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HEADER LYASE 23-MAR-22 7ZB1
TITLE S580A WITH 18MER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MACROCYCLASE,OPHP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 18MER;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OMPHALOTUS OLEARIUS;
SOURCE 3 ORGANISM_TAXID: 72120;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: OMPHALOTUS OLEARIUS;
SOURCE 9 ORGANISM_TAXID: 72120;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MACROCYCLASE FOR OMPHALOTIN A BIOSYNTHESIS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SONG,J.H.NAISMITH
REVDAT 1 06-JUL-22 7ZB1 0
JRNL AUTH H.SONG,J.H.NAISMITH
JRNL TITL S580A WITH 18MER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 173300
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 9445
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12735
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE SET COUNT : 666
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23327
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 682
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.19000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : -1.26000
REMARK 3 B12 (A**2) : 1.21000
REMARK 3 B13 (A**2) : 0.60000
REMARK 3 B23 (A**2) : -1.28000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.236
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.769
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24099 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 21787 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32683 ; 1.431 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 50312 ; 1.216 ; 1.577
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2900 ; 7.086 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1328 ;31.162 ;21.935
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3831 ;13.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 152 ;16.634 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3007 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27432 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5808 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 731 B 3 731 23592 0.070 0.050
REMARK 3 2 A 4 730 C 4 730 23581 0.070 0.050
REMARK 3 3 A 4 731 D 4 731 23439 0.080 0.050
REMARK 3 4 B 4 729 C 4 729 23756 0.070 0.050
REMARK 3 5 B 4 731 D 4 731 23672 0.080 0.050
REMARK 3 6 C 4 730 D 4 730 23762 0.070 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 67
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4092 -5.6456 84.9450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1618 T22: 0.5915
REMARK 3 T33: 0.5648 T12: 0.1737
REMARK 3 T13: -0.0865 T23: -0.1782
REMARK 3 L TENSOR
REMARK 3 L11: 1.4539 L22: 1.4395
REMARK 3 L33: 2.8010 L12: -0.3805
REMARK 3 L13: -0.3017 L23: 0.6339
REMARK 3 S TENSOR
REMARK 3 S11: -0.1461 S12: -0.2866 S13: -0.3219
REMARK 3 S21: 0.2167 S22: 0.4255 S23: -0.1268
REMARK 3 S31: 0.6540 S32: 0.6382 S33: -0.2794
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 68 A 147
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1708 -1.3342 97.9836
REMARK 3 T TENSOR
REMARK 3 T11: 0.1195 T22: 0.5167
REMARK 3 T33: 0.4665 T12: 0.0448
REMARK 3 T13: 0.0178 T23: -0.1050
REMARK 3 L TENSOR
REMARK 3 L11: 3.7293 L22: 0.8999
REMARK 3 L33: 0.8821 L12: 1.3941
REMARK 3 L13: 0.3061 L23: 0.6513
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.4094 S13: -0.2226
REMARK 3 S21: 0.1973 S22: -0.0683 S23: 0.0045
REMARK 3 S31: 0.2652 S32: -0.0659 S33: 0.0492
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 148 A 229
REMARK 3 ORIGIN FOR THE GROUP (A): -32.7522 -15.4603 83.9826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.3003
REMARK 3 T33: 0.5067 T12: 0.0402
REMARK 3 T13: 0.0990 T23: -0.0732
REMARK 3 L TENSOR
REMARK 3 L11: 1.9554 L22: 1.1577
REMARK 3 L33: 4.9648 L12: 0.3822
REMARK 3 L13: -2.4572 L23: 0.0672
REMARK 3 S TENSOR
REMARK 3 S11: -0.3166 S12: -0.1482 S13: -0.4464
REMARK 3 S21: 0.1532 S22: 0.0101 S23: 0.0876
REMARK 3 S31: 0.3092 S32: 0.0882 S33: 0.3065
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 230 A 438
REMARK 3 ORIGIN FOR THE GROUP (A): -35.0577 2.0193 69.6698
REMARK 3 T TENSOR
REMARK 3 T11: 0.0328 T22: 0.5135
REMARK 3 T33: 0.5205 T12: 0.0285
REMARK 3 T13: -0.0643 T23: -0.2359
REMARK 3 L TENSOR
REMARK 3 L11: 0.8007 L22: 0.8089
REMARK 3 L33: 1.5846 L12: 0.0893
REMARK 3 L13: -0.6420 L23: 0.6779
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: 0.1303 S13: -0.1009
REMARK 3 S21: -0.0928 S22: -0.1510 S23: 0.2098
REMARK 3 S31: -0.0790 S32: -0.4076 S33: 0.2192
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 439 A 649
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8546 13.8787 83.3936
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: 0.3543
REMARK 3 T33: 0.4284 T12: -0.0043
REMARK 3 T13: -0.0379 T23: -0.2087
REMARK 3 L TENSOR
REMARK 3 L11: 1.0342 L22: 0.9604
REMARK 3 L33: 1.5635 L12: -0.2066
REMARK 3 L13: -0.3579 L23: 0.6668
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: -0.1918 S13: 0.0831
REMARK 3 S21: -0.0608 S22: 0.0690 S23: -0.0204
REMARK 3 S31: -0.1345 S32: 0.1878 S33: -0.0629
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 650 A 731
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2175 2.4073 92.4814
REMARK 3 T TENSOR
REMARK 3 T11: 0.0651 T22: 0.4888
REMARK 3 T33: 0.4618 T12: 0.0942
REMARK 3 T13: -0.0902 T23: -0.1855
REMARK 3 L TENSOR
REMARK 3 L11: 1.1681 L22: 1.4558
REMARK 3 L33: 2.8204 L12: 0.2157
REMARK 3 L13: -0.4585 L23: 1.0540
REMARK 3 S TENSOR
REMARK 3 S11: -0.1081 S12: -0.3375 S13: -0.0633
REMARK 3 S21: 0.1414 S22: 0.2089 S23: -0.0733
REMARK 3 S31: 0.3655 S32: 0.4633 S33: -0.1007
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 1 B 78
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7528 -43.6702 77.4283
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: 0.6690
REMARK 3 T33: 0.9029 T12: -0.0286
REMARK 3 T13: 0.0249 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 2.1988 L22: 1.1675
REMARK 3 L33: 3.0278 L12: 0.3973
REMARK 3 L13: 0.5886 L23: 0.7913
REMARK 3 S TENSOR
REMARK 3 S11: 0.0555 S12: 0.3624 S13: 0.5675
REMARK 3 S21: -0.0921 S22: 0.0088 S23: -0.0456
REMARK 3 S31: -0.2665 S32: 0.5716 S33: -0.0642
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 79 B 146
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5921 -46.4043 71.0727
REMARK 3 T TENSOR
REMARK 3 T11: 0.0392 T22: 0.6937
REMARK 3 T33: 0.5583 T12: 0.0781
REMARK 3 T13: -0.0616 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 3.3046 L22: 1.5224
REMARK 3 L33: 1.9011 L12: 0.3578
REMARK 3 L13: -0.5459 L23: -0.0612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0786 S12: 0.4352 S13: 0.0318
REMARK 3 S21: -0.1629 S22: -0.1181 S23: 0.0970
REMARK 3 S31: -0.1630 S32: -0.3737 S33: 0.0394
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 147 B 225
REMARK 3 ORIGIN FOR THE GROUP (A): -45.7942 -35.1096 85.3231
REMARK 3 T TENSOR
REMARK 3 T11: 0.0812 T22: 0.3794
REMARK 3 T33: 0.5513 T12: 0.1106
REMARK 3 T13: -0.0216 T23: -0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 1.6475 L22: 0.4153
REMARK 3 L33: 5.6576 L12: -0.1751
REMARK 3 L13: 1.0570 L23: 0.3377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0997 S12: 0.0550 S13: 0.2150
REMARK 3 S21: -0.0049 S22: -0.0293 S23: 0.0250
REMARK 3 S31: -0.4124 S32: -0.2989 S33: -0.0704
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 230 B 399
REMARK 3 ORIGIN FOR THE GROUP (A): -45.2039 -52.5782 100.8628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0266 T22: 0.5254
REMARK 3 T33: 0.5674 T12: -0.0097
REMARK 3 T13: 0.0112 T23: -0.1345
REMARK 3 L TENSOR
REMARK 3 L11: 1.3646 L22: 1.3500
REMARK 3 L33: 1.8045 L12: -0.4712
REMARK 3 L13: 0.0314 L23: 0.2781
REMARK 3 S TENSOR
REMARK 3 S11: -0.1207 S12: -0.1143 S13: -0.0949
REMARK 3 S21: 0.1676 S22: 0.0883 S23: 0.2045
REMARK 3 S31: 0.0739 S32: -0.3739 S33: 0.0324
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 400 B 630
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1816 -63.3984 79.5144
REMARK 3 T TENSOR
REMARK 3 T11: 0.0611 T22: 0.4087
REMARK 3 T33: 0.5226 T12: 0.0111
REMARK 3 T13: -0.0055 T23: -0.1721
REMARK 3 L TENSOR
REMARK 3 L11: 1.2196 L22: 0.6062
REMARK 3 L33: 1.5847 L12: -0.2974
REMARK 3 L13: -0.2616 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: 0.2421 S13: 0.0619
REMARK 3 S21: -0.0257 S22: -0.0641 S23: 0.0876
REMARK 3 S31: 0.2972 S32: -0.0552 S33: 0.0383
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 631 B 730
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5265 -50.4355 77.1895
REMARK 3 T TENSOR
REMARK 3 T11: 0.0101 T22: 0.4840
REMARK 3 T33: 0.6183 T12: 0.0484
REMARK 3 T13: 0.0189 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 1.5870 L22: 0.8249
REMARK 3 L33: 3.8459 L12: 0.1632
REMARK 3 L13: 0.1976 L23: -0.0891
REMARK 3 S TENSOR
REMARK 3 S11: 0.0827 S12: 0.1889 S13: 0.3751
REMARK 3 S21: 0.0246 S22: -0.0629 S23: -0.0537
REMARK 3 S31: 0.0127 S32: 0.2816 S33: -0.0198
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 81
REMARK 3 ORIGIN FOR THE GROUP (A): -39.8516 -17.4939 127.5599
REMARK 3 T TENSOR
REMARK 3 T11: 0.1204 T22: 0.4310
REMARK 3 T33: 0.5083 T12: 0.0119
REMARK 3 T13: -0.0913 T23: -0.1282
REMARK 3 L TENSOR
REMARK 3 L11: 2.6117 L22: 1.3593
REMARK 3 L33: 0.5222 L12: -0.8138
REMARK 3 L13: 0.5588 L23: -0.1900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0773 S12: -0.0749 S13: 0.1011
REMARK 3 S21: -0.1762 S22: -0.0036 S23: 0.2298
REMARK 3 S31: -0.1655 S32: -0.2398 S33: 0.0809
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 82 C 169
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8717 -11.1039 126.0786
REMARK 3 T TENSOR
REMARK 3 T11: 0.0781 T22: 0.2732
REMARK 3 T33: 0.5997 T12: -0.0269
REMARK 3 T13: -0.1352 T23: -0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 3.0306 L22: 2.3044
REMARK 3 L33: 3.5917 L12: -0.6810
REMARK 3 L13: 0.3521 L23: 0.2975
REMARK 3 S TENSOR
REMARK 3 S11: -0.1840 S12: 0.0648 S13: 0.5070
REMARK 3 S21: -0.2431 S22: -0.0061 S23: -0.0186
REMARK 3 S31: -0.2414 S32: -0.0263 S33: 0.1901
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 170 C 295
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2677 -24.9653 111.0593
REMARK 3 T TENSOR
REMARK 3 T11: 0.0726 T22: 0.5467
REMARK 3 T33: 0.5612 T12: -0.0871
REMARK 3 T13: -0.0677 T23: -0.1418
REMARK 3 L TENSOR
REMARK 3 L11: 1.7033 L22: 1.6812
REMARK 3 L33: 0.8963 L12: 0.0552
REMARK 3 L13: 1.1773 L23: 0.1505
REMARK 3 S TENSOR
REMARK 3 S11: -0.2083 S12: 0.5800 S13: 0.0379
REMARK 3 S21: -0.2355 S22: 0.0351 S23: -0.1247
REMARK 3 S31: -0.1703 S32: 0.2609 S33: 0.1732
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 296 C 364
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6870 -43.6498 121.1066
REMARK 3 T TENSOR
REMARK 3 T11: 0.0191 T22: 0.3665
REMARK 3 T33: 0.6431 T12: -0.0087
REMARK 3 T13: 0.0170 T23: -0.2243
REMARK 3 L TENSOR
REMARK 3 L11: 2.2136 L22: 1.1911
REMARK 3 L33: 2.4043 L12: 0.7041
REMARK 3 L13: -0.8585 L23: -1.3816
REMARK 3 S TENSOR
REMARK 3 S11: -0.1616 S12: 0.2915 S13: -0.4770
REMARK 3 S21: -0.0651 S22: 0.1142 S23: -0.0602
REMARK 3 S31: 0.1495 S32: 0.0800 S33: 0.0474
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 365 C 656
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7550 -28.9967 140.3077
REMARK 3 T TENSOR
REMARK 3 T11: 0.0206 T22: 0.4316
REMARK 3 T33: 0.5094 T12: 0.0386
REMARK 3 T13: -0.0429 T23: -0.1124
REMARK 3 L TENSOR
REMARK 3 L11: 2.0598 L22: 0.5086
REMARK 3 L33: 0.4817 L12: -0.4322
REMARK 3 L13: 0.3238 L23: -0.0773
REMARK 3 S TENSOR
REMARK 3 S11: -0.1724 S12: -0.3977 S13: -0.1290
REMARK 3 S21: 0.0447 S22: 0.1245 S23: 0.0060
REMARK 3 S31: -0.0325 S32: -0.0732 S33: 0.0479
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 657 C 730
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7906 -15.6797 132.7851
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.3676
REMARK 3 T33: 0.5495 T12: 0.0032
REMARK 3 T13: -0.1007 T23: -0.1487
REMARK 3 L TENSOR
REMARK 3 L11: 2.6683 L22: 2.1477
REMARK 3 L33: 2.1564 L12: 0.4731
REMARK 3 L13: 0.4903 L23: 1.6437
REMARK 3 S TENSOR
REMARK 3 S11: -0.1838 S12: -0.1852 S13: 0.1648
REMARK 3 S21: -0.2608 S22: 0.1541 S23: -0.0068
REMARK 3 S31: -0.1311 S32: 0.1195 S33: 0.0297
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 84
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1016 -36.8990 41.4027
REMARK 3 T TENSOR
REMARK 3 T11: 0.0471 T22: 0.4956
REMARK 3 T33: 0.6885 T12: -0.0475
REMARK 3 T13: 0.0364 T23: -0.2403
REMARK 3 L TENSOR
REMARK 3 L11: 1.3892 L22: 2.4738
REMARK 3 L33: 1.3281 L12: -0.0852
REMARK 3 L13: -0.6708 L23: 1.1578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0937 S12: 0.0757 S13: -0.4774
REMARK 3 S21: 0.2791 S22: -0.2540 S23: 0.5631
REMARK 3 S31: 0.1946 S32: -0.2406 S33: 0.3477
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 85 D 229
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9749 -39.4758 50.5035
REMARK 3 T TENSOR
REMARK 3 T11: 0.0517 T22: 0.3526
REMARK 3 T33: 0.5544 T12: 0.0393
REMARK 3 T13: -0.0074 T23: -0.1428
REMARK 3 L TENSOR
REMARK 3 L11: 1.1304 L22: 0.6399
REMARK 3 L33: 1.5741 L12: -0.5432
REMARK 3 L13: -0.2250 L23: 0.8422
REMARK 3 S TENSOR
REMARK 3 S11: -0.1229 S12: -0.1610 S13: -0.2612
REMARK 3 S21: 0.1739 S22: 0.1417 S23: -0.0229
REMARK 3 S31: 0.2488 S32: 0.0726 S33: -0.0187
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 230 D 326
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4609 -16.5979 56.5015
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.4305
REMARK 3 T33: 0.5366 T12: 0.0352
REMARK 3 T13: -0.0472 T23: -0.1969
REMARK 3 L TENSOR
REMARK 3 L11: 1.3127 L22: 0.7083
REMARK 3 L33: 1.3680 L12: -0.1591
REMARK 3 L13: -0.4496 L23: 0.5386
REMARK 3 S TENSOR
REMARK 3 S11: -0.1575 S12: -0.2026 S13: 0.0871
REMARK 3 S21: 0.1379 S22: 0.2025 S23: -0.1151
REMARK 3 S31: -0.0262 S32: 0.1998 S33: -0.0450
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 327 D 570
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5489 -23.4037 27.4667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0359 T22: 0.4529
REMARK 3 T33: 0.4601 T12: -0.0315
REMARK 3 T13: -0.0147 T23: -0.1792
REMARK 3 L TENSOR
REMARK 3 L11: 1.2181 L22: 0.7648
REMARK 3 L33: 0.7951 L12: -0.2795
REMARK 3 L13: 0.0289 L23: 0.4592
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: 0.2759 S13: -0.0169
REMARK 3 S21: -0.1457 S22: -0.0222 S23: -0.0424
REMARK 3 S31: -0.1240 S32: 0.0116 S33: 0.0072
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 571 D 697
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2596 -27.1015 37.4657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0657 T22: 0.4805
REMARK 3 T33: 0.6108 T12: -0.0325
REMARK 3 T13: -0.0085 T23: -0.2557
REMARK 3 L TENSOR
REMARK 3 L11: 1.8162 L22: 0.8513
REMARK 3 L33: 1.0193 L12: 0.2359
REMARK 3 L13: -0.0338 L23: 0.7044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.2155 S13: -0.1934
REMARK 3 S21: 0.1362 S22: -0.1230 S23: 0.2451
REMARK 3 S31: 0.0290 S32: -0.2136 S33: 0.1343
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 698 D 731
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8487 -43.9878 30.4644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1603 T22: 0.4651
REMARK 3 T33: 0.6552 T12: 0.0016
REMARK 3 T13: -0.0003 T23: -0.2252
REMARK 3 L TENSOR
REMARK 3 L11: 1.2435 L22: 1.9819
REMARK 3 L33: 7.4071 L12: -0.8280
REMARK 3 L13: -1.5025 L23: 3.8126
REMARK 3 S TENSOR
REMARK 3 S11: -0.2617 S12: 0.0195 S13: -0.5417
REMARK 3 S21: 0.2308 S22: 0.2277 S23: 0.1202
REMARK 3 S31: 0.4884 S32: 0.5224 S33: 0.0340
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7ZB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1292121164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : APEX
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 182773
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 55.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 1.23400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
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: 5N4C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE (PH 6.0-6.5) AND 28% PEG 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 225
REMARK 465 ASP A 226
REMARK 465 GLU A 227
REMARK 465 GLY A 228
REMARK 465 ASN A 698
REMARK 465 SER A 699
REMARK 465 GLY A 700
REMARK 465 HIS A 701
REMARK 465 PHE A 702
REMARK 465 ALA A 703
REMARK 465 GLN A 732
REMARK 465 GLY A 733
REMARK 465 SER A 734
REMARK 465 VAL A 735
REMARK 465 ASP A 736
REMARK 465 SER A 737
REMARK 465 SER A 738
REMARK 465 ARG A 739
REMARK 465 TRP A 740
REMARK 465 SER A 741
REMARK 465 CYS A 742
REMARK 465 VAL A 743
REMARK 465 THR A 744
REMARK 465 VAL A 745
REMARK 465 ASP B 226
REMARK 465 GLU B 227
REMARK 465 GLY B 228
REMARK 465 LYS B 229
REMARK 465 PHE B 702
REMARK 465 ALA B 703
REMARK 465 GLN B 732
REMARK 465 GLY B 733
REMARK 465 SER B 734
REMARK 465 VAL B 735
REMARK 465 ASP B 736
REMARK 465 SER B 737
REMARK 465 SER B 738
REMARK 465 ARG B 739
REMARK 465 TRP B 740
REMARK 465 SER B 741
REMARK 465 CYS B 742
REMARK 465 VAL B 743
REMARK 465 THR B 744
REMARK 465 VAL B 745
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 PHE C 3
REMARK 465 ASP C 225
REMARK 465 ASP C 226
REMARK 465 GLU C 227
REMARK 465 GLY C 228
REMARK 465 PHE C 702
REMARK 465 ALA C 703
REMARK 465 THR C 731
REMARK 465 GLN C 732
REMARK 465 GLY C 733
REMARK 465 SER C 734
REMARK 465 VAL C 735
REMARK 465 ASP C 736
REMARK 465 SER C 737
REMARK 465 SER C 738
REMARK 465 ARG C 739
REMARK 465 TRP C 740
REMARK 465 SER C 741
REMARK 465 CYS C 742
REMARK 465 VAL C 743
REMARK 465 THR C 744
REMARK 465 VAL C 745
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 PHE D 3
REMARK 465 PHE D 702
REMARK 465 ALA D 703
REMARK 465 GLY D 704
REMARK 465 LYS D 705
REMARK 465 GLN D 732
REMARK 465 GLY D 733
REMARK 465 SER D 734
REMARK 465 VAL D 735
REMARK 465 ASP D 736
REMARK 465 SER D 737
REMARK 465 SER D 738
REMARK 465 ARG D 739
REMARK 465 TRP D 740
REMARK 465 SER D 741
REMARK 465 CYS D 742
REMARK 465 VAL D 743
REMARK 465 THR D 744
REMARK 465 VAL D 745
REMARK 465 TRP E 795
REMARK 465 MVA E 796
REMARK 465 ILE E 797
REMARK 465 MVA E 798
REMARK 465 MVA E 799
REMARK 465 SAR E 800
REMARK 465 MVA E 801
REMARK 465 MET E 809
REMARK 465 SER E 810
REMARK 465 THR E 811
REMARK 465 GLU E 812
REMARK 465 TRP F 795
REMARK 465 MVA F 796
REMARK 465 ILE F 797
REMARK 465 MVA F 798
REMARK 465 MVA F 799
REMARK 465 SAR F 800
REMARK 465 MVA F 801
REMARK 465 MET F 809
REMARK 465 SER F 810
REMARK 465 THR F 811
REMARK 465 GLU F 812
REMARK 465 TRP G 795
REMARK 465 MVA G 796
REMARK 465 ILE G 797
REMARK 465 MVA G 798
REMARK 465 MVA G 799
REMARK 465 SAR G 800
REMARK 465 MVA G 801
REMARK 465 MET G 809
REMARK 465 SER G 810
REMARK 465 THR G 811
REMARK 465 GLU G 812
REMARK 465 TRP H 795
REMARK 465 MVA H 796
REMARK 465 ILE H 797
REMARK 465 MVA H 798
REMARK 465 MVA H 799
REMARK 465 SAR H 800
REMARK 465 MVA H 801
REMARK 465 IML H 802
REMARK 465 MET H 809
REMARK 465 SER H 810
REMARK 465 THR H 811
REMARK 465 GLU H 812
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 OE1 GLU A 246 O GLY B 189 2.04
REMARK 500 OD1 ASP C 257 O HOH C 901 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 GLU A 323 CD GLU A 323 OE1 -0.089
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 168 136.65 -38.07
REMARK 500 HIS A 201 35.89 73.49
REMARK 500 ASN A 236 51.00 75.22
REMARK 500 ASN A 303 42.33 -100.53
REMARK 500 ALA A 335 82.91 -157.18
REMARK 500 TYR A 338 154.17 72.14
REMARK 500 GLN A 372 -52.79 75.76
REMARK 500 ASP A 373 28.10 -144.65
REMARK 500 TYR A 499 -76.40 -134.58
REMARK 500 LEU A 546 -124.22 54.08
REMARK 500 ALA A 580 -110.09 58.91
REMARK 500 ILE A 607 -40.50 -134.08
REMARK 500 THR A 616 -107.69 31.60
REMARK 500 SER A 641 104.91 -43.23
REMARK 500 GLN A 730 70.43 -106.76
REMARK 500 SER B 2 161.55 163.99
REMARK 500 SER B 168 134.92 -34.54
REMARK 500 SER B 185 6.75 84.68
REMARK 500 HIS B 201 35.45 74.90
REMARK 500 ASN B 236 51.15 74.14
REMARK 500 ALA B 335 84.42 -158.84
REMARK 500 TYR B 338 152.57 73.89
REMARK 500 GLN B 372 -53.92 75.29
REMARK 500 ASP B 373 28.22 -145.31
REMARK 500 TYR B 499 -76.31 -131.55
REMARK 500 LEU B 546 -124.40 54.15
REMARK 500 ALA B 580 -110.22 57.77
REMARK 500 ILE B 607 -42.17 -133.79
REMARK 500 THR B 616 -108.61 30.29
REMARK 500 SER B 641 104.72 -43.16
REMARK 500 HIS C 166 -163.80 64.47
REMARK 500 HIS C 201 35.94 72.97
REMARK 500 ASN C 236 50.24 74.37
REMARK 500 ASN C 303 37.84 -99.54
REMARK 500 ALA C 335 85.89 -161.68
REMARK 500 TYR C 338 154.53 72.64
REMARK 500 GLN C 372 -53.44 75.06
REMARK 500 ASP C 373 28.53 -143.21
REMARK 500 TYR C 499 -75.03 -130.08
REMARK 500 LEU C 546 -124.89 52.63
REMARK 500 ALA C 580 -110.02 58.96
REMARK 500 ILE C 607 -39.23 -135.17
REMARK 500 THR C 616 -108.19 31.33
REMARK 500 SER C 641 104.68 -42.57
REMARK 500 ASP C 651 45.81 -142.47
REMARK 500 HIS D 166 84.09 50.79
REMARK 500 ASP D 191 79.30 -112.93
REMARK 500 HIS D 201 36.76 73.49
REMARK 500 ASN D 236 50.85 75.14
REMARK 500 ASN D 303 45.93 -103.45
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 IML E 802 SAR E 803 -143.43
REMARK 500 IML F 802 SAR F 803 -145.53
REMARK 500 IML G 802 SAR G 803 -146.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D1113 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH D1114 DISTANCE = 7.08 ANGSTROMS
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 NA A 804 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 56 O
REMARK 620 2 GLN A 56 OE1 99.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 806 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 470 OG
REMARK 620 2 HOH A 926 O 148.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 802 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 504 O
REMARK 620 2 HOH A 967 O 111.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 807 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 509 O
REMARK 620 2 HOH A 958 O 101.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 803 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 600 O
REMARK 620 2 THR A 602 OG1 123.5
REMARK 620 3 LEU A 658 O 73.0 107.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 803 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 262 O
REMARK 620 2 HOH B 931 O 137.8
REMARK 620 3 HOH B1005 O 78.3 128.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 804 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 337 O
REMARK 620 2 TYR B 338 O 65.9
REMARK 620 3 ALA B 362 O 89.7 155.1
REMARK 620 4 HOH B 912 O 127.7 73.5 129.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 802 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 499 O
REMARK 620 2 ASN B 581 O 95.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 801 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 544 O
REMARK 620 2 GLU B 624 OE1 120.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 807 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 544 O
REMARK 620 2 GLU C 624 OE1 120.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 806 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL C 600 O
REMARK 620 2 THR C 602 OG1 120.8
REMARK 620 3 LEU C 658 O 73.7 103.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 805 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 660 O
REMARK 620 2 THR C 673 OG1 111.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 807 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 281 OG
REMARK 620 2 ASP D 283 O 91.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 806 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE D 401 O
REMARK 620 2 PHE D 402 O 84.0
REMARK 620 3 HOH D 937 O 147.1 63.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 805 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 587 O
REMARK 620 2 ASN D 591 OD1 72.3
REMARK 620 N 1
DBREF 7ZB1 A 1 745 PDB 7ZB1 7ZB1 1 745
DBREF 7ZB1 B 1 745 PDB 7ZB1 7ZB1 1 745
DBREF 7ZB1 C 1 745 PDB 7ZB1 7ZB1 1 745
DBREF 7ZB1 D 1 745 PDB 7ZB1 7ZB1 1 745
DBREF 7ZB1 E 795 812 PDB 7ZB1 7ZB1 795 812
DBREF 7ZB1 F 795 812 PDB 7ZB1 7ZB1 795 812
DBREF 7ZB1 G 795 812 PDB 7ZB1 7ZB1 795 812
DBREF 7ZB1 H 795 812 PDB 7ZB1 7ZB1 795 812
SEQRES 1 A 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 A 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 A 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 A 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 A 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 A 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 A 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 A 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 A 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 A 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 A 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 A 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 A 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 A 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 A 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 A 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 A 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 A 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 A 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 A 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 A 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 A 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 A 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 A 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 A 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 A 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 A 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 A 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 A 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 A 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 A 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 A 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 A 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 A 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 A 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 A 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 A 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 A 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 A 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 A 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 A 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 A 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 A 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 A 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 A 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 A 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 A 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 A 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 A 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 A 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 A 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 A 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 A 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 A 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 A 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 A 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 A 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 A 745 CYS VAL THR VAL
SEQRES 1 B 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 B 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 B 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 B 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 B 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 B 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 B 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 B 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 B 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 B 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 B 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 B 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 B 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 B 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 B 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 B 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 B 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 B 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 B 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 B 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 B 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 B 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 B 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 B 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 B 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 B 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 B 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 B 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 B 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 B 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 B 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 B 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 B 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 B 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 B 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 B 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 B 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 B 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 B 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 B 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 B 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 B 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 B 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 B 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 B 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 B 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 B 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 B 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 B 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 B 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 B 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 B 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 B 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 B 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 B 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 B 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 B 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 B 745 CYS VAL THR VAL
SEQRES 1 C 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 C 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 C 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 C 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 C 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 C 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 C 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 C 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 C 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 C 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 C 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 C 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 C 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 C 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 C 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 C 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 C 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 C 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 C 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 C 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 C 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 C 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 C 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 C 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 C 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 C 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 C 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 C 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 C 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 C 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 C 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 C 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 C 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 C 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 C 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 C 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 C 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 C 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 C 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 C 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 C 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 C 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 C 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 C 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 C 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 C 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 C 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 C 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 C 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 C 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 C 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 C 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 C 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 C 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 C 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 C 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 C 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 C 745 CYS VAL THR VAL
SEQRES 1 D 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 D 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 D 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 D 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 D 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 D 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 D 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 D 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 D 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 D 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 D 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 D 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 D 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 D 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 D 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 D 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 D 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 D 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 D 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 D 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 D 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 D 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 D 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 D 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 D 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 D 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 D 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 D 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 D 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 D 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 D 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 D 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 D 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 D 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 D 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 D 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 D 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 D 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 D 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 D 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 D 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 D 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 D 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 D 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 D 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 D 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 D 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 D 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 D 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 D 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 D 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 D 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 D 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 D 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 D 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 D 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 D 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 D 745 CYS VAL THR VAL
SEQRES 1 E 18 TRP MVA ILE MVA MVA SAR MVA IML SAR VAL IML SAR SER
SEQRES 2 E 18 MVA MET SER THR GLU
SEQRES 1 F 18 TRP MVA ILE MVA MVA SAR MVA IML SAR VAL IML SAR SER
SEQRES 2 F 18 MVA MET SER THR GLU
SEQRES 1 G 18 TRP MVA ILE MVA MVA SAR MVA IML SAR VAL IML SAR SER
SEQRES 2 G 18 MVA MET SER THR GLU
SEQRES 1 H 18 TRP MVA ILE MVA MVA SAR MVA IML SAR VAL IML SAR SER
SEQRES 2 H 18 MVA MET SER THR GLU
HET IML E 802 9
HET SAR E 803 5
HET IML E 805 9
HET SAR E 806 5
HET MVA E 808 8
HET IML F 802 9
HET SAR F 803 5
HET IML F 805 9
HET SAR F 806 5
HET MVA F 808 8
HET IML G 802 9
HET SAR G 803 5
HET IML G 805 9
HET SAR G 806 5
HET MVA G 808 8
HET SAR H 803 5
HET IML H 805 9
HET SAR H 806 5
HET MVA H 808 8
HET EDO A 801 4
HET NA A 802 1
HET NA A 803 1
HET NA A 804 1
HET NA A 805 1
HET NA A 806 1
HET NA A 807 1
HET NA B 801 1
HET NA B 802 1
HET NA B 803 1
HET NA B 804 1
HET EDO C 801 4
HET BCT C 802 4
HET GOL C 803 6
HET EDO C 804 4
HET NA C 805 1
HET NA C 806 1
HET NA C 807 1
HET BCT D 801 4
HET EDO D 802 4
HET BCT D 803 4
HET BCT D 804 4
HET NA D 805 1
HET NA D 806 1
HET NA D 807 1
HETNAM IML N-METHYL-ISOLEUCINE
HETNAM SAR SARCOSINE
HETNAM MVA N-METHYLVALINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETNAM BCT BICARBONATE ION
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 IML 7(C7 H15 N O2)
FORMUL 5 SAR 8(C3 H7 N O2)
FORMUL 5 MVA 4(C6 H13 N O2)
FORMUL 9 EDO 4(C2 H6 O2)
FORMUL 10 NA 16(NA 1+)
FORMUL 21 BCT 4(C H O3 1-)
FORMUL 22 GOL C3 H8 O3
FORMUL 34 HOH *682(H2 O)
HELIX 1 AA1 TYR A 36 VAL A 41 5 6
HELIX 2 AA2 PRO A 42 ASP A 45 5 4
HELIX 3 AA3 SER A 46 GLU A 66 1 21
HELIX 4 AA4 PRO A 68 TRP A 81 1 14
HELIX 5 AA5 GLU A 118 VAL A 122 5 5
HELIX 6 AA6 ASN A 135 LEU A 139 5 5
HELIX 7 AA7 GLU A 165 SER A 168 5 4
HELIX 8 AA8 ASP A 247 ASP A 251 5 5
HELIX 9 AA9 HIS A 347 GLU A 350 5 4
HELIX 10 AB1 ASN A 457 ASP A 459 5 3
HELIX 11 AB2 SER A 511 ARG A 522 1 12
HELIX 12 AB3 GLU A 538 GLU A 543 1 6
HELIX 13 AB4 GLY A 544 LYS A 548 5 5
HELIX 14 AB5 LYS A 549 ASN A 566 1 18
HELIX 15 AB6 ASN A 581 ALA A 593 1 13
HELIX 16 AB7 PRO A 594 TYR A 597 5 4
HELIX 17 AB8 ARG A 611 PHE A 615 5 5
HELIX 18 AB9 PHE A 617 SER A 620 5 4
HELIX 19 AC1 TRP A 621 GLY A 626 1 6
HELIX 20 AC2 ASP A 630 SER A 641 1 12
HELIX 21 AC3 PRO A 642 ASN A 645 5 4
HELIX 22 AC4 PRO A 670 PHE A 684 1 15
HELIX 23 AC5 SER A 706 GLY A 726 1 21
HELIX 24 AC6 TYR B 36 VAL B 41 5 6
HELIX 25 AC7 PRO B 42 ASP B 45 5 4
HELIX 26 AC8 SER B 46 GLU B 66 1 21
HELIX 27 AC9 ASN B 67 TRP B 81 1 15
HELIX 28 AD1 GLU B 118 VAL B 122 5 5
HELIX 29 AD2 ASN B 135 LEU B 139 5 5
HELIX 30 AD3 GLU B 165 SER B 168 5 4
HELIX 31 AD4 ASP B 247 ASP B 251 5 5
HELIX 32 AD5 HIS B 347 GLU B 350 5 4
HELIX 33 AD6 ASN B 457 ASP B 459 5 3
HELIX 34 AD7 SER B 511 TYR B 521 1 11
HELIX 35 AD8 GLY B 537 GLU B 543 1 7
HELIX 36 AD9 GLY B 544 LYS B 548 5 5
HELIX 37 AE1 LYS B 549 ASN B 566 1 18
HELIX 38 AE2 ASN B 581 ALA B 593 1 13
HELIX 39 AE3 PRO B 594 TYR B 597 5 4
HELIX 40 AE4 ARG B 611 PHE B 615 5 5
HELIX 41 AE5 PHE B 617 SER B 620 5 4
HELIX 42 AE6 TRP B 621 GLY B 626 1 6
HELIX 43 AE7 ASP B 630 SER B 641 1 12
HELIX 44 AE8 PRO B 642 ASN B 645 5 4
HELIX 45 AE9 PRO B 670 PHE B 684 1 15
HELIX 46 AF1 SER B 706 GLY B 726 1 21
HELIX 47 AF2 TYR C 36 VAL C 41 5 6
HELIX 48 AF3 PRO C 42 ASP C 45 5 4
HELIX 49 AF4 SER C 46 ASN C 67 1 22
HELIX 50 AF5 PRO C 68 TRP C 81 1 14
HELIX 51 AF6 GLU C 118 VAL C 122 5 5
HELIX 52 AF7 ASN C 135 LEU C 139 5 5
HELIX 53 AF8 ASP C 247 ASP C 251 5 5
HELIX 54 AF9 HIS C 347 GLU C 350 5 4
HELIX 55 AG1 ASN C 457 ASP C 459 5 3
HELIX 56 AG2 SER C 511 TYR C 521 1 11
HELIX 57 AG3 GLY C 537 GLU C 543 1 7
HELIX 58 AG4 GLY C 544 LYS C 548 5 5
HELIX 59 AG5 LYS C 549 ASN C 566 1 18
HELIX 60 AG6 ASN C 581 ALA C 593 1 13
HELIX 61 AG7 PRO C 594 TYR C 597 5 4
HELIX 62 AG8 ARG C 611 PHE C 615 5 5
HELIX 63 AG9 PHE C 617 SER C 620 5 4
HELIX 64 AH1 TRP C 621 GLY C 626 1 6
HELIX 65 AH2 ASP C 630 SER C 641 1 12
HELIX 66 AH3 PRO C 642 ASN C 645 5 4
HELIX 67 AH4 PRO C 648 THR C 652 5 5
HELIX 68 AH5 PRO C 670 PHE C 684 1 15
HELIX 69 AH6 SER C 706 GLY C 726 1 21
HELIX 70 AH7 TYR D 36 VAL D 41 5 6
HELIX 71 AH8 PRO D 42 ASP D 45 5 4
HELIX 72 AH9 SER D 46 GLU D 66 1 21
HELIX 73 AI1 ASN D 67 TRP D 81 1 15
HELIX 74 AI2 GLU D 118 VAL D 122 5 5
HELIX 75 AI3 ASN D 135 LEU D 139 5 5
HELIX 76 AI4 ASP D 247 ASP D 251 5 5
HELIX 77 AI5 HIS D 347 GLU D 350 5 4
HELIX 78 AI6 ASN D 457 ASP D 459 5 3
HELIX 79 AI7 SER D 511 ARG D 522 1 12
HELIX 80 AI8 GLY D 537 GLU D 543 1 7
HELIX 81 AI9 GLY D 544 LYS D 548 5 5
HELIX 82 AJ1 LYS D 549 ASN D 566 1 18
HELIX 83 AJ2 ASN D 581 ALA D 593 1 13
HELIX 84 AJ3 PRO D 594 TYR D 597 5 4
HELIX 85 AJ4 ARG D 611 PHE D 615 5 5
HELIX 86 AJ5 PHE D 617 SER D 620 5 4
HELIX 87 AJ6 TRP D 621 GLY D 626 1 6
HELIX 88 AJ7 ASP D 630 SER D 641 1 12
HELIX 89 AJ8 PRO D 642 ASN D 645 5 4
HELIX 90 AJ9 PRO D 648 THR D 652 5 5
HELIX 91 AK1 PRO D 670 PHE D 684 1 15
HELIX 92 AK2 THR D 707 GLY D 726 1 20
SHEET 1 AA1 2 ALA A 19 SER A 24 0
SHEET 2 AA1 2 GLY A 28 ARG A 33 -1 O VAL A 32 N ILE A 20
SHEET 1 AA2 3 ARG A 85 PHE A 86 0
SHEET 2 AA2 3 HIS A 96 ASN A 102 -1 O ASN A 102 N ARG A 85
SHEET 3 AA2 3 LYS A 90 PRO A 91 -1 N LYS A 90 O TYR A 98
SHEET 1 AA3 4 ARG A 85 PHE A 86 0
SHEET 2 AA3 4 HIS A 96 ASN A 102 -1 O ASN A 102 N ARG A 85
SHEET 3 AA3 4 SER A 110 ARG A 115 -1 O TYR A 112 N PHE A 99
SHEET 4 AA3 4 GLU A 131 PHE A 134 -1 O GLU A 131 N ARG A 113
SHEET 1 AA4 4 ALA A 146 MET A 152 0
SHEET 2 AA4 4 TYR A 158 SER A 164 -1 O GLY A 162 N THR A 148
SHEET 3 AA4 4 MET A 171 LYS A 177 -1 O TYR A 174 N TYR A 161
SHEET 4 AA4 4 ILE A 199 VAL A 202 -1 O VAL A 202 N MET A 171
SHEET 1 AA5 4 SER A 208 TRP A 209 0
SHEET 2 AA5 4 GLY A 215 ARG A 220 -1 O PHE A 217 N SER A 208
SHEET 3 AA5 4 MET A 238 ARG A 243 -1 O MET A 238 N ARG A 220
SHEET 4 AA5 4 VAL A 252 HIS A 255 -1 O VAL A 254 N VAL A 239
SHEET 1 AA6 4 ILE A 264 LEU A 269 0
SHEET 2 AA6 4 TYR A 275 SER A 281 -1 O LEU A 277 N GLN A 268
SHEET 3 AA6 4 LEU A 289 ASP A 294 -1 O LYS A 291 N PHE A 278
SHEET 4 AA6 4 LYS A 307 ASN A 308 -1 O LYS A 307 N ILE A 292
SHEET 1 AA7 4 PHE A 317 GLU A 323 0
SHEET 2 AA7 4 LYS A 326 THR A 331 -1 O TYR A 328 N VAL A 320
SHEET 3 AA7 4 LYS A 339 ASP A 344 -1 O PHE A 343 N ILE A 327
SHEET 4 AA7 4 LEU A 352 ILE A 356 -1 O THR A 353 N THR A 342
SHEET 1 AA8 4 PHE A 363 HIS A 370 0
SHEET 2 AA8 4 LYS A 374 ARG A 381 -1 O LEU A 376 N SER A 368
SHEET 3 AA8 4 SER A 384 ASP A 391 -1 O ARG A 390 N LEU A 375
SHEET 4 AA8 4 PRO A 397 ILE A 401 -1 O GLY A 399 N ILE A 389
SHEET 1 AA9 4 GLN A 408 SER A 412 0
SHEET 2 AA9 4 ASP A 419 SER A 425 -1 O LEU A 423 N MET A 410
SHEET 3 AA9 4 THR A 432 THR A 437 -1 O THR A 432 N PHE A 424
SHEET 4 AA9 4 TYR A 444 ALA A 450 -1 O ARG A 449 N VAL A 433
SHEET 1 AB1 8 PHE A 461 PRO A 469 0
SHEET 2 AB1 8 SER A 475 PRO A 483 -1 O MET A 478 N VAL A 466
SHEET 3 AB1 8 ILE A 524 PRO A 528 -1 O TYR A 525 N THR A 481
SHEET 4 AB1 8 VAL A 494 TYR A 497 1 N LEU A 495 O ALA A 526
SHEET 5 AB1 8 ILE A 574 GLY A 579 1 O ALA A 575 N GLN A 496
SHEET 6 AB1 8 CYS A 599 ILE A 603 1 O ILE A 601 N ILE A 576
SHEET 7 AB1 8 ALA A 656 ALA A 662 1 O PHE A 660 N THR A 602
SHEET 8 AB1 8 CYS A 691 ASP A 696 1 O ARG A 694 N PHE A 659
SHEET 1 AB2 2 ALA B 19 SER B 24 0
SHEET 2 AB2 2 GLY B 28 ARG B 33 -1 O VAL B 32 N ILE B 20
SHEET 1 AB3 3 ARG B 85 PHE B 86 0
SHEET 2 AB3 3 HIS B 96 ASN B 102 -1 O ASN B 102 N ARG B 85
SHEET 3 AB3 3 LYS B 90 PRO B 91 -1 N LYS B 90 O TYR B 98
SHEET 1 AB4 4 ARG B 85 PHE B 86 0
SHEET 2 AB4 4 HIS B 96 ASN B 102 -1 O ASN B 102 N ARG B 85
SHEET 3 AB4 4 SER B 110 ARG B 115 -1 O SER B 110 N TYR B 101
SHEET 4 AB4 4 GLU B 131 PHE B 134 -1 O GLU B 131 N ARG B 113
SHEET 1 AB5 4 ALA B 146 MET B 152 0
SHEET 2 AB5 4 TYR B 158 SER B 164 -1 O GLY B 162 N THR B 148
SHEET 3 AB5 4 MET B 171 LYS B 177 -1 O TYR B 174 N TYR B 161
SHEET 4 AB5 4 LYS B 198 VAL B 202 -1 O VAL B 202 N MET B 171
SHEET 1 AB6 4 SER B 208 TRP B 209 0
SHEET 2 AB6 4 GLY B 215 ARG B 220 -1 O PHE B 217 N SER B 208
SHEET 3 AB6 4 MET B 238 ARG B 243 -1 O MET B 238 N ARG B 220
SHEET 4 AB6 4 VAL B 252 HIS B 255 -1 O VAL B 254 N VAL B 239
SHEET 1 AB7 4 ILE B 264 LEU B 269 0
SHEET 2 AB7 4 TYR B 275 SER B 281 -1 O LEU B 277 N GLN B 268
SHEET 3 AB7 4 LEU B 289 ASP B 294 -1 O LYS B 291 N PHE B 278
SHEET 4 AB7 4 LYS B 307 ASN B 308 -1 O LYS B 307 N ILE B 292
SHEET 1 AB8 4 PHE B 317 GLU B 323 0
SHEET 2 AB8 4 LYS B 326 THR B 331 -1 O TYR B 328 N VAL B 320
SHEET 3 AB8 4 LYS B 339 ASP B 344 -1 O PHE B 343 N ILE B 327
SHEET 4 AB8 4 LEU B 352 ILE B 356 -1 O THR B 353 N THR B 342
SHEET 1 AB9 4 PHE B 363 HIS B 370 0
SHEET 2 AB9 4 LYS B 374 ARG B 381 -1 O LEU B 376 N SER B 368
SHEET 3 AB9 4 SER B 384 ASP B 391 -1 O ARG B 390 N LEU B 375
SHEET 4 AB9 4 PRO B 397 ILE B 401 -1 O GLY B 399 N ILE B 389
SHEET 1 AC1 4 GLN B 408 SER B 412 0
SHEET 2 AC1 4 ASP B 419 SER B 425 -1 O SER B 425 N GLN B 408
SHEET 3 AC1 4 THR B 432 THR B 437 -1 O THR B 432 N PHE B 424
SHEET 4 AC1 4 TYR B 444 ALA B 450 -1 O ARG B 449 N VAL B 433
SHEET 1 AC2 8 PHE B 461 PRO B 469 0
SHEET 2 AC2 8 SER B 475 PRO B 483 -1 O MET B 478 N VAL B 466
SHEET 3 AC2 8 ILE B 524 PRO B 528 -1 O TYR B 525 N THR B 481
SHEET 4 AC2 8 VAL B 494 TYR B 497 1 N LEU B 495 O ILE B 524
SHEET 5 AC2 8 ILE B 574 GLY B 579 1 O ALA B 575 N GLN B 496
SHEET 6 AC2 8 CYS B 599 ILE B 603 1 O ILE B 601 N ILE B 576
SHEET 7 AC2 8 ALA B 656 ALA B 662 1 O PHE B 660 N THR B 602
SHEET 8 AC2 8 CYS B 691 ASP B 696 1 O ARG B 694 N PHE B 659
SHEET 1 AC3 2 ALA C 19 SER C 24 0
SHEET 2 AC3 2 GLY C 28 ARG C 33 -1 O VAL C 32 N ILE C 20
SHEET 1 AC4 3 ARG C 85 PHE C 86 0
SHEET 2 AC4 3 HIS C 96 ASN C 102 -1 O ASN C 102 N ARG C 85
SHEET 3 AC4 3 LYS C 90 PRO C 91 -1 N LYS C 90 O TYR C 98
SHEET 1 AC5 4 ARG C 85 PHE C 86 0
SHEET 2 AC5 4 HIS C 96 ASN C 102 -1 O ASN C 102 N ARG C 85
SHEET 3 AC5 4 SER C 110 ARG C 115 -1 O SER C 110 N TYR C 101
SHEET 4 AC5 4 GLU C 131 PHE C 134 -1 O GLU C 131 N ARG C 113
SHEET 1 AC6 4 ALA C 146 MET C 152 0
SHEET 2 AC6 4 TYR C 158 SER C 164 -1 O GLY C 162 N THR C 148
SHEET 3 AC6 4 MET C 171 LYS C 177 -1 O TYR C 174 N TYR C 161
SHEET 4 AC6 4 LYS C 198 VAL C 202 -1 O VAL C 202 N MET C 171
SHEET 1 AC7 4 SER C 208 TRP C 209 0
SHEET 2 AC7 4 GLY C 215 ARG C 220 -1 O PHE C 217 N SER C 208
SHEET 3 AC7 4 MET C 238 ARG C 243 -1 O MET C 238 N ARG C 220
SHEET 4 AC7 4 VAL C 252 HIS C 255 -1 O VAL C 254 N VAL C 239
SHEET 1 AC8 4 ILE C 264 LEU C 269 0
SHEET 2 AC8 4 TYR C 275 SER C 281 -1 O LEU C 277 N GLN C 268
SHEET 3 AC8 4 LEU C 289 ASP C 294 -1 O LYS C 291 N PHE C 278
SHEET 4 AC8 4 TRP C 306 ASN C 308 -1 O LYS C 307 N ILE C 292
SHEET 1 AC9 4 PHE C 317 GLU C 323 0
SHEET 2 AC9 4 LYS C 326 THR C 331 -1 O TYR C 328 N VAL C 320
SHEET 3 AC9 4 LYS C 339 ASP C 344 -1 O PHE C 343 N ILE C 327
SHEET 4 AC9 4 LEU C 352 ILE C 356 -1 O THR C 353 N THR C 342
SHEET 1 AD1 4 PHE C 363 HIS C 370 0
SHEET 2 AD1 4 LYS C 374 ARG C 381 -1 O LEU C 376 N SER C 368
SHEET 3 AD1 4 SER C 384 ASP C 391 -1 O ARG C 390 N LEU C 375
SHEET 4 AD1 4 PRO C 397 ILE C 401 -1 O GLY C 399 N ILE C 389
SHEET 1 AD2 4 GLN C 408 SER C 412 0
SHEET 2 AD2 4 ASP C 419 SER C 425 -1 O LEU C 423 N MET C 410
SHEET 3 AD2 4 THR C 432 THR C 437 -1 O THR C 432 N PHE C 424
SHEET 4 AD2 4 TYR C 444 ALA C 450 -1 O ARG C 449 N VAL C 433
SHEET 1 AD3 8 PHE C 461 PRO C 469 0
SHEET 2 AD3 8 SER C 475 PRO C 483 -1 O MET C 478 N VAL C 466
SHEET 3 AD3 8 ILE C 524 PRO C 528 -1 O TYR C 525 N THR C 481
SHEET 4 AD3 8 VAL C 494 TYR C 497 1 N LEU C 495 O ILE C 524
SHEET 5 AD3 8 ILE C 574 GLY C 579 1 O ALA C 575 N GLN C 496
SHEET 6 AD3 8 CYS C 599 ILE C 603 1 O ILE C 601 N ILE C 576
SHEET 7 AD3 8 ALA C 656 ALA C 662 1 O PHE C 660 N THR C 602
SHEET 8 AD3 8 CYS C 691 ASP C 696 1 O ARG C 694 N PHE C 659
SHEET 1 AD4 2 ALA D 19 SER D 24 0
SHEET 2 AD4 2 GLY D 28 ARG D 33 -1 O VAL D 32 N ILE D 20
SHEET 1 AD5 3 ARG D 85 PHE D 86 0
SHEET 2 AD5 3 HIS D 96 ASN D 102 -1 O ASN D 102 N ARG D 85
SHEET 3 AD5 3 LYS D 90 PRO D 91 -1 N LYS D 90 O TYR D 98
SHEET 1 AD6 4 ARG D 85 PHE D 86 0
SHEET 2 AD6 4 HIS D 96 ASN D 102 -1 O ASN D 102 N ARG D 85
SHEET 3 AD6 4 SER D 110 ARG D 115 -1 O SER D 110 N TYR D 101
SHEET 4 AD6 4 GLU D 131 PHE D 134 -1 O GLU D 131 N ARG D 113
SHEET 1 AD7 4 ALA D 146 MET D 152 0
SHEET 2 AD7 4 TYR D 158 SER D 164 -1 O GLY D 162 N THR D 148
SHEET 3 AD7 4 MET D 171 LYS D 177 -1 O TYR D 174 N TYR D 161
SHEET 4 AD7 4 ILE D 199 VAL D 202 -1 O VAL D 202 N MET D 171
SHEET 1 AD8 4 SER D 208 TRP D 209 0
SHEET 2 AD8 4 GLY D 215 ARG D 220 -1 O PHE D 217 N SER D 208
SHEET 3 AD8 4 MET D 238 ARG D 243 -1 O HIS D 242 N PHE D 216
SHEET 4 AD8 4 VAL D 252 HIS D 255 -1 O VAL D 254 N VAL D 239
SHEET 1 AD9 4 ILE D 264 LEU D 269 0
SHEET 2 AD9 4 TYR D 275 SER D 281 -1 O LEU D 277 N GLN D 268
SHEET 3 AD9 4 LEU D 289 ASP D 294 -1 O LYS D 291 N PHE D 278
SHEET 4 AD9 4 TRP D 306 ASN D 308 -1 O LYS D 307 N ILE D 292
SHEET 1 AE1 4 PHE D 317 GLU D 323 0
SHEET 2 AE1 4 LYS D 326 THR D 331 -1 O TYR D 328 N VAL D 320
SHEET 3 AE1 4 LYS D 339 ASP D 344 -1 O PHE D 343 N ILE D 327
SHEET 4 AE1 4 LEU D 352 ILE D 356 -1 O THR D 353 N THR D 342
SHEET 1 AE2 4 PHE D 363 HIS D 370 0
SHEET 2 AE2 4 LYS D 374 ARG D 381 -1 O LEU D 376 N SER D 368
SHEET 3 AE2 4 SER D 384 ASP D 391 -1 O ARG D 390 N LEU D 375
SHEET 4 AE2 4 PRO D 397 ILE D 401 -1 O GLY D 399 N ILE D 389
SHEET 1 AE3 4 GLN D 408 SER D 412 0
SHEET 2 AE3 4 ASP D 419 SER D 425 -1 O LEU D 423 N MET D 410
SHEET 3 AE3 4 THR D 432 THR D 437 -1 O THR D 432 N PHE D 424
SHEET 4 AE3 4 TYR D 444 ALA D 450 -1 O ARG D 449 N VAL D 433
SHEET 1 AE4 8 PHE D 461 PRO D 469 0
SHEET 2 AE4 8 SER D 475 PRO D 483 -1 O MET D 478 N VAL D 466
SHEET 3 AE4 8 ILE D 524 PRO D 528 -1 O TYR D 525 N THR D 481
SHEET 4 AE4 8 VAL D 494 TYR D 497 1 N LEU D 495 O ILE D 524
SHEET 5 AE4 8 ILE D 574 GLY D 579 1 O ALA D 575 N GLN D 496
SHEET 6 AE4 8 CYS D 599 ILE D 603 1 O ILE D 601 N ILE D 576
SHEET 7 AE4 8 ALA D 656 ALA D 662 1 O PHE D 660 N THR D 602
SHEET 8 AE4 8 CYS D 691 ASP D 696 1 O ARG D 694 N PHE D 659
LINK C IML E 802 N SAR E 803 1555 1555 1.36
LINK C SAR E 803 N VAL E 804 1555 1555 1.34
LINK C VAL E 804 N IML E 805 1555 1555 1.35
LINK C IML E 805 N SAR E 806 1555 1555 1.35
LINK C SAR E 806 N SER E 807 1555 1555 1.34
LINK C SER E 807 N MVA E 808 1555 1555 1.38
LINK C IML F 802 N SAR F 803 1555 1555 1.36
LINK C SAR F 803 N VAL F 804 1555 1555 1.33
LINK C VAL F 804 N IML F 805 1555 1555 1.36
LINK C IML F 805 N SAR F 806 1555 1555 1.35
LINK C SAR F 806 N SER F 807 1555 1555 1.34
LINK C SER F 807 N MVA F 808 1555 1555 1.37
LINK C IML G 802 N SAR G 803 1555 1555 1.36
LINK C SAR G 803 N VAL G 804 1555 1555 1.34
LINK C VAL G 804 N IML G 805 1555 1555 1.35
LINK C IML G 805 N SAR G 806 1555 1555 1.36
LINK C SAR G 806 N SER G 807 1555 1555 1.34
LINK C SER G 807 N MVA G 808 1555 1555 1.37
LINK C SAR H 803 N VAL H 804 1555 1555 1.34
LINK C VAL H 804 N IML H 805 1555 1555 1.36
LINK C IML H 805 N SAR H 806 1555 1555 1.36
LINK C SAR H 806 N SER H 807 1555 1555 1.34
LINK C SER H 807 N MVA H 808 1555 1555 1.37
LINK O GLN A 56 NA NA A 804 1555 1555 2.52
LINK OE1 GLN A 56 NA NA A 804 1555 1555 2.89
LINK OG SER A 219 NA NA A 805 1555 1555 2.93
LINK OG SER A 470 NA NA A 806 1555 1555 3.08
LINK O LEU A 504 NA NA A 802 1555 1555 2.47
LINK O THR A 509 NA NA A 807 1555 1555 2.73
LINK O VAL A 600 NA NA A 803 1555 1555 2.85
LINK OG1 THR A 602 NA NA A 803 1555 1555 2.76
LINK O LEU A 658 NA NA A 803 1555 1555 3.17
LINK NA NA A 802 O HOH A 967 1555 1555 2.50
LINK NA NA A 806 O HOH A 926 1555 1555 2.30
LINK NA NA A 807 O HOH A 958 1555 1555 2.80
LINK O PHE B 262 NA NA B 803 1555 1555 2.90
LINK O ASN B 337 NA NA B 804 1555 1555 2.73
LINK O TYR B 338 NA NA B 804 1555 1555 2.75
LINK O ALA B 362 NA NA B 804 1555 1555 2.89
LINK O TYR B 499 NA NA B 802 1555 1555 2.78
LINK O GLY B 544 NA NA B 801 1555 1555 2.42
LINK O ASN B 581 NA NA B 802 1555 1555 2.79
LINK OE1 GLU B 624 NA NA B 801 1555 1555 2.60
LINK NA NA B 803 O HOH B 931 1555 1555 2.84
LINK NA NA B 803 O HOH B1005 1555 1555 2.76
LINK NA NA B 804 O HOH B 912 1555 1555 2.92
LINK O GLY C 544 NA NA C 807 1555 1555 2.51
LINK O VAL C 600 NA NA C 806 1555 1555 2.73
LINK OG1 THR C 602 NA NA C 806 1555 1555 2.89
LINK OE1 GLU C 624 NA NA C 807 1555 1555 2.58
LINK O LEU C 658 NA NA C 806 1555 1555 3.20
LINK O PHE C 660 NA NA C 805 1555 1555 2.87
LINK OG1 THR C 673 NA NA C 805 1555 1555 2.54
LINK OG SER D 281 NA NA D 807 1555 1555 2.87
LINK O ASP D 283 NA NA D 807 1555 1555 2.68
LINK O ILE D 401 NA NA D 806 1555 1555 2.67
LINK O PHE D 402 NA NA D 806 1555 1555 2.97
LINK O THR D 587 NA NA D 805 1555 1555 3.13
LINK OD1 ASN D 591 NA NA D 805 1555 1555 2.98
LINK NA NA D 806 O HOH D 937 1555 1555 2.75
CISPEP 1 GLY A 7 PRO A 8 0 -3.91
CISPEP 2 GLY A 687 PRO A 688 0 3.01
CISPEP 3 GLY B 7 PRO B 8 0 -4.14
CISPEP 4 GLY B 687 PRO B 688 0 7.55
CISPEP 5 GLY C 7 PRO C 8 0 -5.34
CISPEP 6 GLY C 687 PRO C 688 0 6.74
CISPEP 7 GLY D 7 PRO D 8 0 -4.50
CISPEP 8 GLY D 687 PRO D 688 0 7.75
CRYST1 70.010 104.610 110.650 115.81 98.87 93.79 P 1 4
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 0.014284 0.000946 0.002978 0.00000
SCALE2 0.000000 0.009580 0.004854 0.00000
SCALE3 0.000000 0.000000 0.010254 0.00000
TER 5772 THR A 731
TER 11586 THR B 731
TER 17381 GLN C 730
TER 23208 THR D 731
TER 23258 MVA E 808
TER 23308 MVA F 808
TER 23358 MVA G 808
TER 23399 MVA H 808
MASTER 1089 0 44 92 164 0 0 624063 8 242 240
END |