 8 BB11 ASP B 366 ASN B 372 1 O ASP B 366 N ALA B 276
SHEET 9 BB11 THR B 467 PHE B 472 1 O TYR B 468 N LEU B 369
SHEET 10 BB11 LEU B 568 ILE B 572 1 O LEU B 570 N ALA B 471
SHEET 11 BB11 ARG B 577 ASP B 580 -1 O ARG B 577 N HIS B 571
SHEET 1 BC 2 GLN B 477 SER B 478 0
SHEET 2 BC 2 CYS B 510 ASN B 511 -1 O ASN B 511 N GLN B 477
SHEET 1 CA 7 ILE C 159 GLU C 162 0
SHEET 2 CA 7 LYS C 147 ASN C 153 -1 O VAL C 150 N ILE C 161
SHEET 3 CA 7 TYR C 138 HIS C 144 1 O TYR C 138 N ASN C 153
SHEET 4 CA 7 GLU C 123 SER C 131 1 O ALA C 124 N ILE C 143
SHEET 5 CA 7 GLN C 240 ILE C 245 1 N ALA C 241 O ASP C 130
SHEET 6 CA 7 THR C 86 LYS C 99 -1 O ILE C 96 N ILE C 245
SHEET 7 CA 7 ILE C 279 ARG C 286 -1 O ALA C 280 N THR C 97
SHEET 1 CB11 ILE C 159 GLU C 162 0
SHEET 2 CB11 LYS C 147 ASN C 153 -1 O VAL C 150 N ILE C 161
SHEET 3 CB11 TYR C 138 HIS C 144 1 O TYR C 138 N ASN C 153
SHEET 4 CB11 GLU C 123 SER C 131 1 O ALA C 124 N ILE C 143
SHEET 5 CB11 GLN C 240 ILE C 245 1 N ALA C 241 O ASP C 130
SHEET 6 CB11 THR C 86 LYS C 99 -1 O ILE C 96 N ILE C 245
SHEET 7 CB11 GLY C 256 TYR C 263 -1 O GLY C 256 N PHE C 89
SHEET 8 CB11 ALA C 110 SER C 118 -1 O ALA C 114 N TYR C 262
SHEET 9 CB11 HIS C 174 SER C 181 -1 O HIS C 174 N PHE C 117
SHEET 10 CB11 ASN C 184 VAL C 189 -1 O ASN C 184 N SER C 181
SHEET 11 CB11 ILE C 195 ARG C 197 -1 O ILE C 195 N LEU C 187
SHEET 1 CC 2 ILE C 279 ARG C 286 0
SHEET 2 CC 2 THR C 86 LYS C 99 -1 O ILE C 88 N ARG C 286
SHEET 1 DA 7 ILE D 159 GLU D 162 0
SHEET 2 DA 7 LYS D 147 ASN D 153 -1 O VAL D 150 N ILE D 161
SHEET 3 DA 7 TYR D 138 HIS D 144 1 O TYR D 138 N ASN D 153
SHEET 4 DA 7 ALA D 124 SER D 131 1 O ALA D 124 N ILE D 143
SHEET 5 DA 7 GLN D 240 ILE D 245 1 N ALA D 241 O ASP D 130
SHEET 6 DA 7 THR D 86 LYS D 99 -1 O ILE D 96 N ILE D 245
SHEET 7 DA 7 ILE D 279 ARG D 286 -1 O ALA D 280 N THR D 97
SHEET 1 DB11 ILE D 159 GLU D 162 0
SHEET 2 DB11 LYS D 147 ASN D 153 -1 O VAL D 150 N ILE D 161
SHEET 3 DB11 TYR D 138 HIS D 144 1 O TYR D 138 N ASN D 153
SHEET 4 DB11 ALA D 124 SER D 131 1 O ALA D 124 N ILE D 143
SHEET 5 DB11 GLN D 240 ILE D 245 1 N ALA D 241 O ASP D 130
SHEET 6 DB11 THR D 86 LYS D 99 -1 O ILE D 96 N ILE D 245
SHEET 7 DB11 GLY D 256 TYR D 263 -1 O GLY D 256 N PHE D 89
SHEET 8 DB11 ALA D 110 SER D 118 -1 O ALA D 114 N TYR D 262
SHEET 9 DB11 HIS D 174 SER D 181 -1 O HIS D 174 N PHE D 117
SHEET 10 DB11 ASN D 184 VAL D 189 -1 O ASN D 184 N SER D 181
SHEET 11 DB11 ILE D 195 ARG D 197 -1 O ILE D 195 N LEU D 187
SHEET 1 DC 2 ILE D 279 ARG D 286 0
SHEET 2 DC 2 THR D 86 LYS D 99 -1 O ILE D 88 N ARG D 286
SSBOND 1 CYS A 110 CYS A 146 1555 1555 2.05
SSBOND 2 CYS A 306 CYS A 317 1555 1555 2.09
SSBOND 3 CYS A 476 CYS A 510 1555 1555 2.07
SSBOND 4 CYS B 110 CYS B 146 1555 1555 2.07
SSBOND 5 CYS B 306 CYS B 317 1555 1555 2.07
SSBOND 6 CYS B 476 CYS B 510 1555 1555 2.06
LINK ND2 ASN A 102 C1 NAG A 700 1555 1555 1.44
LINK ND2 ASN A 511 C1 NAG A 701 1555 1555 1.37
LINK ND2 ASN B 102 C1 NAG B 700 1555 1555 1.39
LINK ND2 ASN B 511 C1 NAG B 701 1555 1555 1.52
LINK CA CA C1296 O ILE C 236 1555 1555 2.24
LINK CA CA C1296 OD2 ASP C 137 1555 1555 2.34
LINK CA CA C1296 OD1 ASN C 238 1555 1555 2.30
LINK CA CA C1296 O HOH C2012 1555 1555 2.11
LINK CA CA C1296 O VAL C 154 1555 1555 2.36
LINK CA CA C1296 O HOH A2060 1555 1555 2.53
LINK CA CA D1289 OD2 ASP D 137 1555 1555 2.30
LINK CA CA D1289 O HOH B2096 1555 1555 2.27
LINK CA CA D1289 O VAL D 154 1555 1555 2.34
LINK CA CA D1289 O ILE D 236 1555 1555 2.27
LINK CA CA D1289 O HOH D2006 1555 1555 1.98
LINK CA CA D1289 OD1 ASN D 238 1555 1555 2.27
CISPEP 1 PRO A 410 GLU A 411 0 2.93
SITE 1 AC1 4 ARG A 56 ASN A 102 HOH A2124 ASN D 165
SITE 1 AC2 1 ASN A 511
SITE 1 AC3 4 ARG A 232 GLU A 235 GLU A 270 LEU A 272
SITE 1 AC4 4 GLN A 292 PRO A 293 ALA A 294 LYS A 295
SITE 1 AC5 7 PHE A 106 ALA A 107 ALA A 108 VAL A 109
SITE 2 AC5 7 CYS A 146 ASN A 183 ASN A 202
SITE 1 AC6 4 ASN A 386 EDO A1608 GLN C 121 GLU C 123
SITE 1 AC7 4 THR A 391 PRO A 392 PRO A 433 ARG A 436
SITE 1 AC8 7 TYR A 569 ASP A 580 HIS A 581 TYR A 582
SITE 2 AC8 7 ARG A 583 HOH A2125 HOH A2126
SITE 1 AC9 6 ILE A 126 CYS A 476 MET A 480 LYS A 481
SITE 2 AC9 6 ASP A 491 PHE A 508
SITE 1 BC1 4 THR A 137 TYR A 138 GLN A 140 ASP A 141
SITE 1 BC2 1 GLN A 373
SITE 1 BC3 5 GLY A 382 VAL A 384 EDO A1602 HOH A2129
SITE 2 BC3 5 LYS C 122
SITE 1 BC4 2 ARG A 583 THR A 585
SITE 1 BC5 2 MET A 423 LYS A 586
SITE 1 BC6 5 ILE B 100 ASN B 102 EDO B1609 HOH B2157
SITE 2 BC6 5 HOH B2158
SITE 1 BC7 1 ASN B 511
SITE 1 BC8 3 GLN B 292 ALA B 294 LYS B 295
SITE 1 BC9 7 VAL B 454 TYR B 562 GLN B 567 TYR B 569
SITE 2 BC9 7 HIS B 581 TYR B 582 HOH B2159
SITE 1 CC1 4 MET B 178 GLN B 329 THR B 330 ILE B 331
SITE 1 CC2 2 HIS B 447 LEU B 591
SITE 1 CC3 2 ASP B -8 LYS B 54
SITE 1 CC4 3 GLU B 235 PRO B 245 GLY B 271
SITE 1 CC5 8 PHE B 88 GLN B 89 PRO B 90 GLN B 216
SITE 2 CC5 8 ALA B 217 LYS B 219 TYR B 222 HOH B2161
SITE 1 CC6 4 ASP B 122 TYR B 336 LYS B 378 PHE B 379
SITE 1 CC7 7 ASP B 122 LEU B 124 ILE B 126 GLU B 375
SITE 2 CC7 7 GLY B 376 LYS B 378 PHE B 444
SITE 1 CC8 2 ASP B 385 THR B 391
SITE 1 CC9 2 TYR B 45 NAG B 700
SITE 1 DC1 2 GLY B 84 ASN B 320
SITE 1 DC2 5 LYS A 575 LEU B 62 ASN B 64 GLU B 65
SITE 2 DC2 5 LEU B 67
SITE 1 DC3 6 GLY B 174 GLY B 175 GLU B 179 GLY B 180
SITE 2 DC3 6 THR B 181 MET B 184
SITE 1 DC4 3 ARG B 583 THR B 585 LYS B 586
SITE 1 DC5 2 MET B 423 LYS B 586
SITE 1 DC6 1 GLU B 592
SITE 1 DC7 6 TRP B 97 THR B 98 ILE B 100 ARG B 101
SITE 2 DC7 6 GLU C 196 HOH C2038
SITE 1 DC8 4 SER B 96 HOH B2024 VAL C 194 GLU C 196
SITE 1 DC9 3 LYS C 122 GLN C 145 ASN C 169
SITE 1 EC1 2 TYR C 173 ASP C 190
SITE 1 EC2 3 ALA C 110 ASP C 111 ARG C 112
SITE 1 EC3 4 GLU B 85 GLY C 260 TYR C 262 EDO C1295
SITE 1 EC4 4 ALA C 114 TYR C 173 GLY C 260 EDO C1294
SITE 1 EC5 6 HOH A2060 ASP C 137 VAL C 154 ILE C 236
SITE 2 EC5 6 ASN C 238 HOH C2012
SITE 1 EC6 6 HOH B2096 ASP D 137 VAL D 154 ILE D 236
SITE 2 EC6 6 ASN D 238 HOH D2006
CRYST1 136.307 198.779 85.896 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 0.007336 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011642 0.00000
TER 4183 HIS A 598
TER 8460 HIS B 598
TER 9820 VAL C 288
TER 11180 VAL D 288
MASTER 992 0 42 52 70 0 55 611720 4 220 120
END |