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HEADER HYDROLASE/HYDROLASE INHIBITOR 15-MAR-14 4PV7
TITLE COCRYSTAL STRUCTURE OF DIPEPTIDYL-PEPTIDASE 4 WITH AN INDOLE SCAFFOLD
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 6 TP103, DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADCP2, CD26, DPP4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS BETA-PROPELLER, HYDROLASE, EXTROCELLULAR SIDE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.XIAO,R.GUO,S.HUANG,H.CUI,S.YE,Z.ZHANG
REVDAT 1 18-MAR-15 4PV7 0
JRNL AUTH P.XIAO,R.GUO,S.HUANG,H.CUI,S.YE,Z.ZHANG
JRNL TITL DISCOVERY OF DIPEPTIDYL PEPTIDASE IV (DPP4) INHIBITORS BASED
JRNL TITL 2 ON A NOVEL INDOLE SCAFFOLD
JRNL REF CHIN.CHEM.LETT. V. 25 673 2014
JRNL REFN ISSN 1001-8417
JRNL DOI 10.1016/J.CCLET.2014.03.047
REMARK 2
REMARK 2 RESOLUTION. 3.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31241
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1332
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2354
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 146.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.88000
REMARK 3 B22 (A**2) : 4.88000
REMARK 3 B33 (A**2) : -7.32000
REMARK 3 B12 (A**2) : 2.44000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.536
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.449
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.906
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12306 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16754 ; 1.163 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1452 ; 5.905 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 614 ;34.885 ;24.007
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1986 ;17.622 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;16.843 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1758 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9530 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5479 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8247 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 434 ; 0.136 ; 0.200
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): 31 ; 0.396 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.242 ; 0.200
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): 7386 ; 0.205 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11748 ; 0.366 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5798 ; 0.578 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5006 ; 0.955 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 40 A 766 1
REMARK 3 1 B 40 B 766 1
REMARK 3 2 A 1000 A 1000 1
REMARK 3 2 B 1000 B 1000 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 5974 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 5974 ; 0.07 ; 0.50
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 40 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3384 14.2155 30.0950
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.5216
REMARK 3 T33: 0.7124 T12: 0.0994
REMARK 3 T13: -0.0444 T23: 0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 4.5410 L22: 3.6453
REMARK 3 L33: 2.9468 L12: 1.2092
REMARK 3 L13: -3.0897 L23: -1.8758
REMARK 3 S TENSOR
REMARK 3 S11: -0.3510 S12: 0.0959 S13: -1.6257
REMARK 3 S21: -0.3701 S22: -0.3594 S23: 0.1235
REMARK 3 S31: 1.0546 S32: -0.2088 S33: 0.7104
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 91 A 206
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5127 21.2204 23.5853
REMARK 3 T TENSOR
REMARK 3 T11: -0.2285 T22: 0.0084
REMARK 3 T33: -0.0203 T12: -0.1639
REMARK 3 T13: 0.1358 T23: -0.1918
REMARK 3 L TENSOR
REMARK 3 L11: 3.9331 L22: 3.1843
REMARK 3 L33: 3.6180 L12: 0.4237
REMARK 3 L13: -0.0813 L23: -0.4517
REMARK 3 S TENSOR
REMARK 3 S11: -0.1919 S12: 0.3073 S13: -1.1465
REMARK 3 S21: -0.4229 S22: -0.0818 S23: 0.3073
REMARK 3 S31: 1.0518 S32: -0.2805 S33: 0.2737
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 207 A 284
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1322 36.4325 25.5941
REMARK 3 T TENSOR
REMARK 3 T11: -0.5093 T22: -0.0761
REMARK 3 T33: -0.3593 T12: -0.0195
REMARK 3 T13: 0.0143 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 2.0644 L22: 2.8430
REMARK 3 L33: 3.1259 L12: 1.5182
REMARK 3 L13: -2.1640 L23: -2.0570
REMARK 3 S TENSOR
REMARK 3 S11: -0.2793 S12: -0.0294 S13: -0.0843
REMARK 3 S21: 0.0436 S22: 0.2058 S23: 0.4821
REMARK 3 S31: 0.6654 S32: -0.4440 S33: 0.0734
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 285 A 358
REMARK 3 ORIGIN FOR THE GROUP (A): -31.3918 38.9268 45.6360
REMARK 3 T TENSOR
REMARK 3 T11: -0.0427 T22: 0.3307
REMARK 3 T33: -0.4164 T12: -0.1193
REMARK 3 T13: 0.3374 T23: -0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 2.4951 L22: 3.3194
REMARK 3 L33: 0.4441 L12: -0.6065
REMARK 3 L13: 0.3838 L23: -0.7698
REMARK 3 S TENSOR
REMARK 3 S11: 0.2085 S12: -0.8981 S13: 0.0711
REMARK 3 S21: 1.1945 S22: -0.3134 S23: 0.8775
REMARK 3 S31: -0.2201 S32: -0.0435 S33: 0.1049
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 359 A 429
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4586 32.1417 54.0449
REMARK 3 T TENSOR
REMARK 3 T11: 0.2225 T22: 0.4949
REMARK 3 T33: -0.5561 T12: -0.0327
REMARK 3 T13: -0.0914 T23: 0.1198
REMARK 3 L TENSOR
REMARK 3 L11: 6.3173 L22: 2.4550
REMARK 3 L33: 2.3190 L12: 0.9172
REMARK 3 L13: 0.3057 L23: -1.9718
REMARK 3 S TENSOR
REMARK 3 S11: -0.1123 S12: -1.0285 S13: -0.6501
REMARK 3 S21: 1.1890 S22: -0.1390 S23: 0.2173
REMARK 3 S31: -0.0607 S32: 0.2428 S33: 0.2513
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 430 A 578
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1650 28.6782 40.8542
REMARK 3 T TENSOR
REMARK 3 T11: -0.1870 T22: 0.4437
REMARK 3 T33: -0.2040 T12: 0.0709
REMARK 3 T13: -0.2535 T23: 0.3029
REMARK 3 L TENSOR
REMARK 3 L11: 3.8650 L22: 3.2396
REMARK 3 L33: 2.2032 L12: -0.4213
REMARK 3 L13: -0.8703 L23: -0.8054
REMARK 3 S TENSOR
REMARK 3 S11: -0.0488 S12: -0.6221 S13: -0.8045
REMARK 3 S21: 0.7118 S22: -0.4804 S23: -0.6893
REMARK 3 S31: 0.3135 S32: 0.6945 S33: 0.5291
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 : A 579 A 671
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4401 50.6043 34.5202
REMARK 3 T TENSOR
REMARK 3 T11: -0.4269 T22: 0.0245
REMARK 3 T33: -0.4510 T12: -0.0664
REMARK 3 T13: -0.2087 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 4.6010 L22: 2.9450
REMARK 3 L33: 4.0397 L12: 0.3592
REMARK 3 L13: -0.6996 L23: -0.9449
REMARK 3 S TENSOR
REMARK 3 S11: 0.1409 S12: -0.5840 S13: 0.1558
REMARK 3 S21: 0.6780 S22: -0.4714 S23: -0.7382
REMARK 3 S31: -0.3247 S32: 0.6042 S33: 0.3305
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 : A 672 A 712
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3619 56.5813 26.4625
REMARK 3 T TENSOR
REMARK 3 T11: -0.4719 T22: -0.1377
REMARK 3 T33: -0.5048 T12: -0.0692
REMARK 3 T13: -0.2091 T23: -0.1071
REMARK 3 L TENSOR
REMARK 3 L11: 2.7149 L22: 4.6436
REMARK 3 L33: 5.1690 L12: -1.2967
REMARK 3 L13: -3.1660 L23: 1.3232
REMARK 3 S TENSOR
REMARK 3 S11: 0.3038 S12: -1.0178 S13: 0.1122
REMARK 3 S21: 0.1066 S22: -0.5408 S23: 0.0119
REMARK 3 S31: -0.7493 S32: 0.6824 S33: 0.2371
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 : A 713 A 766
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0419 46.2766 16.4535
REMARK 3 T TENSOR
REMARK 3 T11: -0.6969 T22: -0.1784
REMARK 3 T33: -0.3867 T12: 0.0814
REMARK 3 T13: -0.1135 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.5807 L22: 2.8040
REMARK 3 L33: 4.8711 L12: -0.6677
REMARK 3 L13: -1.7304 L23: -0.8205
REMARK 3 S TENSOR
REMARK 3 S11: 0.3121 S12: -0.5380 S13: 0.0116
REMARK 3 S21: -0.1609 S22: -0.5244 S23: -0.8219
REMARK 3 S31: 0.2275 S32: 0.8316 S33: 0.2123
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 40 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9534 84.5922 -9.0291
REMARK 3 T TENSOR
REMARK 3 T11: 0.2962 T22: 0.3951
REMARK 3 T33: 0.5222 T12: 0.0150
REMARK 3 T13: 0.0791 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 6.2421 L22: 1.3955
REMARK 3 L33: 4.2632 L12: -1.7145
REMARK 3 L13: 4.8270 L23: -0.6254
REMARK 3 S TENSOR
REMARK 3 S11: -0.3595 S12: -0.4202 S13: 1.7940
REMARK 3 S21: -0.1394 S22: -0.3607 S23: -0.1402
REMARK 3 S31: -1.1367 S32: -0.1716 S33: 0.7201
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 91 B 206
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5423 77.0707 -5.0900
REMARK 3 T TENSOR
REMARK 3 T11: -0.0743 T22: 0.0427
REMARK 3 T33: 0.1634 T12: 0.2925
REMARK 3 T13: -0.1642 T23: 0.1326
REMARK 3 L TENSOR
REMARK 3 L11: 2.9749 L22: 6.2752
REMARK 3 L33: 5.7828 L12: -1.1797
REMARK 3 L13: -0.3491 L23: -0.5695
REMARK 3 S TENSOR
REMARK 3 S11: 0.1013 S12: -0.1589 S13: 0.8494
REMARK 3 S21: -0.2626 S22: 0.3559 S23: 1.1545
REMARK 3 S31: -1.2241 S32: -0.7128 S33: -0.4572
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 207 B 284
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5903 61.8239 -7.2122
REMARK 3 T TENSOR
REMARK 3 T11: -0.3809 T22: 0.1292
REMARK 3 T33: -0.2033 T12: 0.0630
REMARK 3 T13: -0.3680 T23: 0.1390
REMARK 3 L TENSOR
REMARK 3 L11: 1.6185 L22: 4.2664
REMARK 3 L33: 6.3683 L12: -0.6392
REMARK 3 L13: 0.9225 L23: -3.5223
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: 0.3048 S13: 0.3530
REMARK 3 S21: -1.0912 S22: 0.3994 S23: 0.9280
REMARK 3 S31: -0.1533 S32: -1.0335 S33: -0.3585
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 : B 285 B 358
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5749 59.2817 -27.2619
REMARK 3 T TENSOR
REMARK 3 T11: 0.6465 T22: 0.5644
REMARK 3 T33: -0.2974 T12: -0.0628
REMARK 3 T13: -0.6418 T23: 0.1236
REMARK 3 L TENSOR
REMARK 3 L11: 1.7463 L22: 1.0365
REMARK 3 L33: 1.6581 L12: -0.5685
REMARK 3 L13: -1.6305 L23: 0.1908
REMARK 3 S TENSOR
REMARK 3 S11: -0.3995 S12: 1.1216 S13: 0.1345
REMARK 3 S21: -1.3086 S22: 0.2824 S23: 0.5993
REMARK 3 S31: 0.0528 S32: -1.0304 S33: 0.1172
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 : B 359 B 429
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9666 66.4176 -33.8861
REMARK 3 T TENSOR
REMARK 3 T11: 0.8919 T22: 0.2250
REMARK 3 T33: -0.5683 T12: -0.0939
REMARK 3 T13: -0.1223 T23: 0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 8.6484 L22: 4.3791
REMARK 3 L33: 3.3555 L12: -1.2202
REMARK 3 L13: 3.6198 L23: -3.2933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: 1.1131 S13: 0.1785
REMARK 3 S21: -1.4556 S22: 0.1307 S23: 0.2600
REMARK 3 S31: 0.2442 S32: -0.0569 S33: -0.0817
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 : B 430 B 578
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0059 70.3151 -18.7345
REMARK 3 T TENSOR
REMARK 3 T11: 0.2081 T22: 0.0662
REMARK 3 T33: -0.2305 T12: -0.1142
REMARK 3 T13: 0.2430 T23: 0.1219
REMARK 3 L TENSOR
REMARK 3 L11: 2.3982 L22: 2.3650
REMARK 3 L33: 2.9707 L12: -0.2541
REMARK 3 L13: 0.6037 L23: -0.7678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0691 S12: 0.5166 S13: 0.6179
REMARK 3 S21: -1.2172 S22: -0.1961 S23: -0.7653
REMARK 3 S31: -0.3712 S32: 0.7524 S33: 0.2653
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 : B 579 B 671
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2207 48.2966 -12.8706
REMARK 3 T TENSOR
REMARK 3 T11: -0.0272 T22: -0.2382
REMARK 3 T33: -0.4707 T12: 0.0749
REMARK 3 T13: 0.1842 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 4.9988 L22: 1.9563
REMARK 3 L33: 3.2458 L12: 0.4443
REMARK 3 L13: 0.5681 L23: -0.0980
REMARK 3 S TENSOR
REMARK 3 S11: -0.2445 S12: 0.2670 S13: -0.2274
REMARK 3 S21: -1.1611 S22: -0.1022 S23: -0.6845
REMARK 3 S31: 0.4474 S32: 0.4437 S33: 0.3467
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 : B 672 B 712
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4129 42.1724 -5.6045
REMARK 3 T TENSOR
REMARK 3 T11: -0.2445 T22: -0.3241
REMARK 3 T33: -0.5484 T12: 0.0237
REMARK 3 T13: 0.1756 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 9.3972 L22: 4.8651
REMARK 3 L33: 4.7716 L12: -1.0500
REMARK 3 L13: 2.4072 L23: 0.7045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.7419 S13: -0.6649
REMARK 3 S21: -0.7937 S22: -0.2254 S23: -0.1710
REMARK 3 S31: 0.7761 S32: 0.3423 S33: 0.2402
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 : B 713 B 766
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6032 52.6748 5.2342
REMARK 3 T TENSOR
REMARK 3 T11: -0.6175 T22: -0.0843
REMARK 3 T33: -0.4714 T12: 0.1106
REMARK 3 T13: -0.0086 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.8101 L22: 5.0768
REMARK 3 L33: 3.3640 L12: 1.0978
REMARK 3 L13: -1.0401 L23: -0.2739
REMARK 3 S TENSOR
REMARK 3 S11: 0.2788 S12: -0.3880 S13: -0.0385
REMARK 3 S21: -0.2498 S22: -0.4266 S23: -0.7308
REMARK 3 S31: 0.1273 S32: 0.8514 S33: 0.1477
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4PV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32631
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.240
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 FOR THE DATA SET : 29.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : 1.00000
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 2000, 0.1M BICINE, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 191.17067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 95.58533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 4360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 ASP A 21
REMARK 465 TYR A 22
REMARK 465 ASP A 23
REMARK 465 ILE A 24
REMARK 465 PRO A 25
REMARK 465 THR A 26
REMARK 465 THR A 27
REMARK 465 GLU A 28
REMARK 465 ASN A 29
REMARK 465 LEU A 30
REMARK 465 TYR A 31
REMARK 465 PHE A 32
REMARK 465 GLN A 33
REMARK 465 GLY A 34
REMARK 465 ALA A 35
REMARK 465 MET A 36
REMARK 465 GLY A 37
REMARK 465 SER A 38
REMARK 465 SER A 39
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 HIS B 20
REMARK 465 ASP B 21
REMARK 465 TYR B 22
REMARK 465 ASP B 23
REMARK 465 ILE B 24
REMARK 465 PRO B 25
REMARK 465 THR B 26
REMARK 465 THR B 27
REMARK 465 GLU B 28
REMARK 465 ASN B 29
REMARK 465 LEU B 30
REMARK 465 TYR B 31
REMARK 465 PHE B 32
REMARK 465 GLN B 33
REMARK 465 GLY B 34
REMARK 465 ALA B 35
REMARK 465 MET B 36
REMARK 465 GLY B 37
REMARK 465 SER B 38
REMARK 465 SER B 39
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 40 CG CD NE CZ NH1 NH2
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 64 -145.78 -118.47
REMARK 500 HIS A 66 11.32 -156.26
REMARK 500 GLU A 73 -59.34 57.87
REMARK 500 GLN A 123 -97.26 -107.88
REMARK 500 TRP A 124 -150.32 -99.23
REMARK 500 HIS A 162 38.68 -159.13
REMARK 500 ASN A 169 56.56 33.23
REMARK 500 ILE A 193 -58.58 -128.88
REMARK 500 VAL A 207 -63.04 -103.37
REMARK 500 SER A 242 -162.93 62.45
REMARK 500 SER A 275 49.58 -106.86
REMARK 500 ILE A 295 -18.76 -46.68
REMARK 500 GLN A 320 45.26 -74.88
REMARK 500 ALA A 342 0.82 -63.55
REMARK 500 ALA A 409 144.33 -174.29
REMARK 500 ASN A 450 79.46 -151.90
REMARK 500 GLN A 455 -10.75 -140.55
REMARK 500 ASP A 488 9.26 55.86
REMARK 500 GLN A 508 97.61 -69.69
REMARK 500 ASN A 520 54.71 35.66
REMARK 500 ASN A 562 -168.27 -127.10
REMARK 500 ARG A 596 14.47 51.55
REMARK 500 THR A 600 -97.53 -131.94
REMARK 500 SER A 630 -104.39 64.30
REMARK 500 ALA A 654 62.03 33.76
REMARK 500 ASP A 678 -85.37 -112.75
REMARK 500 ASN A 679 16.71 -147.16
REMARK 500 ASN A 710 -79.32 -79.59
REMARK 500 ASP A 737 -0.75 64.80
REMARK 500 ASP A 739 -147.22 -99.40
REMARK 500 ILE A 742 50.30 37.23
REMARK 500 SER B 64 -145.77 -119.08
REMARK 500 HIS B 66 10.74 -156.97
REMARK 500 GLU B 73 -59.40 57.67
REMARK 500 SER B 93 4.33 -69.73
REMARK 500 GLN B 123 -94.93 -107.96
REMARK 500 TRP B 124 -145.22 -100.31
REMARK 500 HIS B 162 36.47 -159.46
REMARK 500 ASN B 169 55.08 34.74
REMARK 500 ILE B 193 -57.86 -129.98
REMARK 500 VAL B 207 -64.37 -103.06
REMARK 500 SER B 242 -164.11 62.60
REMARK 500 SER B 275 47.52 -106.96
REMARK 500 GLN B 320 47.12 -76.38
REMARK 500 ALA B 342 2.49 -61.45
REMARK 500 ILE B 389 -39.96 -37.08
REMARK 500 ALA B 409 146.53 -173.34
REMARK 500 ASN B 450 79.18 -152.82
REMARK 500 GLN B 455 -8.81 -142.80
REMARK 500 ASP B 488 7.23 55.07
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CJP A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CJP B 1000
DBREF 4PV7 A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4PV7 B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 4PV7 HIS A 15 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS A 16 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS A 17 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS A 18 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS A 19 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS A 20 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ASP A 21 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 TYR A 22 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ASP A 23 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ILE A 24 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 PRO A 25 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 THR A 26 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 THR A 27 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLU A 28 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ASN A 29 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 LEU A 30 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 TYR A 31 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 PHE A 32 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLN A 33 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLY A 34 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ALA A 35 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 MET A 36 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLY A 37 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 SER A 38 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS B 15 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS B 16 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS B 17 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS B 18 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS B 19 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 HIS B 20 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ASP B 21 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 TYR B 22 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ASP B 23 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ILE B 24 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 PRO B 25 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 THR B 26 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 THR B 27 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLU B 28 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ASN B 29 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 LEU B 30 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 TYR B 31 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 PHE B 32 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLN B 33 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLY B 34 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 ALA B 35 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 MET B 36 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 GLY B 37 UNP P27487 EXPRESSION TAG
SEQADV 4PV7 SER B 38 UNP P27487 EXPRESSION TAG
SEQRES 1 A 752 HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR
SEQRES 2 A 752 GLU ASN LEU TYR PHE GLN GLY ALA MET GLY SER SER ARG
SEQRES 3 A 752 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 4 A 752 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 5 A 752 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 6 A 752 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 7 A 752 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 8 A 752 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 9 A 752 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 10 A 752 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 11 A 752 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 12 A 752 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 13 A 752 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 14 A 752 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 15 A 752 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 16 A 752 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 17 A 752 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 18 A 752 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 19 A 752 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 20 A 752 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 21 A 752 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 22 A 752 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 23 A 752 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 24 A 752 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 25 A 752 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 26 A 752 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 27 A 752 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 28 A 752 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 29 A 752 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 30 A 752 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 31 A 752 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 32 A 752 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 33 A 752 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 34 A 752 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 35 A 752 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 36 A 752 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 37 A 752 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 38 A 752 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 39 A 752 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 40 A 752 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 41 A 752 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 42 A 752 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 43 A 752 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 44 A 752 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 45 A 752 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 46 A 752 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 47 A 752 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 48 A 752 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 49 A 752 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 50 A 752 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 51 A 752 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 52 A 752 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 53 A 752 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 54 A 752 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 55 A 752 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 56 A 752 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 57 A 752 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 58 A 752 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 752 HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR
SEQRES 2 B 752 GLU ASN LEU TYR PHE GLN GLY ALA MET GLY SER SER ARG
SEQRES 3 B 752 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 4 B 752 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 5 B 752 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 6 B 752 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 7 B 752 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 8 B 752 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 9 B 752 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 10 B 752 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 11 B 752 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 12 B 752 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 13 B 752 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 14 B 752 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 15 B 752 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 16 B 752 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 17 B 752 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 18 B 752 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 19 B 752 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 20 B 752 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 21 B 752 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 22 B 752 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 23 B 752 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 24 B 752 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 25 B 752 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 26 B 752 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 27 B 752 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 28 B 752 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 29 B 752 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 30 B 752 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 31 B 752 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 32 B 752 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 33 B 752 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 34 B 752 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 35 B 752 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 36 B 752 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 37 B 752 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 38 B 752 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 39 B 752 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 40 B 752 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 41 B 752 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 42 B 752 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 43 B 752 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 44 B 752 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 45 B 752 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 46 B 752 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 47 B 752 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 48 B 752 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 49 B 752 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 50 B 752 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 51 B 752 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 52 B 752 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 53 B 752 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 54 B 752 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 55 B 752 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 56 B 752 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 57 B 752 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 58 B 752 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET CJP A1000 23
HET CJP B1000 23
HETNAM CJP 1-[2-(2,4-DICHLOROPHENYL)-1-(METHYLSULFONYL)-1H-INDOL-
HETNAM 2 CJP 3-YL]METHANAMINE
FORMUL 3 CJP 2(C16 H14 CL2 N2 O2 S)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 GLU A 91 ASP A 96 5 6
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 ASP A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 LEU A 340 GLN A 344 5 5
HELIX 7 7 GLU A 421 MET A 425 5 5
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 ASN A 562 ASN A 572 1 11
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 ASN A 685 1 7
HELIX 17 17 SER A 686 THR A 687 5 2
HELIX 18 18 VAL A 688 VAL A 698 5 11
HELIX 19 19 HIS A 712 VAL A 726 1 15
HELIX 20 20 SER A 744 PHE A 763 1 20
HELIX 21 21 THR B 44 LYS B 50 1 7
HELIX 22 22 GLU B 91 ASP B 96 5 6
HELIX 23 23 ASP B 200 VAL B 207 1 8
HELIX 24 24 ASP B 274 LEU B 276 5 3
HELIX 25 25 PRO B 290 ILE B 295 1 6
HELIX 26 26 LEU B 340 GLN B 344 5 5
HELIX 27 27 GLU B 421 MET B 425 5 5
HELIX 28 28 ASN B 497 GLN B 505 1 9
HELIX 29 29 ASN B 562 ASN B 572 1 11
HELIX 30 30 GLY B 587 HIS B 592 1 6
HELIX 31 31 ALA B 593 ASN B 595 5 3
HELIX 32 32 THR B 600 LYS B 615 1 16
HELIX 33 33 SER B 630 GLY B 641 1 12
HELIX 34 34 ARG B 658 TYR B 662 5 5
HELIX 35 35 ASP B 663 GLY B 672 1 10
HELIX 36 36 ASN B 679 ASN B 685 1 7
HELIX 37 37 SER B 686 THR B 687 5 2
HELIX 38 38 VAL B 688 VAL B 698 5 11
HELIX 39 39 HIS B 712 VAL B 726 1 15
HELIX 40 40 SER B 744 PHE B 763 1 20
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 LEU A 60 TRP A 62 0
SHEET 2 B 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 B 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 C 4 ILE A 102 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O VAL A 271 N LEU A 223
SHEET 4 F 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 H 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 ARG A 336 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 I 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 I 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O CYS A 385 N LYS A 373
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 L 4 GLY A 490 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 LEU B 60 TRP B 62 0
SHEET 2 O 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 O 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 P 4 ILE B 102 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O ASP B 133 N LEU B 116
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 S 4 ILE B 285 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 U 4 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 V 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 V 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 Y 4 GLY B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O TYR B 526 N ASP B 515
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 544
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.04
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.05
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
CISPEP 1 GLY A 474 PRO A 475 0 4.97
CISPEP 2 GLY B 474 PRO B 475 0 2.33
SITE 1 AC1 10 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 10 SER A 630 VAL A 656 TYR A 662 TYR A 666
SITE 3 AC1 10 ASN A 710 HIS A 740
SITE 1 AC2 9 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 AC2 9 SER B 630 VAL B 656 TYR B 662 TYR B 666
SITE 3 AC2 9 HIS B 740
CRYST1 79.815 79.815 286.756 90.00 90.00 120.00 P 32 6
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 0.012529 0.007234 0.000000 0.00000
SCALE2 0.000000 0.014467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003487 0.00000
TER 5952 PRO A 766
TER 11904 PRO B 766
MASTER 713 0 2 40 102 0 6 611948 2 66 116
END |