| 2WQZ-pdb | HEADER CELL ADHESION 28-AUG-09 2WQZ
TITLE STRUCTURAL ANALYSIS OF THE SYNAPTIC PROTEIN NEUROLIGIN AND
TITLE 2 ITS BETA-NEUREXIN COMPLEX: DETERMINANTS FOR FOLDING AND
TITLE 3 CELL ADHESION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN 4, X-LINKED;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ACETYLCHOLINESTERASE-LIKE DOMAIN, RESIDUES
COMPND 5 43-619;
COMPND 6 SYNONYM: NEUROLIGIN X, HNLX, NEUROLIGIN 4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NEUREXIN-1-BETA;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: LNS DOMAIN, RESIDUES 80-258;
COMPND 12 SYNONYM: NEUREXIN I-BETA, BETA-NEUREXIN 1;
COMPND 13 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 EXPRESSION_SYSTEM_PLASMID: PCDNA3;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 11 ORGANISM_COMMON: NORWAY RAT;
SOURCE 12 ORGANISM_TAXID: 10116;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS TRANSMEMBRANE, DISULFIDE BOND, ALTERNATIVE SPLICING,
KEYWDS 2 ALPHA/BETA-HYDROLASE CHOLINESTERASE AUTISM BRAIN,
KEYWDS 3 ALTERNATIVE PROMOTER USAGE, MEMBRANE, POLYMORPHISM,
KEYWDS 4 GLYCOPROTEIN, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR I.P.FABRICHNY,P.LEONE,G.SULZENBACHER,D.COMOLETTI,M.T.MILLER,
AUTHOR 2 P.TAYLOR,Y.BOURNE,P.MARCHOT
REVDAT 1 08-SEP-09 2WQZ 0
SPRSDE 08-SEP-09 2WQZ 2VH8
JRNL AUTH I.P.FABRICHNY,P.LEONE,G.SULZENBACHER,D.COMOLETTI,
JRNL AUTH 2 M.T.MILLER,P.TAYLOR,Y.BOURNE,P.MARCHOT
JRNL TITL STRUCTURAL ANALYSIS OF THE SYNAPTIC PROTEIN
JRNL TITL 2 NEUROLIGIN AND ITS BETA-NEUREXIN COMPLEX:
JRNL TITL 3 DETERMINANTS FOR FOLDING AND CELL ADHESION.
JRNL REF NEURON V. 56 979 2007
JRNL REFN ISSN 0896-6273
JRNL PMID 18093521
JRNL DOI 10.1016/J.NEURON.2007.11.013
REMARK 2
REMARK 2 RESOLUTION. 3.90 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) : 3.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 23955
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1261
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) : 3.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1708
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11329
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 0.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.45000
REMARK 3 B22 (A**2) : 1.97000
REMARK 3 B33 (A**2) : -4.42000
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): 0.000
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.754
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.634
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 107.112
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11652 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7685 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15870 ; 1.396 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18751 ; 0.964 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1434 ; 8.921 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 555 ;37.618 ;24.595
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1825 ;21.169 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;15.843 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1728 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13088 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2340 ; 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): 7162 ; 0.265 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2926 ; 0.031 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11575 ; 0.505 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4490 ; 0.518 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4295 ; 0.935 ; 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 41 A 62 4
REMARK 3 1 B 41 B 62 4
REMARK 3 2 A 69 A 110 4
REMARK 3 2 B 69 B 110 4
REMARK 3 3 A 143 A 407 4
REMARK 3 3 B 143 B 407 4
REMARK 3 4 A 414 A 598 4
REMARK 3 4 B 414 B 598 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 6558 ; 0.58 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 6558 ; 0.58 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 6558 ; 0.19 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 6558 ; 0.19 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 82 C 288 6
REMARK 3 1 D 82 D 288 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 2 C (A): 2284 ; 0.69 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 D (A): 2284 ; 0.69 ; 5.00
REMARK 3 LOOSE THERMAL 2 C (A**2): 2284 ; 2.42 ; 10.00
REMARK 3 LOOSE THERMAL 2 D (A**2): 2284 ; 2.42 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 36 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): 16.9210 -27.9620 -22.9670
REMARK 3 T TENSOR
REMARK 3 T11: 0.7429 T22: 0.9095
REMARK 3 T33: 0.1342 T12: 0.3462
REMARK 3 T13: 0.0274 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 3.4087 L22: 4.7559
REMARK 3 L33: 2.7718 L12: 0.5660
REMARK 3 L13: -0.1984 L23: 0.6453
REMARK 3 S TENSOR
REMARK 3 S11: -0.1461 S12: -0.1220 S13: -0.2798
REMARK 3 S21: -0.1501 S22: -0.0044 S23: 0.2469
REMARK 3 S31: 0.6732 S32: 0.4592 S33: 0.1505
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): 24.3170 -28.1930 -3.2510
REMARK 3 T TENSOR
REMARK 3 T11: 1.8188 T22: 1.6665
REMARK 3 T33: 0.7178 T12: 0.3443
REMARK 3 T13: 0.0402 T23: 0.2418
REMARK 3 L TENSOR
REMARK 3 L11: 1.6048 L22: 1.2814
REMARK 3 L33: 17.4789 L12: 0.6610
REMARK 3 L13: 4.9744 L23: 3.3775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0338 S12: -0.1830 S13: -0.1868
REMARK 3 S21: 1.2982 S22: 0.4799 S23: -0.0128
REMARK 3 S31: 1.4267 S32: 0.7992 S33: -0.4460
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): 41.9160 -35.1760 -12.7890
REMARK 3 T TENSOR
REMARK 3 T11: 1.1128 T22: 1.5468
REMARK 3 T33: 0.6496 T12: 0.6648
REMARK 3 T13: -0.1894 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 2.5074 L22: 14.4300
REMARK 3 L33: 1.6264 L12: 0.0103
REMARK 3 L13: 1.0342 L23: 1.7792
REMARK 3 S TENSOR
REMARK 3 S11: -0.2819 S12: -0.7186 S13: -0.6403
REMARK 3 S21: 0.5785 S22: 0.8047 S23: -0.9152
REMARK 3 S31: 0.4611 S32: 0.3944 S33: -0.5228
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): 33.1300 -1.9570 -8.5740
REMARK 3 T TENSOR
REMARK 3 T11: 0.5279 T22: 1.3331
REMARK 3 T33: 0.2211 T12: 0.0308
REMARK 3 T13: -0.0257 T23: -0.1738
REMARK 3 L TENSOR
REMARK 3 L11: 2.3860 L22: 10.6577
REMARK 3 L33: 7.5802 L12: -0.3204
REMARK 3 L13: -1.4227 L23: 1.5534
REMARK 3 S TENSOR
REMARK 3 S11: 0.1149 S12: -0.5092 S13: 0.2596
REMARK 3 S21: -0.0385 S22: 0.0884 S23: -1.2435
REMARK 3 S31: -0.2373 S32: 0.9898 S33: -0.2034
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): 8.2220 -15.3340 -11.9190
REMARK 3 T TENSOR
REMARK 3 T11: 0.6723 T22: 0.9139
REMARK 3 T33: 0.4586 T12: 0.3120
REMARK 3 T13: 0.0583 T23: -0.0878
REMARK 3 L TENSOR
REMARK 3 L11: 2.8971 L22: 7.2514
REMARK 3 L33: 7.8824 L12: 4.0361
REMARK 3 L13: -1.2665 L23: 1.5828
REMARK 3 S TENSOR
REMARK 3 S11: 0.2050 S12: -0.5095 S13: 0.2750
REMARK 3 S21: 0.6509 S22: -0.6814 S23: 0.7435
REMARK 3 S31: 0.2661 S32: -0.2073 S33: 0.4764
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 41 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): 35.9700 44.9260 -9.7840
REMARK 3 T TENSOR
REMARK 3 T11: 0.9559 T22: 1.0702
REMARK 3 T33: 0.7037 T12: -0.3283
REMARK 3 T13: 0.0001 T23: 0.3163
REMARK 3 L TENSOR
REMARK 3 L11: 3.1243 L22: 4.8910
REMARK 3 L33: 2.6647 L12: 1.1567
REMARK 3 L13: 0.5052 L23: -0.2695
REMARK 3 S TENSOR
REMARK 3 S11: -0.4155 S12: 0.6157 S13: 1.0476
REMARK 3 S21: -0.3023 S22: 0.1884 S23: 0.1987
REMARK 3 S31: -0.6450 S32: 0.3613 S33: 0.2272
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): 37.7780 42.6570 -30.5740
REMARK 3 T TENSOR
REMARK 3 T11: 2.1428 T22: 1.7674
REMARK 3 T33: 1.1731 T12: -0.1076
REMARK 3 T13: 0.4352 T23: 0.5133
REMARK 3 L TENSOR
REMARK 3 L11: 11.6148 L22: 3.4745
REMARK 3 L33: 13.3244 L12: 5.8267
REMARK 3 L13: 8.5614 L23: 6.1620
REMARK 3 S TENSOR
REMARK 3 S11: -0.1439 S12: -0.2084 S13: 0.7209
REMARK 3 S21: -0.5226 S22: -0.1115 S23: 0.2169
REMARK 3 S31: -0.7035 S32: 0.4766 S33: 0.2554
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): 58.3240 41.0030 -26.1960
REMARK 3 T TENSOR
REMARK 3 T11: 1.3321 T22: 2.2185
REMARK 3 T33: 1.1905 T12: -0.6116
REMARK 3 T13: 0.4093 T23: 0.3029
REMARK 3 L TENSOR
REMARK 3 L11: 4.6730 L22: 1.5079
REMARK 3 L33: 3.7246 L12: -2.2472
REMARK 3 L13: -4.0441 L23: 2.2478
REMARK 3 S TENSOR
REMARK 3 S11: -0.3863 S12: 0.3345 S13: 0.2952
REMARK 3 S21: -0.0838 S22: 0.6924 S23: -0.5626
REMARK 3 S31: 0.1771 S32: 0.2600 S33: -0.3061
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 599
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4510 15.2320 -25.2780
REMARK 3 T TENSOR
REMARK 3 T11: 1.0246 T22: 1.5831
REMARK 3 T33: 0.2570 T12: -0.2006
REMARK 3 T13: 0.2911 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 2.3970 L22: 8.5945
REMARK 3 L33: 6.9745 L12: 1.7912
REMARK 3 L13: 1.8220 L23: -0.8028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0492 S12: 1.1385 S13: -0.1969
REMARK 3 S21: -0.7862 S22: 0.0790 S23: -0.7292
REMARK 3 S31: 0.0925 S32: 0.9092 S33: -0.0298
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): 20.1700 37.8770 -17.8340
REMARK 3 T TENSOR
REMARK 3 T11: 1.1597 T22: 1.2944
REMARK 3 T33: 0.9970 T12: -0.3895
REMARK 3 T13: -0.1281 T23: 0.4885
REMARK 3 L TENSOR
REMARK 3 L11: 1.7031 L22: 5.8026
REMARK 3 L33: 3.2643 L12: -2.7990
REMARK 3 L13: 1.5292 L23: -1.5818
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: 0.6180 S13: 0.1203
REMARK 3 S21: -0.9769 S22: -0.5067 S23: 0.7353
REMARK 3 S31: -0.8661 S32: 0.3537 S33: 0.3548
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 : C 82 C 288
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8220 34.7450 24.5020
REMARK 3 T TENSOR
REMARK 3 T11: 1.0191 T22: 0.6880
REMARK 3 T33: 0.5771 T12: -0.1776
REMARK 3 T13: 0.1893 T23: 0.2732
REMARK 3 L TENSOR
REMARK 3 L11: 8.6491 L22: 3.8831
REMARK 3 L33: 8.0125 L12: 0.1871
REMARK 3 L13: -1.0385 L23: 1.4070
REMARK 3 S TENSOR
REMARK 3 S11: 0.1207 S12: -0.2955 S13: 0.0303
REMARK 3 S21: 0.8591 S22: 0.0575 S23: -0.0884
REMARK 3 S31: 0.0819 S32: -0.5901 S33: -0.1782
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 : D 82 D 288
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3140 -18.1800 -58.7990
REMARK 3 T TENSOR
REMARK 3 T11: 1.5971 T22: 1.7505
REMARK 3 T33: 0.4634 T12: 0.4487
REMARK 3 T13: -0.1152 T23: -0.1523
REMARK 3 L TENSOR
REMARK 3 L11: 3.4926 L22: 2.4429
REMARK 3 L33: 8.4211 L12: 2.3321
REMARK 3 L13: 1.1626 L23: -0.2421
REMARK 3 S TENSOR
REMARK 3 S11: -0.2306 S12: 1.3767 S13: -0.2489
REMARK 3 S21: -0.9179 S22: 0.2282 S23: 0.1569
REMARK 3 S31: 0.4506 S32: -0.1325 S33: 0.0024
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2WQZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-AUG-09.
REMARK 100 THE PDBE ID CODE IS EBI-40882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25251
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.90
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.8
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.9
REMARK 200 R MERGE FOR SHELL (I) : 0.56
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRIES 3BE8 AND 1C4R
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 20000, 0.1M MES PH6.5
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 79.26000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 99.33500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 79.26000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 99.33500
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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 32
REMARK 465 TYR A 33
REMARK 465 LYS A 34
REMARK 465 ASP A 35
REMARK 465 ASP A 161
REMARK 465 GLN A 162
REMARK 465 ASN A 163
REMARK 465 VAL A 540
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 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 32
REMARK 465 TYR B 33
REMARK 465 LYS B 34
REMARK 465 ASP B 35
REMARK 465 ASP B 36
REMARK 465 ASP B 37
REMARK 465 ASP B 38
REMARK 465 LYS B 39
REMARK 465 LEU B 40
REMARK 465 VAL B 540
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 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 ND2 ASN A 432 - OG1 THR A 435 2.09
REMARK 500 O PRO A 452 - O ALA A 455 2.16
REMARK 500 O LEU B 263 - OG SER B 269 2.15
REMARK 500 O GLY B 360 - N PHE B 362 2.16
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 C 200 C GLY C 231 N 1.411
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 PRO A 504 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500 PRO A 564 C - N - CA ANGL. DEV. = 10.6 DEGREES
REMARK 500 ALA C 200 CA - C - N ANGL. DEV. = -40.2 DEGREES
REMARK 500 ALA C 200 O - C - N ANGL. DEV. = -33.3 DEGREES
REMARK 500 GLY C 231 C - N - CA ANGL. DEV. = -32.6 DEGREES
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 37 -71.55 -147.99
REMARK 500 LEU A 40 -75.36 -67.98
REMARK 500 PRO A 46 -173.95 -68.85
REMARK 500 PRO A 81 121.27 -37.70
REMARK 500 ARG A 87 131.99 -16.21
REMARK 500 PRO A 93 167.11 -40.96
REMARK 500 SER A 95 -139.69 -95.06
REMARK 500 THR A 104 25.06 -145.03
REMARK 500 ALA A 108 159.36 -45.09
REMARK 500 PRO A 111 106.38 -51.49
REMARK 500 GLU A 116 -32.09 -36.46
REMARK 500 SER A 118 32.95 98.00
REMARK 500 LEU A 119 -148.08 -103.64
REMARK 500 HIS A 121 -62.47 3.21
REMARK 500 ILE A 126 -56.73 -8.81
REMARK 500 PHE A 128 -60.35 -177.45
REMARK 500 ASN A 131 -52.57 83.97
REMARK 500 LEU A 132 -60.82 11.52
REMARK 500 ASP A 133 -83.94 -19.59
REMARK 500 THR A 134 34.37 -99.79
REMARK 500 LEU A 135 48.17 -97.21
REMARK 500 MET A 136 34.59 -156.07
REMARK 500 VAL A 139 -93.30 -67.15
REMARK 500 GLN A 140 138.31 -39.50
REMARK 500 ASP A 141 71.82 89.78
REMARK 500 ASP A 145 91.40 -59.81
REMARK 500 LEU A 147 88.96 -69.72
REMARK 500 ILE A 159 68.97 -69.89
REMARK 500 SER A 176 33.25 -148.03
REMARK 500 TYR A 177 -174.50 56.01
REMARK 500 GLU A 179 174.54 173.62
REMARK 500 ARG A 204 150.85 -49.58
REMARK 500 GLN A 216 -68.51 58.30
REMARK 500 ALA A 218 76.57 -159.15
REMARK 500 LEU A 224 82.67 -58.31
REMARK 500 LEU A 225 -40.80 177.54
REMARK 500 GLU A 235 -46.85 -28.52
REMARK 500 THR A 282 -159.29 -136.74
REMARK 500 ALA A 294 -70.03 -38.23
REMARK 500 LYS A 303 49.33 -88.87
REMARK 500 VAL A 304 18.95 -169.76
REMARK 500 MET A 308 126.63 -38.04
REMARK 500 LEU A 309 43.80 -95.60
REMARK 500 LYS A 321 -116.98 -118.76
REMARK 500 TYR A 323 -14.86 -46.15
REMARK 500 LYS A 324 -157.35 -89.95
REMARK 500 GLU A 325 -65.96 50.25
REMARK 500 GLN A 328 -1.97 -58.84
REMARK 500 THR A 335 117.61 -28.10
REMARK 500 TYR A 336 44.70 71.03
REMARK 500 ASP A 347 -87.81 -111.27
REMARK 500 GLU A 358 -22.64 -36.12
REMARK 500 GLN A 359 -90.80 -149.88
REMARK 500 LEU A 363 -113.81 -82.61
REMARK 500 ASP A 366 96.79 -59.07
REMARK 500 LEU A 377 -59.56 25.85
REMARK 500 VAL A 380 36.52 -92.32
REMARK 500 ASP A 388 5.71 157.03
REMARK 500 ASN A 393 30.92 -75.26
REMARK 500 PHE A 402 -62.47 -130.74
REMARK 500 TYR A 407 60.31 -104.08
REMARK 500 TYR A 409 -29.12 95.98
REMARK 500 PRO A 410 5.43 -68.65
REMARK 500 GLU A 411 36.91 -28.12
REMARK 500 LYS A 413 -85.67 27.76
REMARK 500 ASP A 414 -54.50 -12.12
REMARK 500 ASP A 429 62.70 -105.35
REMARK 500 GLU A 431 -74.63 -83.78
REMARK 500 ASN A 432 98.17 -2.30
REMARK 500 LEU A 443 -76.59 -58.74
REMARK 500 TRP A 449 -53.43 -139.40
REMARK 500 THR A 456 -65.90 81.02
REMARK 500 TYR A 463 79.31 -113.93
REMARK 500 GLN A 477 124.04 54.96
REMARK 500 SER A 478 -173.95 -172.11
REMARK 500 MET A 480 98.68 47.71
REMARK 500 LYS A 481 105.46 105.75
REMARK 500 SER A 487 107.55 -56.15
REMARK 500 PRO A 500 33.60 -69.26
REMARK 500 ILE A 502 133.77 -175.43
REMARK 500 PRO A 504 -128.71 0.55
REMARK 500 THR A 505 164.21 175.22
REMARK 500 LEU A 507 -71.72 66.80
REMARK 500 PHE A 508 57.75 -103.73
REMARK 500 THR A 533 -133.24 -119.28
REMARK 500 ASP A 535 96.14 -175.89
REMARK 500 TRP A 559 -99.36 -74.77
REMARK 500 SER A 560 151.21 107.82
REMARK 500 ASN A 563 98.89 178.10
REMARK 500 PRO A 564 -21.27 -28.35
REMARK 500 ILE A 572 88.06 -69.14
REMARK 500 ARG A 579 -167.77 -122.47
REMARK 500 HIS A 581 61.95 62.38
REMARK 500 TYR A 582 101.13 -59.54
REMARK 500 ALA A 584 -69.90 -19.71
REMARK 500 GLU A 592 -79.47 -128.30
REMARK 500 VAL A 594 -64.56 -166.51
REMARK 500 HIS A 596 85.68 -69.12
REMARK 500 LEU A 597 -66.39 -157.98
REMARK 500 PRO B 94 -178.28 -63.01
REMARK 500 SER B 95 -149.03 -115.27
REMARK 500 THR B 98 98.72 -56.35
REMARK 500 THR B 104 -20.78 -154.91
REMARK 500 ALA B 108 -168.72 -59.73
REMARK 500 PRO B 111 69.92 -16.85
REMARK 500 HIS B 113 101.27 -163.96
REMARK 500 SER B 118 44.14 -140.43
REMARK 500 LEU B 120 -59.52 52.85
REMARK 500 HIS B 121 -31.76 71.02
REMARK 500 MET B 123 59.33 -105.88
REMARK 500 PRO B 125 131.91 -39.23
REMARK 500 ALA B 130 137.45 142.46
REMARK 500 ASN B 131 -5.37 79.17
REMARK 500 THR B 155 -130.46 -73.23
REMARK 500 GLU B 156 122.04 57.41
REMARK 500 ILE B 159 56.36 -111.62
REMARK 500 ASN B 163 -86.91 -138.55
REMARK 500 SER B 164 162.09 62.04
REMARK 500 LYS B 165 113.29 58.31
REMARK 500 SER B 176 42.92 31.37
REMARK 500 TYR B 177 -13.35 64.03
REMARK 500 THR B 181 127.05 176.88
REMARK 500 PHE B 210 30.09 -140.62
REMARK 500 GLN B 216 -100.16 55.72
REMARK 500 ALA B 240 -75.88 -65.92
REMARK 500 ILE B 278 76.52 -118.34
REMARK 500 SER B 286 14.77 -60.37
REMARK 500 TRP B 287 51.98 -145.33
REMARK 500 LYS B 303 49.83 -91.56
REMARK 500 VAL B 304 -26.73 -166.01
REMARK 500 LYS B 321 -140.77 -72.52
REMARK 500 TYR B 323 -18.72 -35.58
REMARK 500 LYS B 324 -66.54 -91.04
REMARK 500 GLN B 328 69.52 -60.57
REMARK 500 THR B 335 125.55 -34.81
REMARK 500 TYR B 336 -46.72 84.60
REMARK 500 ASP B 347 -91.58 -100.10
REMARK 500 GLU B 361 50.14 -24.61
REMARK 500 ASN B 364 89.00 -53.06
REMARK 500 LEU B 377 -37.94 -30.10
REMARK 500 VAL B 380 47.45 -87.79
REMARK 500 TYR B 407 -123.63 -80.48
REMARK 500 TYR B 409 -72.77 93.07
REMARK 500 GLU B 411 -144.79 33.90
REMARK 500 LYS B 413 -22.04 -29.16
REMARK 500 ASP B 429 58.32 -149.82
REMARK 500 ASN B 432 111.83 -25.39
REMARK 500 TRP B 449 -46.74 -138.90
REMARK 500 TYR B 463 63.22 -118.58
REMARK 500 CYS B 476 -91.67 -57.04
REMARK 500 GLN B 477 94.34 167.24
REMARK 500 GLU B 479 1.94 -65.32
REMARK 500 SER B 487 93.72 -47.26
REMARK 500 ILE B 502 -146.36 -129.98
REMARK 500 GLU B 506 79.29 -62.80
REMARK 500 LEU B 507 -63.93 170.61
REMARK 500 SER B 509 76.84 36.46
REMARK 500 ASP B 535 106.65 -178.30
REMARK 500 PRO B 536 5.59 -65.42
REMARK 500 GLU B 556 -157.21 -48.26
REMARK 500 VAL B 557 139.99 127.10
REMARK 500 GLN B 567 46.69 72.37
REMARK 500 HIS B 581 -58.33 91.62
REMARK 500 TYR B 582 91.87 63.39
REMARK 500 LEU B 597 124.41 8.07
REMARK 500 ALA C 83 147.55 -173.06
REMARK 500 ASN C 103 3.84 102.09
REMARK 500 ASP C 111 113.18 178.54
REMARK 500 ALA C 124 122.60 179.41
REMARK 500 LEU C 126 -82.40 -111.59
REMARK 500 SER C 132 176.68 170.21
REMARK 500 THR C 156 -82.68 -81.27
REMARK 500 ASN C 169 76.23 -102.11
REMARK 500 ASP C 170 38.02 -141.07
REMARK 500 ASP C 190 -135.67 54.43
REMARK 500 PHE C 237 82.27 -66.39
REMARK 500 SER C 239 84.71 55.41
REMARK 500 ALA C 241 -16.65 -142.61
REMARK 500 ASN C 264 -101.94 51.34
REMARK 500 ASN C 275 69.69 92.89
REMARK 500 ASN C 278 41.89 -87.99
REMARK 500 THR D 85 88.08 -66.26
REMARK 500 PRO D 102 -35.82 -37.06
REMARK 500 SER D 107 105.82 65.90
REMARK 500 PHE D 117 -164.16 -106.64
REMARK 500 SER D 118 100.35 -177.85
REMARK 500 VAL D 120 35.02 -142.13
REMARK 500 ALA D 124 170.45 178.39
REMARK 500 SER D 131 -101.64 73.12
REMARK 500 SER D 132 -156.14 -159.96
REMARK 500 ILE D 143 38.13 -84.68
REMARK 500 THR D 156 -88.41 -83.70
REMARK 500 ALA D 160 107.53 -164.29
REMARK 500 ASN D 169 45.50 -85.01
REMARK 500 VAL D 175 72.61 -102.08
REMARK 500 THR D 186 108.54 -163.78
REMARK 500 GLN D 188 91.35 -166.60
REMARK 500 ASP D 190 -61.28 74.87
REMARK 500 SER D 191 -6.48 -153.91
REMARK 500 TRP D 192 -160.17 -65.00
REMARK 500 TYR D 198 58.35 -143.29
REMARK 500 ARG D 232 86.05 -173.51
REMARK 500 PHE D 237 167.80 -44.89
REMARK 500 ALA D 241 -57.21 -120.14
REMARK 500 GLN D 257 -178.69 -171.37
REMARK 500 LYS D 267 98.21 -68.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 360 GLU A 361 -123.19
REMARK 500 PRO A 410 GLU A 411 -134.52
REMARK 500 GLU A 411 GLY A 412 149.91
REMARK 500 ASN A 537 GLN A 538 -143.98
REMARK 500 LEU A 597 HIS A 598 -147.48
REMARK 500 GLU B 556 VAL B 557 138.91
REMARK 500 HIS B 596 LEU B 597 -139.34
REMARK 500 LEU B 597 HIS B 598 149.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA C 200 27.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--N1(N9)--O4'--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLN A 538 24.9 L L OUTSIDE RANGE
REMARK 500 LEU B 597 24.0 L L OUTSIDE RANGE
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 D1289 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 137 OD2
REMARK 620 2 VAL D 154 O 56.2
REMARK 620 3 ILE D 236 O 85.5 72.5
REMARK 620 4 ASN D 238 OD1 70.8 120.2 78.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1289 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 137 OD2
REMARK 620 2 ASN C 238 OD1 82.2
REMARK 620 3 VAL C 154 O 81.5 136.3
REMARK 620 4 ILE C 236 O 71.5 57.4 79.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AX A1599
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AX A1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
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
DBREF 2WQZ A 32 42 PDB 2WQZ 2WQZ 32 42
DBREF 2WQZ A 43 619 UNP Q8N0W4 NLGNX_HUMAN 43 619
DBREF 2WQZ B 32 42 PDB 2WQZ 2WQZ 32 42
DBREF 2WQZ B 43 619 UNP Q8N0W4 NLGNX_HUMAN 43 619
DBREF 2WQZ C 80 200 UNP Q63373 NRX1B_RAT 80 200
DBREF 2WQZ C 231 288 UNP Q63373 NRX1B_RAT 201 258
DBREF 2WQZ D 80 200 UNP Q63373 NRX1B_RAT 80 200
DBREF 2WQZ D 231 288 UNP Q63373 NRX1B_RAT 201 258
SEQADV 2WQZ ARG A 561 UNP Q8N0W4 LYS 561 CONFLICT
SEQADV 2WQZ ARG B 561 UNP Q8N0W4 LYS 561 CONFLICT
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 5AX A1599 14
HET 5AX A1600 14
HET CA C1289 1
HET CA D1289 1
HETNAM CA CALCIUM ION
HETNAM 5AX 2-(ACETYLAMINO)-1,5-ANHYDRO-2-DEOXY-D-
HETNAM 2 5AX GLUCITOL
FORMUL 5 CA 2(CA 2+)
FORMUL 6 5AX 2(C8 H15 N O5)
HELIX 1 1 ASP A 38 TYR A 45 1 8
HELIX 2 2 LEU A 120 LEU A 124 5 5
HELIX 3 3 PRO A 125 ALA A 130 1 6
HELIX 4 4 ASN A 131 LEU A 135 5 5
HELIX 5 5 SER A 188 TYR A 193 1 6
HELIX 6 6 LEU A 225 VAL A 238 1 14
HELIX 7 7 ALA A 257 LEU A 265 1 9
HELIX 8 8 GLN A 292 LYS A 303 1 12
HELIX 9 9 ASP A 310 ASN A 320 1 11
HELIX 10 10 ASP A 352 GLU A 358 1 7
HELIX 11 11 LEU A 377 ASP A 381 5 5
HELIX 12 12 THR A 391 SER A 400 1 10
HELIX 13 13 PHE A 402 TYR A 407 1 6
HELIX 14 14 ASP A 414 TYR A 424 1 11
HELIX 15 15 ASN A 432 TRP A 449 1 18
HELIX 16 16 TRP A 449 ALA A 455 1 7
HELIX 17 17 THR A 456 TYR A 463 1 8
HELIX 18 18 GLU A 492 PHE A 497 1 6
HELIX 19 19 SER A 513 THR A 533 1 21
HELIX 20 20 ARG A 583 GLU A 592 1 10
HELIX 21 21 ALA B 41 TYR B 45 5 5
HELIX 22 22 PRO B 125 THR B 129 5 5
HELIX 23 23 ASN B 131 THR B 137 1 7
HELIX 24 24 SER B 188 TYR B 193 1 6
HELIX 25 25 LEU B 224 VAL B 238 1 15
HELIX 26 26 ALA B 257 LEU B 263 1 7
HELIX 27 27 GLN B 292 ASP B 302 1 11
HELIX 28 28 ASP B 310 ARG B 319 1 10
HELIX 29 29 ASP B 352 GLN B 359 1 8
HELIX 30 30 LEU B 377 ASP B 381 5 5
HELIX 31 31 THR B 391 LEU B 406 1 16
HELIX 32 32 LYS B 413 TYR B 424 1 12
HELIX 33 33 ASN B 432 TRP B 449 1 18
HELIX 34 34 TRP B 449 TYR B 463 1 15
HELIX 35 35 GLU B 492 PHE B 497 1 6
HELIX 36 36 SER B 513 THR B 533 1 21
HELIX 37 37 ARG B 583 LEU B 593 1 11
HELIX 38 38 LYS C 267 ASN C 275 1 9
HELIX 39 39 ASN D 270 ASN D 275 1 6
SHEET 1 AA 2 ILE A 55 ARG A 56 0
SHEET 2 AA 2 ARG A 101 ASN A 102 1 O ARG A 101 N ARG A 56
SHEET 1 AB11 ARG A 59 THR A 60 0
SHEET 2 AB11 VAL A 70 GLN A 72 -1 O VAL A 70 N THR A 60
SHEET 3 AB11 LEU A 149 PRO A 154 -1 O VAL A 153 N GLU A 71
SHEET 4 AB11 ILE A 197 ILE A 201 -1 O VAL A 198 N TYR A 152
SHEET 5 AB11 VAL A 168 TYR A 171 1 O MET A 169 N ILE A 199
SHEET 6 AB11 VAL A 248 PHE A 251 1 O THR A 249 N VAL A 170
SHEET 7 AB11 LYS A 275 ILE A 277 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 6 ARG B 59 THR B 60 0
SHEET 2 BA 6 VAL B 70 TYR B 73 -1 O VAL B 70 N THR B 60
SHEET 3 BA 6 LEU B 149 PRO B 154 -1 O ILE B 151 N TYR B 73
SHEET 4 BA 6 ILE B 197 ILE B 201 -1 O VAL B 198 N TYR B 152
SHEET 5 BA 6 VAL B 168 TYR B 171 1 O MET B 169 N ILE B 199
SHEET 6 BA 6 ILE B 250 PHE B 251 1 N PHE B 251 O VAL B 170
SHEET 1 BB 5 LYS B 275 ILE B 277 0
SHEET 2 BB 5 ASP B 366 ASN B 372 1 O ASP B 366 N ALA B 276
SHEET 3 BB 5 THR B 467 PHE B 472 1 O TYR B 468 N LEU B 369
SHEET 4 BB 5 LEU B 568 ILE B 572 1 O LEU B 568 N PHE B 469
SHEET 5 BB 5 ARG B 577 ASP B 580 -1 O ARG B 577 N HIS B 571
SHEET 1 CA 2 TYR C 87 ILE C 88 0
SHEET 2 CA 2 ARG C 286 LEU C 287 -1 O ARG C 286 N ILE C 88
SHEET 1 CB 7 ILE C 159 ALA C 160 0
SHEET 2 CB 7 LYS C 151 ASN C 153 -1 O PHE C 152 N ILE C 159
SHEET 3 CB 7 TYR C 138 ILE C 143 -1 O TYR C 138 N ASN C 153
SHEET 4 CB 7 ALA C 124 ASP C 130 -1 O ALA C 124 N ILE C 143
SHEET 5 CB 7 THR C 242 ILE C 245 -1 O THR C 242 N ASP C 130
SHEET 6 CB 7 ILE C 96 LYS C 99 -1 O ILE C 96 N ILE C 245
SHEET 7 CB 7 ILE C 279 ILE C 281 -1 O ALA C 280 N THR C 97
SHEET 1 CC 5 ILE C 195 ARG C 197 0
SHEET 2 CC 5 ALA C 185 VAL C 189 -1 O ALA C 185 N ARG C 197
SHEET 3 CC 5 VAL C 176 PHE C 178 -1 O ARG C 177 N GLN C 188
SHEET 4 CC 5 LEU C 113 ILE C 115 -1 O LEU C 113 N PHE C 178
SHEET 5 CC 5 TYR C 262 TYR C 263 -1 O TYR C 262 N ALA C 114
SHEET 1 DA 2 ILE D 96 THR D 97 0
SHEET 2 DA 2 ALA D 280 ILE D 281 -1 O ALA D 280 N THR D 97
SHEET 1 DB 5 GLU D 196 ARG D 197 0
SHEET 2 DB 5 ALA D 185 VAL D 189 -1 O ALA D 185 N ARG D 197
SHEET 3 DB 5 VAL D 176 ARG D 180 -1 O ARG D 177 N GLN D 188
SHEET 4 DB 5 LEU D 113 ILE D 115 -1 O LEU D 113 N PHE D 178
SHEET 5 DB 5 TYR D 262 TYR D 263 -1 O TYR D 262 N ALA D 114
SHEET 1 DC 2 TYR D 138 LEU D 139 0
SHEET 2 DC 2 PHE D 152 ASN D 153 -1 O ASN D 153 N TYR D 138
SSBOND 1 CYS A 110 CYS A 146 1555 1555 2.04
SSBOND 2 CYS A 306 CYS A 317 1555 1555 2.05
SSBOND 3 CYS A 476 CYS A 510 1555 1555 2.05
SSBOND 4 CYS B 110 CYS B 146 1555 1555 2.04
SSBOND 5 CYS B 306 CYS B 317 1555 1555 2.04
SSBOND 6 CYS B 476 CYS B 510 1555 1555 2.06
LINK CA CA C1289 OD2 ASP C 137 1555 1555 2.43
LINK CA CA C1289 O ILE C 236 1555 1555 2.58
LINK CA CA C1289 O VAL C 154 1555 1555 1.94
LINK CA CA C1289 OD1 ASN C 238 1555 1555 2.65
LINK CA CA D1289 OD1 ASN D 238 1555 1555 2.01
LINK CA CA D1289 O ILE D 236 1555 1555 2.56
LINK CA CA D1289 O VAL D 154 1555 1555 2.40
LINK CA CA D1289 OD2 ASP D 137 1555 1555 2.44
SITE 1 AC1 3 ASN A 102 THR A 104 GLN A 105
SITE 1 AC2 2 ASN A 511 ARG D 286
SITE 1 AC3 5 ASP C 137 VAL C 154 GLY C 155 ILE C 236
SITE 2 AC3 5 ASN C 238
SITE 1 AC4 4 ASP D 137 VAL D 154 ILE D 236 ASN D 238
CRYST1 158.520 198.670 85.740 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 0.006308 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011663 0.00000
TER 4311 HIS A 598
TER 8614 ASN B 599
TER 9974 VAL C 288
TER 11334 VAL D 288
MASTER 965 0 4 39 47 0 5 611360 4 50 120
END
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