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HEADER HYDROLASE 23-MAY-13 4BP9
TITLE OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI WITH COVALENTLY
TITLE 2 BOUND ANTIPAIN - CLOSED FORM
CAVEAT 4BP9 OAR G 4 CA HAS THE WRONG CHIRALITY
CAVEAT 2 4BP9 OAR H 4 CA HAS THE WRONG CHIRALITY
CAVEAT 3 4BP9 OAR I 4 CA HAS THE WRONG CHIRALITY
CAVEAT 4 4BP9 OAR J 4 CA HAS THE WRONG CHIRALITY
CAVEAT 5 4BP9 OAR K 4 CA HAS THE WRONG CHIRALITY
CAVEAT 6 4BP9 OAR L 4 CA HAS THE WRONG CHIRALITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGOPEPTIDASSE B;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.4.21.83;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ANTIPAIN;
COMPND 8 CHAIN: G, H, I, J, K, L
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PRARE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ACTINOBACTERIA;
SOURCE 11 ORGANISM_TAXID: 1760
KEYWDS HYDROLASE, PROLYL OLIGOPEPTIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CANNING,D.REA,R.MORTY,V.FULOP
REVDAT 1 12-FEB-14 4BP9 0
JRNL AUTH P.CANNING,D.REA,R.E.MORTY,V.FULOP
JRNL TITL CRYSTAL STRUCTURES OF TRYPANOSOMA BRUCEI OLIGOPEPTIDASE B
JRNL TITL 2 BROADEN THE PARADIGM OF CATALYTIC REGULATION IN PROLYL
JRNL TITL 3 OLIGOPEPTIDASE FAMILY ENZYMES.
JRNL REF PLOS ONE V. 8E79349 2013
JRNL REFN ISSN 1932-6203
JRNL PMID 24265767
JRNL DOI 10.1371/JOURNAL.PONE.0079349
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.75
REMARK 3 NUMBER OF REFLECTIONS : 121891
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) : 0.21609
REMARK 3 R VALUE (WORKING SET) : 0.21333
REMARK 3 FREE R VALUE : 0.28074
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.1
REMARK 3 FREE R VALUE TEST SET COUNT : 5162
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) : 2.850
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.924
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8894
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.292
REMARK 3 BIN FREE R VALUE SET COUNT : 379
REMARK 3 BIN FREE R VALUE : 0.365
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 33804
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 258
REMARK 3 SOLVENT ATOMS : 344
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.400
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.97
REMARK 3 B22 (A**2) : 1.49
REMARK 3 B33 (A**2) : 0.51
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.69
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.436
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.381
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.636
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 34896 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 47322 ; 1.697 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4254 ; 8.110 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1614 ;35.788 ;23.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5814 ;20.883 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 276 ;20.513 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5136 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26730 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 21210 ; 0.392 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34344 ; 0.774 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13686 ; 1.381 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12978 ; 2.302 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
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 5 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5900 121.8250 223.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.4167 T22: 0.6717
REMARK 3 T33: 0.3381 T12: 0.1220
REMARK 3 T13: 0.1576 T23: 0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 1.6990 L22: 2.1497
REMARK 3 L33: 2.5552 L12: 0.6199
REMARK 3 L13: -0.2926 L23: -0.7631
REMARK 3 S TENSOR
REMARK 3 S11: 0.1958 S12: 0.1253 S13: 0.4175
REMARK 3 S21: 0.3655 S22: 0.1841 S23: 0.5994
REMARK 3 S31: -0.5691 S32: -0.5266 S33: -0.3799
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 87 A 441
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7330 106.1900 248.7460
REMARK 3 T TENSOR
REMARK 3 T11: 0.4345 T22: 0.5750
REMARK 3 T33: 0.1617 T12: 0.0175
REMARK 3 T13: 0.0165 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 0.7974 L22: 0.9615
REMARK 3 L33: 1.3416 L12: 0.0510
REMARK 3 L13: 0.0312 L23: -0.1461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: -0.1981 S13: 0.0613
REMARK 3 S21: 0.2644 S22: 0.0492 S23: 0.0167
REMARK 3 S31: 0.0564 S32: 0.1057 S33: -0.0728
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 442 A 714
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6600 109.6620 220.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.3974 T22: 0.5619
REMARK 3 T33: 0.2233 T12: -0.0135
REMARK 3 T13: 0.0302 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.6979 L22: 1.3464
REMARK 3 L33: 1.2312 L12: 0.2719
REMARK 3 L13: -0.1035 L23: -0.0608
REMARK 3 S TENSOR
REMARK 3 S11: 0.0431 S12: 0.0166 S13: 0.0967
REMARK 3 S21: 0.1000 S22: 0.0223 S23: 0.0333
REMARK 3 S31: 0.1256 S32: -0.0731 S33: -0.0654
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 : B 5 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3490 140.4630 194.0850
REMARK 3 T TENSOR
REMARK 3 T11: 0.5018 T22: 0.5705
REMARK 3 T33: 0.1958 T12: 0.0926
REMARK 3 T13: 0.0635 T23: 0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 1.7073 L22: 2.2222
REMARK 3 L33: 1.7304 L12: 0.8004
REMARK 3 L13: -0.1787 L23: -0.3574
REMARK 3 S TENSOR
REMARK 3 S11: 0.1091 S12: 0.1983 S13: 0.2519
REMARK 3 S21: -0.0253 S22: -0.0500 S23: 0.3722
REMARK 3 S31: -0.5191 S32: -0.2990 S33: -0.0591
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 441
REMARK 3 ORIGIN FOR THE GROUP (A): 60.2030 124.7900 182.9270
REMARK 3 T TENSOR
REMARK 3 T11: 0.2849 T22: 0.9500
REMARK 3 T33: 0.1952 T12: -0.0171
REMARK 3 T13: 0.0462 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.6099 L22: 0.6688
REMARK 3 L33: 2.0683 L12: 0.1180
REMARK 3 L13: -0.1344 L23: 0.0305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0452 S12: 0.1562 S13: -0.0498
REMARK 3 S21: -0.0502 S22: -0.0286 S23: -0.0325
REMARK 3 S31: 0.0113 S32: 0.7632 S33: -0.0166
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 442 B 714
REMARK 3 ORIGIN FOR THE GROUP (A): 43.7200 136.6320 204.7970
REMARK 3 T TENSOR
REMARK 3 T11: 0.5128 T22: 0.6435
REMARK 3 T33: 0.2551 T12: -0.0916
REMARK 3 T13: 0.0492 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.9062 L22: 0.6838
REMARK 3 L33: 1.5649 L12: 0.3395
REMARK 3 L13: 0.0004 L23: -0.0698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.0404 S13: 0.0281
REMARK 3 S21: 0.0167 S22: 0.0346 S23: 0.0325
REMARK 3 S31: -0.4014 S32: 0.2819 S33: -0.0665
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 : C 5 C 86
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7850 42.3530 216.1690
REMARK 3 T TENSOR
REMARK 3 T11: 0.7079 T22: 0.7692
REMARK 3 T33: 0.3170 T12: -0.0160
REMARK 3 T13: 0.1993 T23: -0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 2.9413 L22: 0.9072
REMARK 3 L33: 3.3626 L12: 0.4730
REMARK 3 L13: 1.5078 L23: 0.1774
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: 0.0353 S13: -0.5749
REMARK 3 S21: -0.1498 S22: -0.2024 S23: -0.1314
REMARK 3 S31: 0.7459 S32: -0.4066 S33: 0.1321
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 87 C 441
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3880 72.6490 198.3050
REMARK 3 T TENSOR
REMARK 3 T11: 0.8187 T22: 0.8194
REMARK 3 T33: 0.2041 T12: 0.2483
REMARK 3 T13: 0.0521 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.9881 L22: 0.6715
REMARK 3 L33: 1.8239 L12: 0.2944
REMARK 3 L13: -0.3279 L23: -0.1156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: 0.3042 S13: 0.0102
REMARK 3 S21: -0.1385 S22: -0.0436 S23: 0.0142
REMARK 3 S31: -0.4683 S32: -0.5338 S33: 0.0241
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 : C 442 C 714
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1420 57.7610 221.1940
REMARK 3 T TENSOR
REMARK 3 T11: 0.6350 T22: 0.9659
REMARK 3 T33: 0.2986 T12: 0.1006
REMARK 3 T13: 0.0615 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 0.8321 L22: 0.5125
REMARK 3 L33: 1.7825 L12: 0.1390
REMARK 3 L13: -0.3256 L23: 0.2134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0449 S12: 0.2659 S13: -0.0686
REMARK 3 S21: -0.1575 S22: -0.1292 S23: -0.0214
REMARK 3 S31: -0.0504 S32: -0.6442 S33: 0.0843
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 : D 5 D 86
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6170 42.5170 255.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.6980 T22: 0.6300
REMARK 3 T33: 0.2937 T12: 0.1245
REMARK 3 T13: 0.2327 T23: 0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 3.6422 L22: 1.1404
REMARK 3 L33: 3.2490 L12: 0.4076
REMARK 3 L13: 1.2411 L23: 0.1890
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.1410 S13: -0.4821
REMARK 3 S21: 0.1323 S22: -0.2149 S23: 0.1114
REMARK 3 S31: 0.9723 S32: 0.0914 S33: 0.2078
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 : D 87 D 441
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0250 72.8510 272.8470
REMARK 3 T TENSOR
REMARK 3 T11: 0.5627 T22: 0.6474
REMARK 3 T33: 0.1901 T12: -0.0724
REMARK 3 T13: 0.0417 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.9444 L22: 0.9860
REMARK 3 L33: 1.8714 L12: -0.0542
REMARK 3 L13: -0.3010 L23: -0.1905
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: -0.2001 S13: 0.0299
REMARK 3 S21: 0.1758 S22: -0.0754 S23: 0.0910
REMARK 3 S31: -0.3145 S32: 0.2250 S33: 0.0485
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 442 D 714
REMARK 3 ORIGIN FOR THE GROUP (A): 72.2920 57.8150 250.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.5541 T22: 0.7766
REMARK 3 T33: 0.3074 T12: 0.0411
REMARK 3 T13: 0.1055 T23: 0.1021
REMARK 3 L TENSOR
REMARK 3 L11: 0.6143 L22: 0.5319
REMARK 3 L33: 2.1111 L12: 0.1707
REMARK 3 L13: -0.5368 L23: 0.0843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: -0.0999 S13: -0.0787
REMARK 3 S21: 0.0000 S22: -0.1351 S23: 0.0047
REMARK 3 S31: 0.0555 S32: 0.3940 S33: 0.1272
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 : E 5 E 86
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0760 47.4680 159.1150
REMARK 3 T TENSOR
REMARK 3 T11: 0.3635 T22: 1.2215
REMARK 3 T33: 0.2785 T12: 0.1284
REMARK 3 T13: 0.0073 T23: 0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 1.2776 L22: 0.9642
REMARK 3 L33: 6.0542 L12: 0.0100
REMARK 3 L13: -1.2905 L23: -0.2890
REMARK 3 S TENSOR
REMARK 3 S11: 0.1614 S12: 0.1644 S13: 0.0061
REMARK 3 S21: 0.1345 S22: 0.0118 S23: 0.3237
REMARK 3 S31: -0.5452 S32: -1.9389 S33: -0.1732
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 : E 87 E 441
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4720 31.2900 183.9780
REMARK 3 T TENSOR
REMARK 3 T11: 0.7986 T22: 0.6169
REMARK 3 T33: 0.2453 T12: 0.1113
REMARK 3 T13: 0.0987 T23: 0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 1.1442 L22: 0.6682
REMARK 3 L33: 4.7127 L12: -0.0342
REMARK 3 L13: -1.0401 L23: -0.0614
REMARK 3 S TENSOR
REMARK 3 S11: -0.2468 S12: -0.3082 S13: -0.1246
REMARK 3 S21: 0.2348 S22: 0.0687 S23: -0.0271
REMARK 3 S31: 1.0113 S32: 0.4200 S33: 0.1781
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 : E 442 E 714
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8330 35.1570 155.3530
REMARK 3 T TENSOR
REMARK 3 T11: 0.6198 T22: 0.6742
REMARK 3 T33: 0.2601 T12: -0.1532
REMARK 3 T13: 0.1086 T23: -0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 1.0216 L22: 0.6808
REMARK 3 L33: 5.1965 L12: 0.1705
REMARK 3 L13: -1.1195 L23: -0.2129
REMARK 3 S TENSOR
REMARK 3 S11: -0.2581 S12: 0.1592 S13: -0.0979
REMARK 3 S21: 0.0656 S22: 0.0642 S23: 0.0201
REMARK 3 S31: 0.8737 S32: -0.6651 S33: 0.1939
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 : F 5 F 86
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4370 65.9230 129.6430
REMARK 3 T TENSOR
REMARK 3 T11: 0.8811 T22: 0.6564
REMARK 3 T33: 0.2072 T12: 0.1066
REMARK 3 T13: 0.0490 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 2.1089 L22: 2.5497
REMARK 3 L33: 4.8052 L12: 0.1485
REMARK 3 L13: -0.7594 L23: -0.0812
REMARK 3 S TENSOR
REMARK 3 S11: 0.1890 S12: 0.4240 S13: 0.2735
REMARK 3 S21: -0.0147 S22: -0.0471 S23: 0.2624
REMARK 3 S31: -1.5659 S32: -0.5421 S33: -0.1419
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 : F 87 F 441
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9830 49.4520 118.5030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2921 T22: 1.4549
REMARK 3 T33: 0.2573 T12: -0.1609
REMARK 3 T13: 0.0550 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 0.5034 L22: 0.8560
REMARK 3 L33: 4.5782 L12: -0.0053
REMARK 3 L13: -0.2308 L23: -0.1363
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: -0.0150 S13: -0.0005
REMARK 3 S21: -0.0182 S22: 0.0026 S23: -0.0323
REMARK 3 S31: -0.1926 S32: 1.8657 S33: 0.0046
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 : F 442 F 714
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6280 61.7550 140.3490
REMARK 3 T TENSOR
REMARK 3 T11: 0.7467 T22: 0.7807
REMARK 3 T33: 0.2763 T12: -0.2802
REMARK 3 T13: 0.0675 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 0.8171 L22: 0.6648
REMARK 3 L33: 4.4124 L12: 0.0084
REMARK 3 L13: -0.4684 L23: -0.2158
REMARK 3 S TENSOR
REMARK 3 S11: 0.1334 S12: -0.0515 S13: 0.0705
REMARK 3 S21: 0.0852 S22: 0.0178 S23: -0.0570
REMARK 3 S31: -1.1722 S32: 0.8420 S33: -0.1512
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4BP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAY-13.
REMARK 100 THE PDBE ID CODE IS EBI-56998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
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 : 127053
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.85
REMARK 200 RESOLUTION RANGE LOW (A) : 59.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.5
REMARK 200 R MERGE (I) : 0.22
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.6
REMARK 200 R MERGE FOR SHELL (I) : 1.12
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.20
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: NULL
REMARK 200
REMARK 200 REMARK: STARTING MODEL IS ALSO BEING CURRENTLY DEPOSITED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 4000, 0.2 M CALCIUM
REMARK 280 ACETATE, 0.1 M SODIUM ACETATE PH 5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 74.40000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 ANTIPAIN HYDROCHLORIDE IS A REVERSIBLE INHIBITOR OF SERINE/CYSTEINE
REMARK 400 PROTEASES AND SOME TRYPSIN-LIKE SERINE PROTEASES. ITS ACTION
REMARK 400 RESEMBLES LEUPEPTIN; HOWEVER, ITS PLASMIN INHIBITION IS LESS AND
REMARK 400 ITS CATHEPSIN A INHIBITION IS MORE THAN THAT OBSERVED WITH
REMARK 400 LEUPEPTIN. IT IS AN INHIBITOR OF TRYPSIN-LIKE PROTEASES
REMARK 400 (E.G. TRYPSIN, PAPAIN, CATHEPSIN B); CATHEPSIN A, A CARBOXYPEPTIDASE,
REMARK 400 IS INHIBITED TOO, WHICH IS NOT TRUE FOR OTHER INHIBITORS FROM
REMARK 400 ACTINOMYCES.THE NAME IS DERIVED FROM ANTI-PAPAIN.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ANTIPAIN
REMARK 400 CHAIN: G, H, I, J, K, L
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 4
REMARK 400 DESCRIPTION: ANTIPAIN FORMS A COVALENT LINKAGE BETWEEN THE ARGINAL
REMARK 400 RESIDUE OF THE INHIBITOR AND SER RESIDUE OF THE
REMARK 400 PROTEIN.THE PROTEASE INHIBITOR ANTIPAIN INCREASES THE
REMARK 400 EFFECTIVENESSOF UV IRRADIATION ON CESSATION OF
REMARK 400 RESPIRATION AND CELL KILLING IN ESCHERICHIA COLI B/R
REMARK 400 CULTURES WITHOUT AFFECTING EXCISION OF PYRIMIDINE
REMARK 400 DIMERS. THE ACTIONS ARE SIMILAR TO THOSE CAUSED BY
REMARK 400 CYCLIC AMP IN IRRADIATED CULTURES.
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 GLN A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 LYS A 715
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 GLU B 4
REMARK 465 LYS B 715
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 THR C 3
REMARK 465 GLU C 4
REMARK 465 LYS C 715
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 THR D 3
REMARK 465 GLU D 4
REMARK 465 LYS D 715
REMARK 465 MET E 1
REMARK 465 GLN E 2
REMARK 465 THR E 3
REMARK 465 GLU E 4
REMARK 465 LYS E 715
REMARK 465 MET F 1
REMARK 465 GLN F 2
REMARK 465 THR F 3
REMARK 465 GLU F 4
REMARK 465 LYS F 715
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 OG SER A 563 OH1 OAR G 4 2.07
REMARK 500 O HIS B 381 NH2 ARG B 427 2.15
REMARK 500 OG1 THR B 477 OG1 THR B 552 2.16
REMARK 500 ND2 ASN C 312 OG1 THR C 338 2.15
REMARK 500 O GLY C 367 N ASP C 369 2.13
REMARK 500 OD1 ASP C 466 OG SER C 468 2.20
REMARK 500 OG SER C 563 OH1 OAR I 4 2.06
REMARK 500 OD1 ASP D 455 OG1 THR D 457 2.11
REMARK 500 OG SER D 563 OH1 OAR J 4 2.11
REMARK 500 OH TYR E 444 OD1 ASP E 502 2.06
REMARK 500 OG SER F 563 OH1 OAR L 4 2.16
REMARK 500 NH2 ARG F 664 O VAL F 673 2.14
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 FC0 G 1 C ARG G 2 N 2.320
REMARK 500 FC0 K 1 C ARG K 2 N 2.887
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 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO A 157 C - N - CD ANGL. DEV. = -17.3 DEGREES
REMARK 500 VAL A 350 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 GLY A 483 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 TYR A 482 CA - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 496 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 664 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 PRO B 157 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO B 157 C - N - CD ANGL. DEV. = -18.5 DEGREES
REMARK 500 LEU B 463 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 GLY B 483 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 ARG B 533 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 PRO C 157 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO C 157 C - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO D 156 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO D 157 C - N - CD ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO E 157 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 LEU E 279 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 FC0 G 1 CA - C - N ANGL. DEV. = -58.5 DEGREES
REMARK 500 ARG G 2 C - N - CA ANGL. DEV. = -16.1 DEGREES
REMARK 500 FC0 K 1 CA - C - N ANGL. DEV. = -72.6 DEGREES
REMARK 500 FC0 K 1 O - C - N ANGL. DEV. = 29.1 DEGREES
REMARK 500 ARG K 2 C - N - CA ANGL. DEV. = -26.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 32 112.98 -160.89
REMARK 500 GLU A 88 89.02 60.71
REMARK 500 ASP A 99 -129.36 60.90
REMARK 500 ALA A 121 -57.64 -27.72
REMARK 500 GLU A 142 101.87 -27.60
REMARK 500 PRO A 156 162.68 -26.97
REMARK 500 PRO A 157 -74.67 29.46
REMARK 500 ARG A 180 26.25 38.32
REMARK 500 ASN A 199 39.26 37.94
REMARK 500 LYS A 208 -165.38 -67.25
REMARK 500 ALA A 210 126.45 -37.14
REMARK 500 MET A 281 140.22 -38.27
REMARK 500 VAL A 282 -76.17 -100.86
REMARK 500 PHE A 348 178.26 177.18
REMARK 500 PRO A 368 -32.80 -38.50
REMARK 500 SER A 394 8.46 -66.86
REMARK 500 MET A 411 -9.00 -50.75
REMARK 500 THR A 467 -10.40 -48.05
REMARK 500 TYR A 482 -91.72 -107.00
REMARK 500 TYR A 485 -14.94 63.44
REMARK 500 HIS A 511 59.36 -93.69
REMARK 500 TYR A 529 -136.05 44.47
REMARK 500 LEU A 530 22.77 -74.12
REMARK 500 SER A 563 -122.95 61.27
REMARK 500 VAL A 587 56.74 30.30
REMARK 500 ASP A 591 62.18 -102.00
REMARK 500 GLU A 610 -70.23 -125.56
REMARK 500 PHE A 620 -74.01 -37.44
REMARK 500 ALA A 634 96.84 -63.11
REMARK 500 HIS A 647 34.05 -97.82
REMARK 500 SER A 685 -91.55 -59.83
REMARK 500 ALA A 686 -69.42 65.62
REMARK 500 SER A 687 -174.41 -170.70
REMARK 500 ARG A 689 -150.04 -134.92
REMARK 500 ASN A 708 47.73 75.38
REMARK 500 ASN B 29 58.07 -153.34
REMARK 500 GLU B 88 87.23 56.32
REMARK 500 SER B 93 179.22 -52.68
REMARK 500 ASP B 99 -127.54 42.38
REMARK 500 ALA B 121 90.29 -59.18
REMARK 500 GLU B 142 96.10 -27.81
REMARK 500 CYS B 147 100.38 -160.06
REMARK 500 PRO B 156 180.00 -54.85
REMARK 500 PRO B 157 -75.21 29.55
REMARK 500 ASN B 199 55.26 27.68
REMARK 500 ASP B 214 96.23 -66.14
REMARK 500 ILE B 222 132.67 -39.56
REMARK 500 VAL B 274 -20.01 -33.66
REMARK 500 VAL B 282 -74.63 -95.28
REMARK 500 ASP B 308 32.17 72.67
REMARK 500
REMARK 500 THIS ENTRY HAS 265 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 PRO A 156 PRO A 157 -129.12
REMARK 500 SER A 685 ALA A 686 -137.48
REMARK 500 PRO B 156 PRO B 157 -129.96
REMARK 500 TYR B 482 GLY B 483 -48.31
REMARK 500 SER B 685 ALA B 686 -135.86
REMARK 500 ASP B 688 ARG B 689 -147.02
REMARK 500 PRO C 156 PRO C 157 -126.69
REMARK 500 TYR C 482 GLY C 483 -30.80
REMARK 500 SER C 685 ALA C 686 -145.30
REMARK 500 PRO D 156 PRO D 157 -122.91
REMARK 500 TYR D 482 GLY D 483 -39.14
REMARK 500 PHE D 684 SER D 685 -148.12
REMARK 500 SER D 685 ALA D 686 -142.45
REMARK 500 PRO E 156 PRO E 157 -126.69
REMARK 500 SER E 685 ALA E 686 -134.11
REMARK 500 PRO F 156 PRO F 157 -132.58
REMARK 500 SER F 685 ALA F 686 -131.61
REMARK 500 FC0 G 1 ARG G 2 97.53
REMARK 500 ARG G 2 VAL G 3 -132.88
REMARK 500 FC0 K 1 ARG K 2 105.67
REMARK 500 ARG L 2 VAL L 3 -146.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG G 2 0.25 SIDE CHAIN
REMARK 500 ARG H 2 0.30 SIDE CHAIN
REMARK 500 ARG I 2 0.12 SIDE CHAIN
REMARK 500 ARG J 2 0.16 SIDE CHAIN
REMARK 500 ARG K 2 0.27 SIDE CHAIN
REMARK 500 ARG L 2 0.29 SIDE CHAIN
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 ANGLE, 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 FC0 G 1 -26.52
REMARK 500 FC0 K 1 -19.79
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'--O4'--N1(N9)--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 GLU A 88 22.5 L L OUTSIDE RANGE
REMARK 500 LYS A 109 24.7 L L OUTSIDE RANGE
REMARK 500 GLU B 88 21.5 L L OUTSIDE RANGE
REMARK 500 GLU B 261 25.0 L L OUTSIDE RANGE
REMARK 500 GLU C 261 24.1 L L OUTSIDE RANGE
REMARK 500 TYR C 626 24.9 L L OUTSIDE RANGE
REMARK 500 TYR D 418 21.3 L L OUTSIDE RANGE
REMARK 500 LEU D 603 24.3 L L OUTSIDE RANGE
REMARK 500 GLU E 261 24.1 L L OUTSIDE RANGE
REMARK 500 TYR F 418 21.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ANTIPAIN: COVALENTLY BOUND TO THE CATALYTIC SER563
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN G OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN H OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN J OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN K OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN L OF ANTIPAIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BP8 RELATED DB: PDB
REMARK 900 OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI - OPEN FORM
DBREF 4BP9 A 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 B 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 C 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 D 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 E 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 F 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 G 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 H 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 I 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 J 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 K 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 L 1 4 NOR NOR00664 NOR00664 1 4
SEQADV 4BP9 OAR G 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR H 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR I 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR J 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR K 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR L 4 NOR NOR00664 RGL 4 CONFLICT
SEQRES 1 A 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 A 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 A 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 A 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 A 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 A 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 A 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 A 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 A 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 A 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 A 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 A 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 A 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 A 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 A 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 A 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 A 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 A 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 A 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 A 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 A 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 A 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 A 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 A 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 A 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 A 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 A 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 A 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 A 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 A 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 A 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 A 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 A 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 A 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 A 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 A 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 A 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 A 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 A 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 A 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 A 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 A 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 A 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 A 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 A 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 A 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 A 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 A 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 A 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 A 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 A 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 A 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 A 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 A 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 A 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 B 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 B 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 B 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 B 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 B 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 B 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 B 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 B 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 B 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 B 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 B 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 B 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 B 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 B 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 B 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 B 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 B 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 B 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 B 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 B 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 B 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 B 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 B 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 B 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 B 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 B 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 B 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 B 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 B 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 B 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 B 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 B 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 B 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 B 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 B 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 B 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 B 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 B 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 B 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 B 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 B 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 B 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 B 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 B 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 B 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 B 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 B 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 B 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 B 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 B 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 B 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 B 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 B 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 B 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 B 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 C 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 C 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 C 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 C 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 C 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 C 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 C 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 C 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 C 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 C 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 C 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 C 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 C 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 C 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 C 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 C 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 C 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 C 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 C 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 C 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 C 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 C 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 C 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 C 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 C 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 C 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 C 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 C 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 C 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 C 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 C 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 C 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 C 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 C 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 C 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 C 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 C 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 C 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 C 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 C 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 C 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 C 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 C 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 C 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 C 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 C 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 C 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 C 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 C 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 C 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 C 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 C 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 C 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 C 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 C 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 D 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 D 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 D 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 D 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 D 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 D 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 D 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 D 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 D 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 D 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 D 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 D 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 D 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 D 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 D 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 D 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 D 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 D 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 D 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 D 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 D 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 D 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 D 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 D 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 D 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 D 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 D 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 D 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 D 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 D 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 D 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 D 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 D 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 D 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 D 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 D 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 D 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 D 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 D 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 D 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 D 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 D 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 D 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 D 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 D 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 D 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 D 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 D 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 D 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 D 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 D 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 D 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 D 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 D 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 D 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 E 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 E 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 E 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 E 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 E 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 E 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 E 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 E 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 E 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 E 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 E 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 E 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 E 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 E 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 E 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 E 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 E 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 E 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 E 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 E 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 E 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 E 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 E 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 E 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 E 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 E 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 E 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 E 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 E 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 E 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 E 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 E 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 E 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 E 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 E 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 E 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 E 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 E 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 E 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 E 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 E 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 E 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 E 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 E 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 E 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 E 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 E 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 E 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 E 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 E 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 E 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 E 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 E 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 E 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 E 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 F 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 F 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 F 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 F 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 F 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 F 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 F 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 F 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 F 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 F 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 F 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 F 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 F 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 F 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 F 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 F 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 F 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 F 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 F 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 F 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 F 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 F 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 F 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 F 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 F 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 F 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 F 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 F 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 F 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 F 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 F 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 F 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 F 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 F 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 F 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 F 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 F 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 F 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 F 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 F 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 F 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 F 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 F 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 F 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 F 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 F 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 F 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 F 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 F 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 F 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 F 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 F 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 F 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 F 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 F 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 G 4 FC0 ARG VAL OAR
SEQRES 1 H 4 FC0 ARG VAL OAR
SEQRES 1 I 4 FC0 ARG VAL OAR
SEQRES 1 J 4 FC0 ARG VAL OAR
SEQRES 1 K 4 FC0 ARG VAL OAR
SEQRES 1 L 4 FC0 ARG VAL OAR
MODRES 4BP9 FC0 G 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 FC0 H 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 FC0 I 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 FC0 J 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 FC0 K 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 FC0 L 1 PHE N-CARBOXY-L-PHENYLALANINE
HET FC0 G 1 14
HET OAR G 4 11
HET FC0 H 1 14
HET OAR H 4 11
HET FC0 I 1 14
HET OAR I 4 11
HET FC0 J 1 14
HET OAR J 4 11
HET FC0 K 1 14
HET OAR K 4 11
HET FC0 L 1 14
HET OAR L 4 11
HETNAM FC0 N-CARBOXY-L-PHENYLALANINE
HETNAM OAR N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
FORMUL 2 FC0 6(C10 H11 N O4)
FORMUL 3 OAR 6(C6 H16 N4 O)
FORMUL 4 HOH *344(H2 O)
HELIX 1 1 LEU A 41 ARG A 45 5 5
HELIX 2 2 ASP A 51 ALA A 69 1 19
HELIX 3 3 ILE A 72 HIS A 86 1 15
HELIX 4 4 GLU A 137 GLU A 142 1 6
HELIX 5 5 ARG A 180 VAL A 182 5 3
HELIX 6 6 PRO A 198 ALA A 200 5 3
HELIX 7 7 ASP A 209 ARG A 213 5 5
HELIX 8 8 PRO A 225 ASP A 229 5 5
HELIX 9 9 ARG A 271 GLY A 273 5 3
HELIX 10 10 SER A 373 LEU A 377 5 5
HELIX 11 11 CYS A 393 MET A 396 5 4
HELIX 12 12 GLU A 440 LYS A 442 5 3
HELIX 13 13 ASN A 494 ARG A 496 5 3
HELIX 14 14 PHE A 497 ASP A 502 1 6
HELIX 15 15 ARG A 520 VAL A 525 1 6
HELIX 16 16 LYS A 528 THR A 531 5 4
HELIX 17 17 LYS A 532 SER A 549 1 18
HELIX 18 18 THR A 553 ALA A 555 5 3
HELIX 19 19 SER A 563 ARG A 576 1 14
HELIX 20 20 PRO A 577 PHE A 580 5 4
HELIX 21 21 ASP A 591 ASP A 598 1 8
HELIX 22 22 THR A 605 GLU A 610 5 6
HELIX 23 23 PHE A 619 SER A 625 1 7
HELIX 24 24 SER A 627 VAL A 632 1 6
HELIX 25 25 TYR A 653 LYS A 667 1 15
HELIX 26 26 TYR A 690 ASN A 708 1 19
HELIX 27 27 LEU B 41 ARG B 45 5 5
HELIX 28 28 ASP B 51 VAL B 70 1 20
HELIX 29 29 ILE B 72 GLU B 88 1 17
HELIX 30 30 GLU B 137 GLU B 142 1 6
HELIX 31 31 ARG B 180 VAL B 182 5 3
HELIX 32 32 PRO B 198 ALA B 200 5 3
HELIX 33 33 ALA B 210 LYS B 212 5 3
HELIX 34 34 PRO B 225 ASP B 229 5 5
HELIX 35 35 CYS B 393 MET B 396 5 4
HELIX 36 36 GLU B 440 LYS B 442 5 3
HELIX 37 37 ASN B 494 ARG B 496 5 3
HELIX 38 38 PHE B 497 ASP B 502 1 6
HELIX 39 39 ARG B 520 VAL B 525 1 6
HELIX 40 40 LYS B 528 LYS B 532 5 5
HELIX 41 41 ARG B 533 SER B 549 1 17
HELIX 42 42 THR B 553 ALA B 555 5 3
HELIX 43 43 ALA B 564 ARG B 576 1 13
HELIX 44 44 PRO B 577 PHE B 580 5 4
HELIX 45 45 ASP B 591 CYS B 597 1 7
HELIX 46 46 THR B 604 GLU B 609 5 6
HELIX 47 47 PHE B 619 SER B 625 1 7
HELIX 48 48 PRO B 628 VAL B 632 5 5
HELIX 49 49 TYR B 653 LYS B 667 1 15
HELIX 50 50 TYR B 690 LEU B 707 1 18
HELIX 51 51 LEU C 41 ARG C 45 5 5
HELIX 52 52 ASP C 51 VAL C 70 1 20
HELIX 53 53 ASP C 71 LYS C 73 5 3
HELIX 54 54 ASP C 74 GLU C 88 1 15
HELIX 55 55 GLU C 137 GLU C 142 1 6
HELIX 56 56 ARG C 180 VAL C 182 5 3
HELIX 57 57 PRO C 198 ALA C 200 5 3
HELIX 58 58 ASP C 209 ARG C 213 5 5
HELIX 59 59 PRO C 225 ASP C 229 5 5
HELIX 60 60 ARG C 271 GLY C 273 5 3
HELIX 61 61 CYS C 393 MET C 396 5 4
HELIX 62 62 GLU C 440 LYS C 442 5 3
HELIX 63 63 ASN C 494 ARG C 496 5 3
HELIX 64 64 PHE C 497 ASP C 502 1 6
HELIX 65 65 ARG C 520 VAL C 525 1 6
HELIX 66 66 LYS C 528 THR C 531 5 4
HELIX 67 67 LYS C 532 SER C 549 1 18
HELIX 68 68 THR C 553 ALA C 555 5 3
HELIX 69 69 SER C 563 ARG C 576 1 14
HELIX 70 70 PRO C 577 PHE C 580 5 4
HELIX 71 71 ASP C 591 ASP C 598 1 8
HELIX 72 72 LEU C 603 GLU C 610 5 8
HELIX 73 73 GLU C 616 SER C 627 1 12
HELIX 74 74 PRO C 628 VAL C 632 5 5
HELIX 75 75 TYR C 653 LYS C 667 1 15
HELIX 76 76 LYS C 691 ASN C 708 1 18
HELIX 77 77 LEU D 41 ARG D 45 5 5
HELIX 78 78 ASP D 51 ALA D 69 1 19
HELIX 79 79 ILE D 72 HIS D 86 1 15
HELIX 80 80 GLU D 137 ALA D 141 1 5
HELIX 81 81 ARG D 180 VAL D 182 5 3
HELIX 82 82 ALA D 210 LYS D 212 5 3
HELIX 83 83 PRO D 225 ASP D 229 5 5
HELIX 84 84 ARG D 271 GLY D 273 5 3
HELIX 85 85 SER D 373 LEU D 377 5 5
HELIX 86 86 CYS D 393 MET D 396 5 4
HELIX 87 87 GLU D 440 LYS D 442 5 3
HELIX 88 88 ASN D 494 ARG D 496 5 3
HELIX 89 89 PHE D 497 ASP D 502 1 6
HELIX 90 90 ARG D 520 VAL D 525 1 6
HELIX 91 91 LYS D 528 THR D 531 5 4
HELIX 92 92 LYS D 532 SER D 549 1 18
HELIX 93 93 THR D 553 ALA D 555 5 3
HELIX 94 94 SER D 563 ARG D 576 1 14
HELIX 95 95 PRO D 577 PHE D 580 5 4
HELIX 96 96 ASP D 591 CYS D 597 1 7
HELIX 97 97 THR D 605 GLU D 610 5 6
HELIX 98 98 PHE D 619 SER D 625 1 7
HELIX 99 99 PRO D 628 VAL D 632 5 5
HELIX 100 100 TYR D 653 LYS D 667 1 15
HELIX 101 101 TYR D 690 ASN D 708 1 19
HELIX 102 102 LEU E 41 ARG E 45 5 5
HELIX 103 103 ASP E 51 VAL E 70 1 20
HELIX 104 104 ILE E 72 GLU E 88 1 17
HELIX 105 105 GLU E 137 GLU E 142 1 6
HELIX 106 106 ARG E 180 VAL E 182 5 3
HELIX 107 107 PRO E 198 ALA E 200 5 3
HELIX 108 108 ASP E 209 ARG E 213 5 5
HELIX 109 109 PRO E 225 ASP E 229 5 5
HELIX 110 110 CYS E 393 MET E 396 5 4
HELIX 111 111 GLU E 440 LYS E 442 5 3
HELIX 112 112 ASN E 494 ARG E 496 5 3
HELIX 113 113 PHE E 497 ASP E 502 1 6
HELIX 114 114 ARG E 520 VAL E 525 1 6
HELIX 115 115 LYS E 528 THR E 531 5 4
HELIX 116 116 LYS E 532 SER E 549 1 18
HELIX 117 117 THR E 553 ALA E 555 5 3
HELIX 118 118 ALA E 564 ARG E 576 1 13
HELIX 119 119 PRO E 577 PHE E 580 5 4
HELIX 120 120 ASP E 591 ASP E 598 1 8
HELIX 121 121 LEU E 603 TRP E 608 1 6
HELIX 122 122 GLU E 616 SER E 625 1 10
HELIX 123 123 PRO E 628 VAL E 632 5 5
HELIX 124 124 TYR E 653 LYS E 667 1 15
HELIX 125 125 TYR E 690 ASN E 708 1 19
HELIX 126 126 LEU F 41 ARG F 45 5 5
HELIX 127 127 ASP F 51 VAL F 70 1 20
HELIX 128 128 ILE F 72 SER F 85 1 14
HELIX 129 129 GLU F 137 ALA F 141 1 5
HELIX 130 130 ARG F 180 VAL F 182 5 3
HELIX 131 131 PRO F 198 ALA F 200 5 3
HELIX 132 132 ALA F 210 LYS F 212 5 3
HELIX 133 133 PRO F 225 ASP F 229 5 5
HELIX 134 134 CYS F 393 MET F 396 5 4
HELIX 135 135 GLU F 440 LYS F 442 5 3
HELIX 136 136 ASN F 494 ARG F 496 5 3
HELIX 137 137 PHE F 497 ASP F 502 1 6
HELIX 138 138 ARG F 520 VAL F 525 1 6
HELIX 139 139 LYS F 528 THR F 531 5 4
HELIX 140 140 LYS F 532 SER F 549 1 18
HELIX 141 141 THR F 553 ALA F 555 5 3
HELIX 142 142 SER F 563 ARG F 576 1 14
HELIX 143 143 PRO F 577 PHE F 580 5 4
HELIX 144 144 ASP F 591 CYS F 597 1 7
HELIX 145 145 LEU F 603 TRP F 608 1 6
HELIX 146 146 PHE F 619 SER F 625 1 7
HELIX 147 147 PRO F 628 VAL F 632 5 5
HELIX 148 148 TYR F 653 LYS F 667 1 15
HELIX 149 149 TYR F 690 LEU F 707 1 18
SHEET 1 AA 2 GLU A 15 PHE A 18 0
SHEET 2 AA 2 ARG A 35 VAL A 38 -1 O ARG A 35 N PHE A 18
SHEET 1 AB 2 ASP A 91 MET A 92 0
SHEET 2 AB 2 PHE A 101 ASP A 107 -1 O ASP A 107 N ASP A 91
SHEET 1 AC 2 TYR A 96 TYR A 98 0
SHEET 2 AC 2 PHE A 101 ASP A 107 -1 O PHE A 101 N TYR A 98
SHEET 1 AD 4 GLU A 132 ASP A 136 0
SHEET 2 AD 4 LEU A 115 PRO A 120 -1 O HIS A 116 N VAL A 134
SHEET 3 AD 4 PHE A 101 ASP A 107 -1 O LEU A 102 N VAL A 119
SHEET 4 AD 4 TYR A 96 TYR A 98 -1 O TYR A 96 N TYR A 103
SHEET 1 AE 4 GLU A 132 ASP A 136 0
SHEET 2 AE 4 LEU A 115 PRO A 120 -1 O HIS A 116 N VAL A 134
SHEET 3 AE 4 PHE A 101 ASP A 107 -1 O LEU A 102 N VAL A 119
SHEET 4 AE 4 ASP A 91 MET A 92 -1 O ASP A 91 N ASP A 107
SHEET 1 AF 4 VAL A 148 PRO A 154 0
SHEET 2 AF 4 VAL A 162 ASP A 167 -1 O ALA A 163 N ALA A 153
SHEET 3 AF 4 TYR A 174 PHE A 178 -1 O SER A 175 N VAL A 166
SHEET 4 AF 4 VAL A 187 THR A 190 -1 O VAL A 187 N ILE A 176
SHEET 1 AG 4 VAL A 195 TRP A 196 0
SHEET 2 AG 4 CYS A 202 THR A 207 -1 O PHE A 204 N VAL A 195
SHEET 3 AG 4 LYS A 216 ILE A 221 -1 O LYS A 216 N THR A 207
SHEET 4 AG 4 VAL A 230 THR A 234 -1 O VAL A 230 N ARG A 219
SHEET 1 AH 4 SER A 241 ARG A 246 0
SHEET 2 AH 4 THR A 252 SER A 259 -1 O ILE A 254 N GLY A 245
SHEET 3 AH 4 THR A 262 ASP A 269 -1 O THR A 262 N SER A 259
SHEET 4 AH 4 GLU A 280 MET A 281 -1 O GLU A 280 N LEU A 267
SHEET 1 AI 4 TYR A 291 HIS A 296 0
SHEET 2 AI 4 THR A 300 THR A 305 -1 O THR A 300 N HIS A 296
SHEET 3 AI 4 LYS A 314 LYS A 319 -1 O LYS A 314 N THR A 305
SHEET 4 AI 4 THR A 328 ILE A 331 -1 O THR A 328 N LEU A 317
SHEET 1 AJ 4 THR A 338 VAL A 344 0
SHEET 2 AJ 4 PHE A 348 ARG A 355 -1 O VAL A 350 N ALA A 343
SHEET 3 AJ 4 LEU A 358 ARG A 365 -1 O LEU A 358 N ARG A 355
SHEET 4 AJ 4 LYS A 378 GLU A 379 -1 O LYS A 378 N THR A 363
SHEET 1 AK 4 THR A 388 VAL A 391 0
SHEET 2 AK 4 LEU A 403 SER A 409 -1 O ARG A 407 N HIS A 390
SHEET 3 AK 4 VAL A 416 ASP A 421 -1 O VAL A 416 N TYR A 408
SHEET 4 AK 4 ARG A 427 ALA A 432 -1 O LYS A 428 N ASP A 419
SHEET 1 AL 8 TYR A 444 THR A 452 0
SHEET 2 AL 8 LYS A 458 ASP A 466 -1 O VAL A 459 N ALA A 451
SHEET 3 AL 8 ILE A 506 ALA A 510 -1 O TYR A 507 N VAL A 464
SHEET 4 AL 8 THR A 477 TYR A 480 1 O MET A 478 N ALA A 508
SHEET 5 AL 8 LEU A 557 ARG A 562 1 O SER A 558 N LEU A 479
SHEET 6 AL 8 VAL A 582 GLY A 586 1 O VAL A 582 N CYS A 559
SHEET 7 AL 8 HIS A 639 GLY A 645 1 O HIS A 639 N ALA A 583
SHEET 8 AL 8 VAL A 673 ASP A 678 1 O LEU A 674 N ILE A 642
SHEET 1 BA 2 GLU B 15 PHE B 18 0
SHEET 2 BA 2 ARG B 35 VAL B 38 -1 O ARG B 35 N PHE B 18
SHEET 1 BB 2 ASP B 91 MET B 92 0
SHEET 2 BB 2 PHE B 101 ASP B 107 -1 O ASP B 107 N ASP B 91
SHEET 1 BC 2 TYR B 96 TYR B 98 0
SHEET 2 BC 2 PHE B 101 ASP B 107 -1 O PHE B 101 N TYR B 98
SHEET 1 BD 4 GLU B 132 ASP B 136 0
SHEET 2 BD 4 LEU B 115 PRO B 120 -1 O HIS B 116 N LEU B 135
SHEET 3 BD 4 PHE B 101 ASP B 107 -1 O LEU B 102 N VAL B 119
SHEET 4 BD 4 TYR B 96 TYR B 98 -1 O TYR B 96 N TYR B 103
SHEET 1 BE 4 GLU B 132 ASP B 136 0
SHEET 2 BE 4 LEU B 115 PRO B 120 -1 O HIS B 116 N LEU B 135
SHEET 3 BE 4 PHE B 101 ASP B 107 -1 O LEU B 102 N VAL B 119
SHEET 4 BE 4 ASP B 91 MET B 92 -1 O ASP B 91 N ASP B 107
SHEET 1 BF 4 VAL B 148 PRO B 154 0
SHEET 2 BF 4 VAL B 162 ASP B 167 -1 O ALA B 163 N ALA B 153
SHEET 3 BF 4 TYR B 174 PHE B 178 -1 O SER B 175 N VAL B 166
SHEET 4 BF 4 VAL B 187 THR B 190 -1 O VAL B 187 N ILE B 176
SHEET 1 BG 4 VAL B 195 TRP B 196 0
SHEET 2 BG 4 CYS B 202 LYS B 208 -1 O PHE B 204 N VAL B 195
SHEET 3 BG 4 ASP B 214 ILE B 221 -1 O LYS B 216 N THR B 207
SHEET 4 BG 4 VAL B 230 THR B 234 -1 O VAL B 230 N ARG B 219
SHEET 1 BH 4 SER B 241 ARG B 246 0
SHEET 2 BH 4 THR B 252 MET B 258 -1 O ILE B 254 N GLY B 245
SHEET 3 BH 4 SER B 263 ASP B 269 -1 O GLU B 264 N SER B 257
SHEET 4 BH 4 GLU B 280 MET B 281 -1 O GLU B 280 N LEU B 267
SHEET 1 BI 3 TYR B 291 HIS B 296 0
SHEET 2 BI 3 THR B 300 THR B 305 -1 O THR B 300 N HIS B 296
SHEET 3 BI 3 LYS B 314 LYS B 319 -1 O LYS B 314 N THR B 305
SHEET 1 BJ 4 THR B 338 VAL B 344 0
SHEET 2 BJ 4 PHE B 348 ARG B 355 -1 O VAL B 350 N ALA B 343
SHEET 3 BJ 4 LEU B 358 LEU B 366 -1 O LEU B 358 N ARG B 355
SHEET 4 BJ 4 PHE B 372 GLU B 379 -1 N SER B 373 O ARG B 365
SHEET 1 BK 4 THR B 388 VAL B 391 0
SHEET 2 BK 4 LEU B 403 SER B 409 -1 O ARG B 407 N HIS B 390
SHEET 3 BK 4 VAL B 416 ASP B 421 -1 O VAL B 416 N TYR B 408
SHEET 4 BK 4 ARG B 427 ALA B 432 -1 O LYS B 428 N ASP B 419
SHEET 1 BL 8 TYR B 444 THR B 452 0
SHEET 2 BL 8 LYS B 458 ASP B 466 -1 O VAL B 459 N ALA B 451
SHEET 3 BL 8 ILE B 506 ALA B 510 -1 O TYR B 507 N VAL B 464
SHEET 4 BL 8 THR B 477 GLY B 481 1 O MET B 478 N ALA B 508
SHEET 5 BL 8 LEU B 557 ARG B 562 1 O SER B 558 N LEU B 479
SHEET 6 BL 8 VAL B 582 GLY B 586 1 O VAL B 582 N CYS B 559
SHEET 7 BL 8 HIS B 639 GLY B 645 1 O HIS B 639 N ALA B 583
SHEET 8 BL 8 VAL B 673 ASP B 678 1 O LEU B 674 N ILE B 642
SHEET 1 CA 2 GLU C 15 PHE C 18 0
SHEET 2 CA 2 ARG C 35 VAL C 38 -1 O ARG C 35 N PHE C 18
SHEET 1 CB 4 TYR C 96 TYR C 98 0
SHEET 2 CB 4 PHE C 101 ARG C 106 -1 O PHE C 101 N TYR C 98
SHEET 3 CB 4 LEU C 115 PRO C 120 -1 O LEU C 115 N ARG C 106
SHEET 4 CB 4 GLU C 132 ASP C 136 -1 O GLU C 132 N ARG C 118
SHEET 1 CC 4 VAL C 148 PRO C 154 0
SHEET 2 CC 4 VAL C 162 ASP C 167 -1 O ALA C 163 N ALA C 153
SHEET 3 CC 4 TYR C 174 PHE C 178 -1 O SER C 175 N VAL C 166
SHEET 4 CC 4 VAL C 187 THR C 190 -1 O VAL C 187 N ILE C 176
SHEET 1 CD 4 VAL C 195 TRP C 196 0
SHEET 2 CD 4 CYS C 202 THR C 207 -1 O PHE C 204 N VAL C 195
SHEET 3 CD 4 LYS C 216 ILE C 221 -1 O LYS C 216 N THR C 207
SHEET 4 CD 4 VAL C 230 THR C 234 -1 O VAL C 230 N ARG C 219
SHEET 1 CE 4 SER C 241 ARG C 246 0
SHEET 2 CE 4 THR C 252 SER C 259 -1 O ILE C 254 N GLY C 245
SHEET 3 CE 4 THR C 262 ASP C 269 -1 O THR C 262 N SER C 259
SHEET 4 CE 4 GLU C 280 MET C 281 -1 O GLU C 280 N LEU C 267
SHEET 1 CF 4 TYR C 291 HIS C 296 0
SHEET 2 CF 4 THR C 300 THR C 305 -1 O THR C 300 N HIS C 296
SHEET 3 CF 4 LYS C 314 LYS C 319 -1 O LYS C 314 N THR C 305
SHEET 4 CF 4 THR C 328 ILE C 331 -1 O THR C 328 N LEU C 317
SHEET 1 CG 4 VAL C 337 VAL C 344 0
SHEET 2 CG 4 PHE C 348 ARG C 355 -1 O VAL C 350 N ALA C 343
SHEET 3 CG 4 LEU C 358 GLY C 367 -1 O LEU C 358 N ARG C 355
SHEET 4 CG 4 LEU C 371 PHE C 372 1 O LEU C 371 N GLY C 367
SHEET 1 CH 4 VAL C 337 VAL C 344 0
SHEET 2 CH 4 PHE C 348 ARG C 355 -1 O VAL C 350 N ALA C 343
SHEET 3 CH 4 LEU C 358 GLY C 367 -1 O LEU C 358 N ARG C 355
SHEET 4 CH 4 LYS C 378 GLU C 379 -1 O LYS C 378 N THR C 363
SHEET 1 CI 2 LEU C 371 PHE C 372 0
SHEET 2 CI 2 LEU C 358 GLY C 367 1 N GLY C 367 O LEU C 371
SHEET 1 CJ 4 PHE C 387 VAL C 391 0
SHEET 2 CJ 4 ARG C 405 SER C 410 -1 O ARG C 407 N HIS C 390
SHEET 3 CJ 4 VAL C 416 GLU C 420 -1 O VAL C 416 N TYR C 408
SHEET 4 CJ 4 ARG C 427 ALA C 432 -1 O LYS C 428 N ASP C 419
SHEET 1 CK 8 TYR C 444 THR C 452 0
SHEET 2 CK 8 LYS C 458 ASP C 466 -1 O VAL C 459 N ALA C 451
SHEET 3 CK 8 ILE C 506 ALA C 510 -1 O TYR C 507 N VAL C 464
SHEET 4 CK 8 THR C 477 GLY C 481 1 O MET C 478 N ALA C 508
SHEET 5 CK 8 LEU C 557 ARG C 562 1 O SER C 558 N LEU C 479
SHEET 6 CK 8 VAL C 582 GLY C 586 1 O VAL C 582 N CYS C 559
SHEET 7 CK 8 HIS C 639 GLY C 645 1 O HIS C 639 N ALA C 583
SHEET 8 CK 8 VAL C 673 ASP C 678 1 O LEU C 674 N ILE C 642
SHEET 1 DA 2 GLU D 15 PHE D 18 0
SHEET 2 DA 2 ARG D 35 VAL D 38 -1 O ARG D 35 N PHE D 18
SHEET 1 DB 2 ASP D 91 MET D 92 0
SHEET 2 DB 2 PHE D 101 ASP D 107 -1 O ASP D 107 N ASP D 91
SHEET 1 DC 2 TYR D 96 TYR D 98 0
SHEET 2 DC 2 PHE D 101 ASP D 107 1 O PHE D 101 N TYR D 98
SHEET 1 DD 4 GLU D 132 ASP D 136 0
SHEET 2 DD 4 LEU D 115 PRO D 120 -1 O HIS D 116 N VAL D 134
SHEET 3 DD 4 PHE D 101 ASP D 107 -1 O LEU D 102 N VAL D 119
SHEET 4 DD 4 TYR D 96 TYR D 98 1 O TYR D 96 N TYR D 103
SHEET 1 DE 4 GLU D 132 ASP D 136 0
SHEET 2 DE 4 LEU D 115 PRO D 120 -1 O HIS D 116 N VAL D 134
SHEET 3 DE 4 PHE D 101 ASP D 107 -1 O LEU D 102 N VAL D 119
SHEET 4 DE 4 ASP D 91 MET D 92 -1 O ASP D 91 N ASP D 107
SHEET 1 DF 4 VAL D 148 PRO D 154 0
SHEET 2 DF 4 VAL D 162 ASP D 167 -1 O ALA D 163 N ALA D 153
SHEET 3 DF 4 TYR D 174 PHE D 178 -1 O SER D 175 N VAL D 166
SHEET 4 DF 4 VAL D 187 THR D 190 -1 O VAL D 187 N ILE D 176
SHEET 1 DG 4 VAL D 195 TRP D 196 0
SHEET 2 DG 4 CYS D 202 LYS D 208 -1 O PHE D 204 N VAL D 195
SHEET 3 DG 4 ASP D 214 ILE D 221 -1 N ASN D 215 O THR D 207
SHEET 4 DG 4 VAL D 230 THR D 234 -1 O VAL D 230 N ARG D 219
SHEET 1 DH 4 SER D 241 ARG D 246 0
SHEET 2 DH 4 THR D 252 SER D 259 -1 O ILE D 254 N GLY D 245
SHEET 3 DH 4 THR D 262 ASP D 269 -1 O THR D 262 N SER D 259
SHEET 4 DH 4 GLU D 280 MET D 281 -1 O GLU D 280 N LEU D 267
SHEET 1 DI 4 TYR D 291 HIS D 296 0
SHEET 2 DI 4 THR D 300 THR D 305 -1 O THR D 300 N HIS D 296
SHEET 3 DI 4 LYS D 314 LYS D 319 -1 O LYS D 314 N THR D 305
SHEET 4 DI 4 THR D 328 ILE D 331 -1 O THR D 328 N LEU D 317
SHEET 1 DJ 4 VAL D 337 VAL D 344 0
SHEET 2 DJ 4 PHE D 348 ARG D 355 -1 O VAL D 350 N ALA D 343
SHEET 3 DJ 4 LEU D 358 ARG D 365 -1 O LEU D 358 N ARG D 355
SHEET 4 DJ 4 LYS D 378 GLU D 379 -1 O LYS D 378 N THR D 363
SHEET 1 DK 4 THR D 388 VAL D 391 0
SHEET 2 DK 4 LEU D 403 SER D 409 -1 O ARG D 407 N HIS D 390
SHEET 3 DK 4 VAL D 416 ASP D 421 -1 O VAL D 416 N TYR D 408
SHEET 4 DK 4 ARG D 427 ALA D 432 -1 O LYS D 428 N ASP D 419
SHEET 1 DL 8 TYR D 444 THR D 452 0
SHEET 2 DL 8 LYS D 458 ASP D 466 -1 O VAL D 459 N ALA D 451
SHEET 3 DL 8 ILE D 506 ALA D 510 -1 O TYR D 507 N VAL D 464
SHEET 4 DL 8 THR D 477 GLY D 481 1 O MET D 478 N ALA D 508
SHEET 5 DL 8 LEU D 557 ARG D 562 1 O SER D 558 N LEU D 479
SHEET 6 DL 8 VAL D 582 GLY D 586 1 O VAL D 582 N CYS D 559
SHEET 7 DL 8 HIS D 639 GLY D 645 1 O HIS D 639 N ALA D 583
SHEET 8 DL 8 VAL D 673 ASP D 678 1 O LEU D 674 N ILE D 642
SHEET 1 EA 2 GLU E 15 PHE E 18 0
SHEET 2 EA 2 ARG E 35 VAL E 38 -1 O ARG E 35 N PHE E 18
SHEET 1 EB 2 ASP E 91 MET E 92 0
SHEET 2 EB 2 PHE E 101 VAL E 108 -1 O ASP E 107 N ASP E 91
SHEET 1 EC 2 TYR E 96 TYR E 98 0
SHEET 2 EC 2 PHE E 101 VAL E 108 1 O PHE E 101 N TYR E 98
SHEET 1 ED 4 GLU E 132 ASP E 136 0
SHEET 2 ED 4 LEU E 111 PRO E 120 -1 O HIS E 116 N LEU E 135
SHEET 3 ED 4 PHE E 101 VAL E 108 -1 O LEU E 102 N VAL E 119
SHEET 4 ED 4 TYR E 96 TYR E 98 1 O TYR E 96 N TYR E 103
SHEET 1 EE 4 GLU E 132 ASP E 136 0
SHEET 2 EE 4 LEU E 111 PRO E 120 -1 O HIS E 116 N LEU E 135
SHEET 3 EE 4 PHE E 101 VAL E 108 -1 O LEU E 102 N VAL E 119
SHEET 4 EE 4 ASP E 91 MET E 92 -1 O ASP E 91 N ASP E 107
SHEET 1 EF 4 VAL E 148 PRO E 154 0
SHEET 2 EF 4 VAL E 162 ASP E 167 -1 O ALA E 163 N ALA E 153
SHEET 3 EF 4 TYR E 174 PHE E 178 -1 O SER E 175 N VAL E 166
SHEET 4 EF 4 VAL E 187 THR E 190 -1 O VAL E 187 N ILE E 176
SHEET 1 EG 4 VAL E 195 TRP E 196 0
SHEET 2 EG 4 CYS E 202 THR E 207 -1 O PHE E 204 N VAL E 195
SHEET 3 EG 4 LYS E 216 ILE E 221 -1 O LYS E 216 N THR E 207
SHEET 4 EG 4 VAL E 230 THR E 234 -1 O VAL E 230 N ARG E 219
SHEET 1 EH 4 SER E 241 ARG E 246 0
SHEET 2 EH 4 THR E 252 MET E 258 -1 O ILE E 254 N GLY E 245
SHEET 3 EH 4 SER E 263 ASP E 269 -1 O GLU E 264 N SER E 257
SHEET 4 EH 4 GLU E 280 MET E 281 -1 O GLU E 280 N LEU E 267
SHEET 1 EI 4 TYR E 291 HIS E 296 0
SHEET 2 EI 4 THR E 300 THR E 305 -1 O THR E 300 N HIS E 296
SHEET 3 EI 4 LYS E 314 LYS E 319 -1 O LYS E 314 N THR E 305
SHEET 4 EI 4 THR E 328 ILE E 331 -1 O THR E 328 N LEU E 317
SHEET 1 EJ 4 VAL E 337 PHE E 345 0
SHEET 2 EJ 4 PHE E 348 ARG E 355 -1 O PHE E 348 N PHE E 345
SHEET 3 EJ 4 LEU E 358 LEU E 366 -1 O LEU E 358 N ARG E 355
SHEET 4 EJ 4 PHE E 372 GLU E 379 -1 N SER E 373 O ARG E 365
SHEET 1 EK 4 THR E 388 VAL E 391 0
SHEET 2 EK 4 LEU E 406 SER E 409 -1 O ARG E 407 N HIS E 390
SHEET 3 EK 4 VAL E 416 GLU E 420 -1 O VAL E 416 N TYR E 408
SHEET 4 EK 4 ARG E 427 ALA E 432 -1 O LYS E 428 N ASP E 419
SHEET 1 EL 8 TYR E 444 THR E 452 0
SHEET 2 EL 8 LYS E 458 ASP E 466 -1 O VAL E 459 N ALA E 451
SHEET 3 EL 8 ILE E 506 ALA E 510 -1 O TYR E 507 N VAL E 464
SHEET 4 EL 8 THR E 477 GLY E 481 1 O MET E 478 N ALA E 508
SHEET 5 EL 8 LEU E 557 ARG E 562 1 O SER E 558 N LEU E 479
SHEET 6 EL 8 VAL E 582 GLY E 586 1 O VAL E 582 N CYS E 559
SHEET 7 EL 8 HIS E 639 GLY E 645 1 O HIS E 639 N ALA E 583
SHEET 8 EL 8 VAL E 673 ASP E 678 1 O LEU E 674 N ILE E 642
SHEET 1 FA 2 HIS F 14 PHE F 18 0
SHEET 2 FA 2 ARG F 35 ASP F 39 -1 O ARG F 35 N PHE F 18
SHEET 1 FB 2 ASP F 91 MET F 92 0
SHEET 2 FB 2 PHE F 101 ASP F 107 -1 O ASP F 107 N ASP F 91
SHEET 1 FC 2 TYR F 96 TYR F 98 0
SHEET 2 FC 2 PHE F 101 ASP F 107 1 O PHE F 101 N TYR F 98
SHEET 1 FD 4 GLU F 132 ASP F 136 0
SHEET 2 FD 4 LEU F 115 ARG F 118 -1 O HIS F 116 N VAL F 134
SHEET 3 FD 4 PHE F 101 ASP F 107 -1 O TYR F 104 N CYS F 117
SHEET 4 FD 4 TYR F 96 TYR F 98 1 O TYR F 96 N TYR F 103
SHEET 1 FE 4 GLU F 132 ASP F 136 0
SHEET 2 FE 4 LEU F 115 ARG F 118 -1 O HIS F 116 N VAL F 134
SHEET 3 FE 4 PHE F 101 ASP F 107 -1 O TYR F 104 N CYS F 117
SHEET 4 FE 4 ASP F 91 MET F 92 -1 O ASP F 91 N ASP F 107
SHEET 1 FF 4 VAL F 148 PRO F 154 0
SHEET 2 FF 4 VAL F 162 ASP F 167 -1 O ALA F 163 N ALA F 153
SHEET 3 FF 4 TYR F 174 PHE F 178 -1 O SER F 175 N VAL F 166
SHEET 4 FF 4 VAL F 187 THR F 190 -1 O VAL F 187 N ILE F 176
SHEET 1 FG 4 VAL F 195 TRP F 196 0
SHEET 2 FG 4 CYS F 202 LYS F 208 -1 O PHE F 204 N VAL F 195
SHEET 3 FG 4 ASP F 214 ILE F 221 -1 O LYS F 216 N THR F 207
SHEET 4 FG 4 VAL F 230 THR F 234 -1 O VAL F 230 N ARG F 219
SHEET 1 FH 4 SER F 241 ARG F 246 0
SHEET 2 FH 4 THR F 252 SER F 259 -1 O ILE F 254 N GLY F 245
SHEET 3 FH 4 THR F 262 ASP F 269 -1 O THR F 262 N SER F 259
SHEET 4 FH 4 GLU F 280 MET F 281 -1 O GLU F 280 N LEU F 267
SHEET 1 FI 4 TYR F 291 HIS F 296 0
SHEET 2 FI 4 THR F 300 THR F 305 -1 O THR F 300 N HIS F 296
SHEET 3 FI 4 LYS F 314 LYS F 319 -1 O LYS F 314 N THR F 305
SHEET 4 FI 4 VAL F 329 ILE F 331 -1 N LEU F 330 O VAL F 315
SHEET 1 FJ 4 THR F 338 VAL F 344 0
SHEET 2 FJ 4 PHE F 348 ARG F 355 -1 O VAL F 350 N ALA F 343
SHEET 3 FJ 4 LEU F 358 ARG F 365 -1 O LEU F 358 N ARG F 355
SHEET 4 FJ 4 LYS F 378 GLU F 379 -1 O LYS F 378 N THR F 363
SHEET 1 FK 4 PHE F 387 VAL F 391 0
SHEET 2 FK 4 LEU F 406 SER F 410 -1 O ARG F 407 N HIS F 390
SHEET 3 FK 4 VAL F 416 GLU F 420 -1 O VAL F 416 N TYR F 408
SHEET 4 FK 4 ARG F 427 ALA F 432 -1 O LYS F 428 N ASP F 419
SHEET 1 FL 8 TYR F 444 THR F 452 0
SHEET 2 FL 8 LYS F 458 ASP F 466 -1 O VAL F 459 N ALA F 451
SHEET 3 FL 8 ILE F 506 ALA F 510 -1 O TYR F 507 N VAL F 464
SHEET 4 FL 8 THR F 477 TYR F 480 1 O MET F 478 N ALA F 508
SHEET 5 FL 8 LEU F 557 ARG F 562 1 O SER F 558 N LEU F 479
SHEET 6 FL 8 VAL F 582 GLY F 586 1 O VAL F 582 N CYS F 559
SHEET 7 FL 8 HIS F 639 GLY F 645 1 O HIS F 639 N ALA F 583
SHEET 8 FL 8 VAL F 673 ASP F 678 1 O LEU F 674 N ILE F 642
LINK C1 FC0 G 1 N ARG G 2 1555 1555 1.37
LINK N1 OAR G 4 C VAL G 3 1555 1555 1.34
LINK C6 OAR G 4 OG SER A 563 1555 1555 1.35
LINK C1 FC0 H 1 N ARG H 2 1555 1555 1.34
LINK N1 OAR H 4 C VAL H 3 1555 1555 1.32
LINK C6 OAR H 4 OG SER B 563 1555 1555 1.36
LINK C1 FC0 I 1 N ARG I 2 1555 1555 1.34
LINK C6 OAR I 4 OG SER C 563 1555 1555 1.35
LINK N1 OAR I 4 C VAL I 3 1555 1555 1.34
LINK C1 FC0 J 1 N ARG J 2 1555 1555 1.34
LINK C6 OAR J 4 OG SER D 563 1555 1555 1.35
LINK N1 OAR J 4 C VAL J 3 1555 1555 1.35
LINK C1 FC0 K 1 N ARG K 2 1555 1555 1.36
LINK N1 OAR K 4 C VAL K 3 1555 1555 1.35
LINK C6 OAR K 4 OG SER E 563 1555 1555 1.38
LINK C1 FC0 L 1 N ARG L 2 1555 1555 1.32
LINK C6 OAR L 4 OG SER F 563 1555 1555 1.35
LINK N1 OAR L 4 C VAL L 3 1555 1555 1.32
CISPEP 1 ASP A 32 PRO A 33 0 2.50
CISPEP 2 TYR A 482 GLY A 483 0 -15.32
CISPEP 3 ASP B 32 PRO B 33 0 1.68
CISPEP 4 ASP C 32 PRO C 33 0 -0.74
CISPEP 5 ASP D 32 PRO D 33 0 -1.21
CISPEP 6 ASP E 32 PRO E 33 0 2.44
CISPEP 7 TYR E 482 GLY E 483 0 -22.05
CISPEP 8 ASP F 32 PRO F 33 0 -4.87
CISPEP 9 TYR F 482 GLY F 483 0 -23.29
SITE 1 AC1 14 ASN A 191 LYS A 208 LYS A 212 ASP A 214
SITE 2 AC1 14 TYR A 482 TYR A 485 SER A 563 ALA A 564
SITE 3 AC1 14 PHE A 589 GLU A 607 ARG A 650 VAL A 651
SITE 4 AC1 14 HOH A2039 HOH A2105
SITE 1 AC2 13 GLU B 172 LYS B 208 ASP B 214 TYR B 482
SITE 2 AC2 13 TYR B 485 SER B 563 ALA B 564 PHE B 589
SITE 3 AC2 13 LEU B 603 GLU B 607 ARG B 650 VAL B 651
SITE 4 AC2 13 GLU B 655
SITE 1 AC3 14 GLU C 172 ASN C 191 LYS C 208 ASP C 214
SITE 2 AC3 14 TYR C 482 TYR C 485 SER C 563 ALA C 564
SITE 3 AC3 14 PHE C 589 GLU C 607 ARG C 650 VAL C 651
SITE 4 AC3 14 GLU C 655 HOH C2008
SITE 1 AC4 12 GLU D 172 LYS D 208 ASP D 214 TYR D 482
SITE 2 AC4 12 TYR D 485 SER D 563 ALA D 564 PHE D 589
SITE 3 AC4 12 LEU D 603 GLU D 607 ARG D 650 VAL D 651
SITE 1 AC5 13 ASN E 191 LYS E 208 LYS E 212 ASP E 214
SITE 2 AC5 13 TYR E 482 TYR E 485 SER E 563 ALA E 564
SITE 3 AC5 13 PHE E 589 GLU E 607 ARG E 650 VAL E 651
SITE 4 AC5 13 HOH E2015
SITE 1 AC6 13 GLU F 172 LYS F 208 LYS F 212 ASP F 214
SITE 2 AC6 13 TYR F 482 TYR F 485 SER F 563 ALA F 564
SITE 3 AC6 13 PHE F 589 GLU F 607 ARG F 650 HOH F2013
SITE 4 AC6 13 HOH F2039
CRYST1 71.800 148.800 268.000 90.00 91.00 90.00 P 1 21 1 12
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 0.013928 0.000000 0.000243 0.00000
SCALE2 0.000000 0.006720 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003732 0.00000
TER 5635 ARG A 714
TER 11270 ARG B 714
TER 16905 ARG C 714
TER 22540 ARG D 714
TER 28175 ARG E 714
TER 33810 ARG F 714
TER 33854 OAR G 4
TER 33898 OAR H 4
TER 33942 OAR I 4
TER 33986 OAR J 4
TER 34030 OAR K 4
TER 34074 OAR L 4
MASTER 931 0 12 149 273 0 23 634406 12 168 336
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