HEADER CHAPERONE 27-AUG-10 3OMU
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF AN HSP90 FROM
TITLE 2 TRYPANOSOMA BRUCEI, TB10.26.1080 IN THE PRESENCE OF A
TITLE 3 THIENOPYRIMIDINE DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN 83;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 GENE: TB10.26.1080;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS HSP90, TRYPANOSOMA BRUCEII, STRUCTURAL GENOMICS, DRUG DISCOVERY,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,A.HUTCHINSON,H.SULLIVAN,J.WEADGE,D.COSSAR,Y.LI,
AUTHOR 2 I.KOZIERADZKI,A.BOCHKAREV,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 3 J.WEIGELT,P.G.WYATT,A.H.FAIRLAMB,C.MACKENZIE,M.A.J.FERGUSON,R.HUI,
AUTHOR 4 J.C.PIZARRO,T.HILLS,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-SEP-23 3OMU 1 REMARK SEQADV
REVDAT 3 29-NOV-17 3OMU 1 JRNL
REVDAT 2 08-NOV-17 3OMU 1 REMARK
REVDAT 1 27-OCT-10 3OMU 0
JRNL AUTH J.C.PIZARRO,T.HILLS,G.SENISTERRA,A.K.WERNIMONT,C.MACKENZIE,
JRNL AUTH 2 N.R.NORCROSS,M.A.FERGUSON,P.G.WYATT,I.H.GILBERT,R.HUI
JRNL TITL EXPLORING THE TRYPANOSOMA BRUCEI HSP83 POTENTIAL AS A TARGET
JRNL TITL 2 FOR STRUCTURE GUIDED DRUG DESIGN.
JRNL REF PLOS NEGL TROP DIS V. 7 E2492 2013
JRNL REFN ESSN 1935-2735
JRNL PMID 24147171
JRNL DOI 10.1371/JOURNAL.PNTD.0002492
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 25447
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1298
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1675
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3108
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.44000
REMARK 3 B22 (A**2) : 1.20000
REMARK 3 B33 (A**2) : 1.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.224
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.683
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3286 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4455 ; 1.236 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 418 ; 5.517 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;37.388 ;24.830
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 554 ;14.404 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;16.939 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 507 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2481 ; 0.005 ; 0.020
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): 2055 ; 0.370 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3297 ; 0.712 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1231 ; 1.208 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1158 ; 1.981 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3640 -2.5739 5.9843
REMARK 3 T TENSOR
REMARK 3 T11: 0.2887 T22: 0.2960
REMARK 3 T33: 0.3162 T12: -0.0132
REMARK 3 T13: -0.0090 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 2.3995 L22: 0.6636
REMARK 3 L33: 1.8890 L12: 0.3261
REMARK 3 L13: 0.4489 L23: 0.0947
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: 0.0075 S13: 0.0234
REMARK 3 S21: -0.0275 S22: -0.0662 S23: 0.0610
REMARK 3 S31: -0.0333 S32: -0.1266 S33: 0.0308
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 47 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8678 -5.7346 21.3703
REMARK 3 T TENSOR
REMARK 3 T11: 0.2893 T22: 0.4977
REMARK 3 T33: 0.3430 T12: -0.0845
REMARK 3 T13: 0.0655 T23: 0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 2.6002 L22: 2.0156
REMARK 3 L33: 6.5907 L12: 0.5051
REMARK 3 L13: 1.5763 L23: 3.5784
REMARK 3 S TENSOR
REMARK 3 S11: 0.1121 S12: -0.6638 S13: -0.0301
REMARK 3 S21: -0.0728 S22: -0.1149 S23: 0.0808
REMARK 3 S31: -0.0848 S32: -0.3951 S33: 0.0028
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 74 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5885 3.1025 9.2630
REMARK 3 T TENSOR
REMARK 3 T11: 0.3078 T22: 0.3255
REMARK 3 T33: 0.3526 T12: 0.0136
REMARK 3 T13: 0.0042 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 3.2222 L22: 0.5569
REMARK 3 L33: 0.6951 L12: -0.1337
REMARK 3 L13: -0.1012 L23: 0.5961
REMARK 3 S TENSOR
REMARK 3 S11: 0.1538 S12: -0.1937 S13: 0.5081
REMARK 3 S21: -0.0258 S22: -0.1374 S23: 0.0758
REMARK 3 S31: -0.0367 S32: -0.1070 S33: -0.0165
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 104 A 152
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7236 -1.2419 4.7121
REMARK 3 T TENSOR
REMARK 3 T11: 0.3008 T22: 0.2619
REMARK 3 T33: 0.3160 T12: 0.0043
REMARK 3 T13: 0.0022 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 2.3914 L22: 1.6256
REMARK 3 L33: 1.4163 L12: -0.1949
REMARK 3 L13: -0.3048 L23: 0.4366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0674 S12: 0.0819 S13: 0.1181
REMARK 3 S21: -0.0781 S22: -0.0852 S23: 0.0811
REMARK 3 S31: -0.0503 S32: -0.0879 S33: 0.0178
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 153 A 188
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9435 -9.2418 6.9569
REMARK 3 T TENSOR
REMARK 3 T11: 0.2771 T22: 0.3531
REMARK 3 T33: 0.3460 T12: -0.0306
REMARK 3 T13: -0.0209 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.5735 L22: 1.6597
REMARK 3 L33: 0.9436 L12: 1.1708
REMARK 3 L13: 0.1225 L23: 0.0391
REMARK 3 S TENSOR
REMARK 3 S11: 0.0916 S12: -0.1158 S13: -0.1731
REMARK 3 S21: -0.0184 S22: -0.0398 S23: 0.1172
REMARK 3 S31: 0.1415 S32: -0.3342 S33: -0.0518
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 189 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8076 -15.2016 19.1382
REMARK 3 T TENSOR
REMARK 3 T11: 0.3573 T22: 0.3281
REMARK 3 T33: 0.3158 T12: -0.1133
REMARK 3 T13: -0.0311 T23: 0.1900
REMARK 3 L TENSOR
REMARK 3 L11: 4.8849 L22: 6.4667
REMARK 3 L33: 4.2498 L12: 0.7668
REMARK 3 L13: 1.5389 L23: 4.8432
REMARK 3 S TENSOR
REMARK 3 S11: 0.3543 S12: -0.7546 S13: -0.4552
REMARK 3 S21: 0.2171 S22: -0.0102 S23: -0.3214
REMARK 3 S31: 0.2662 S32: -0.1542 S33: -0.3440
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 15
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0874 18.8435 9.2664
REMARK 3 T TENSOR
REMARK 3 T11: 0.3915 T22: 0.2612
REMARK 3 T33: 0.4187 T12: -0.0713
REMARK 3 T13: 0.0310 T23: 0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 4.4510 L22: 1.9402
REMARK 3 L33: 4.5870 L12: 2.9184
REMARK 3 L13: -2.2738 L23: -1.7150
REMARK 3 S TENSOR
REMARK 3 S11: -0.2150 S12: 0.1812 S13: 0.2358
REMARK 3 S21: -0.2121 S22: 0.1702 S23: 0.1326
REMARK 3 S31: 0.2170 S32: -0.2543 S33: 0.0448
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 16 B 33
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1770 16.5431 26.1013
REMARK 3 T TENSOR
REMARK 3 T11: 0.2960 T22: 0.7801
REMARK 3 T33: 0.3811 T12: -0.0382
REMARK 3 T13: 0.0600 T23: -0.1572
REMARK 3 L TENSOR
REMARK 3 L11: 4.2921 L22: 2.2578
REMARK 3 L33: 4.9434 L12: -2.9228
REMARK 3 L13: 1.8375 L23: -0.5443
REMARK 3 S TENSOR
REMARK 3 S11: -0.4226 S12: -0.3760 S13: 0.5364
REMARK 3 S21: 0.3596 S22: 0.0140 S23: -0.1918
REMARK 3 S31: -0.1841 S32: 0.1562 S33: 0.4087
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 34 B 53
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9620 -6.6333 17.1547
REMARK 3 T TENSOR
REMARK 3 T11: 0.3332 T22: 0.3133
REMARK 3 T33: 0.5731 T12: -0.0584
REMARK 3 T13: 0.0876 T23: 0.1303
REMARK 3 L TENSOR
REMARK 3 L11: 3.4120 L22: 7.6240
REMARK 3 L33: 2.8582 L12: -0.7254
REMARK 3 L13: 0.2504 L23: 4.0772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: -0.4444 S13: -1.0069
REMARK 3 S21: 0.2522 S22: -0.1440 S23: 0.0782
REMARK 3 S31: 0.1968 S32: -0.1843 S33: 0.1076
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 54 B 73
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6585 0.3697 27.7291
REMARK 3 T TENSOR
REMARK 3 T11: 1.2718 T22: 1.0572
REMARK 3 T33: 0.6536 T12: 0.1146
REMARK 3 T13: -0.2469 T23: 0.6531
REMARK 3 L TENSOR
REMARK 3 L11: 10.0117 L22: 9.5345
REMARK 3 L33: 3.9015 L12: -4.7374
REMARK 3 L13: 2.6427 L23: 1.3204
REMARK 3 S TENSOR
REMARK 3 S11: -0.6874 S12: -2.8883 S13: -1.3064
REMARK 3 S21: 2.3507 S22: 0.9278 S23: -0.8795
REMARK 3 S31: 1.0319 S32: -0.2813 S33: -0.2404
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 74 B 117
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5837 10.7955 15.1495
REMARK 3 T TENSOR
REMARK 3 T11: 0.3590 T22: 0.2904
REMARK 3 T33: 0.3165 T12: 0.0014
REMARK 3 T13: 0.0301 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 5.2969 L22: 1.4102
REMARK 3 L33: 0.4759 L12: -0.4527
REMARK 3 L13: 0.3379 L23: 0.5820
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: -0.1134 S13: 0.3599
REMARK 3 S21: -0.1458 S22: -0.0336 S23: 0.0542
REMARK 3 S31: -0.0543 S32: -0.1321 S33: 0.0191
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 118 B 150
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3213 9.9173 17.5235
REMARK 3 T TENSOR
REMARK 3 T11: 0.3467 T22: 0.3209
REMARK 3 T33: 0.2614 T12: 0.0062
REMARK 3 T13: -0.0095 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 6.6186 L22: 3.0686
REMARK 3 L33: 0.5846 L12: -1.1933
REMARK 3 L13: -1.3384 L23: 0.6735
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.2985 S13: 0.2692
REMARK 3 S21: -0.0580 S22: 0.0675 S23: -0.1679
REMARK 3 S31: -0.1102 S32: -0.0131 S33: -0.0828
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 154 B 177
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8328 8.7626 19.5630
REMARK 3 T TENSOR
REMARK 3 T11: 0.3158 T22: 0.3397
REMARK 3 T33: 0.3124 T12: -0.0140
REMARK 3 T13: 0.0015 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 3.8459 L22: 3.0290
REMARK 3 L33: 0.9567 L12: -0.2025
REMARK 3 L13: -0.3001 L23: 0.1041
REMARK 3 S TENSOR
REMARK 3 S11: -0.0652 S12: -0.6079 S13: 0.0985
REMARK 3 S21: -0.1045 S22: 0.0262 S23: -0.4217
REMARK 3 S31: 0.0555 S32: 0.1776 S33: 0.0390
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 178 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7194 5.9355 34.4959
REMARK 3 T TENSOR
REMARK 3 T11: 0.4406 T22: 0.8053
REMARK 3 T33: 0.0470 T12: 0.0573
REMARK 3 T13: 0.0949 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 7.7208 L22: 13.4490
REMARK 3 L33: 3.8114 L12: 1.7319
REMARK 3 L13: 0.8789 L23: 7.1413
REMARK 3 S TENSOR
REMARK 3 S11: -0.4000 S12: -1.8869 S13: -0.1021
REMARK 3 S21: 0.1039 S22: 0.4422 S23: -0.1108
REMARK 3 S31: 0.1058 S32: 0.1759 S33: -0.0422
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 RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3OMU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061314.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25590
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.72400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 3O6O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350 0.2 M AMMONIUM ACETATE
REMARK 280 0.1 M HEPES PH 7.5 4 MM MGCL2 2 MM TCEP 2 MM DDU101329, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 30.02200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.49800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.47050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.49800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.02200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.47050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 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 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 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 -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 ARG A -6
REMARK 465 GLU A -5
REMARK 465 ASN A -4
REMARK 465 LEU A -3
REMARK 465 TYR A -2
REMARK 465 PHE A -1
REMARK 465 GLN A 0
REMARK 465 GLU A 209
REMARK 465 ASN A 210
REMARK 465 THR A 211
REMARK 465 THR A 212
REMARK 465 GLU A 213
REMARK 465 LYS A 214
REMARK 465 MET B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 ARG B -6
REMARK 465 GLU B -5
REMARK 465 ASN B -4
REMARK 465 LEU B -3
REMARK 465 TYR B -2
REMARK 465 PHE B -1
REMARK 465 GLN B 0
REMARK 465 GLY B 1
REMARK 465 GLU B 59
REMARK 465 PRO B 60
REMARK 465 SER B 151
REMARK 465 ALA B 152
REMARK 465 GLY B 153
REMARK 465 GLU B 198
REMARK 465 PHE B 199
REMARK 465 VAL B 208
REMARK 465 GLU B 209
REMARK 465 ASN B 210
REMARK 465 THR B 211
REMARK 465 THR B 212
REMARK 465 GLU B 213
REMARK 465 LYS B 214
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 MET A 2 CG SD CE
REMARK 470 SER A 54 OG
REMARK 470 VAL A 55 CG1 CG2
REMARK 470 ASP A 58 CG OD1 OD2
REMARK 470 ARG A 98 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 102 CE NZ
REMARK 470 GLU A 178 CG CD OE1 OE2
REMARK 470 LYS A 190 CD CE NZ
REMARK 470 LYS A 194 CD CE NZ
REMARK 470 GLU A 198 CG CD OE1 OE2
REMARK 470 THR B 3 OG1 CG2
REMARK 470 ILE B 20 CG1 CG2 CD1
REMARK 470 THR B 22 OG1 CG2
REMARK 470 PHE B 23 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 44 CE NZ
REMARK 470 GLN B 53 CD OE1 NE2
REMARK 470 ASP B 58 CG OD1 OD2
REMARK 470 ARG B 70 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 71 CG1 CG2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 GLU B 109 CG CD OE1 OE2
REMARK 470 GLU B 149 CG CD OE1 OE2
REMARK 470 LYS B 167 CG CD CE NZ
REMARK 470 HIS B 175 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 186 CG CD OE1 OE2
REMARK 470 ARG B 187 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 190 CG CD CE NZ
REMARK 470 LYS B 194 CG CD CE NZ
REMARK 470 SER B 197 OG
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 ASN A 26 59.98 -112.39
REMARK 500 ASN A 52 -52.54 -132.17
REMARK 500 GLN A 53 -46.60 78.15
REMARK 500 ASN B 26 64.36 -100.29
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 IBD A 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IBD B 215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O6O RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH ALTERNATE INHIBITOR
DBREF 3OMU A 2 214 UNP Q389P1 Q389P1_9TRYP 1 213
DBREF 3OMU B 2 214 UNP Q389P1 Q389P1_9TRYP 1 213
SEQADV 3OMU MET A -16 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS A -15 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS A -14 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS A -13 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS A -12 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS A -11 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS A -10 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU SER A -9 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU SER A -8 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLY A -7 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU ARG A -6 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLU A -5 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU ASN A -4 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU LEU A -3 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU TYR A -2 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU PHE A -1 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLN A 0 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLY A 1 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU MET B -16 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS B -15 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS B -14 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS B -13 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS B -12 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS B -11 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU HIS B -10 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU SER B -9 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU SER B -8 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLY B -7 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU ARG B -6 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLU B -5 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU ASN B -4 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU LEU B -3 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU TYR B -2 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU PHE B -1 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLN B 0 UNP Q389P1 EXPRESSION TAG
SEQADV 3OMU GLY B 1 UNP Q389P1 EXPRESSION TAG
SEQRES 1 A 231 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 231 LEU TYR PHE GLN GLY MET THR GLU THR PHE ALA PHE GLN
SEQRES 3 A 231 ALA GLU ILE ASN GLN LEU MET SER LEU ILE ILE ASN THR
SEQRES 4 A 231 PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE
SEQRES 5 A 231 SER ASN SER SER ASP ALA CYS ASP LYS ILE ARG TYR GLN
SEQRES 6 A 231 SER LEU THR ASN GLN SER VAL LEU GLY ASP GLU PRO HIS
SEQRES 7 A 231 LEU ARG ILE ARG VAL ILE PRO ASP ARG VAL ASN LYS THR
SEQRES 8 A 231 LEU THR VAL GLU ASP SER GLY ILE GLY MET THR LYS ALA
SEQRES 9 A 231 ASP LEU VAL ASN ASN LEU GLY THR ILE ALA ARG SER GLY
SEQRES 10 A 231 THR LYS SER PHE MET GLU ALA LEU GLU ALA GLY GLY ASP
SEQRES 11 A 231 MET SER MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER
SEQRES 12 A 231 ALA TYR LEU VAL ALA ASP ARG VAL THR VAL VAL SER LYS
SEQRES 13 A 231 ASN ASN GLU ASP ASP ALA TYR THR TRP GLU SER SER ALA
SEQRES 14 A 231 GLY GLY THR PHE THR VAL THR SER THR PRO ASP CYS ASP
SEQRES 15 A 231 LEU LYS ARG GLY THR ARG ILE VAL LEU HIS LEU LYS GLU
SEQRES 16 A 231 ASP GLN GLN GLU TYR LEU GLU GLU ARG ARG LEU LYS ASP
SEQRES 17 A 231 LEU ILE LYS LYS HIS SER GLU PHE ILE GLY TYR ASP ILE
SEQRES 18 A 231 GLU LEU MET VAL GLU ASN THR THR GLU LYS
SEQRES 1 B 231 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 B 231 LEU TYR PHE GLN GLY MET THR GLU THR PHE ALA PHE GLN
SEQRES 3 B 231 ALA GLU ILE ASN GLN LEU MET SER LEU ILE ILE ASN THR
SEQRES 4 B 231 PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE
SEQRES 5 B 231 SER ASN SER SER ASP ALA CYS ASP LYS ILE ARG TYR GLN
SEQRES 6 B 231 SER LEU THR ASN GLN SER VAL LEU GLY ASP GLU PRO HIS
SEQRES 7 B 231 LEU ARG ILE ARG VAL ILE PRO ASP ARG VAL ASN LYS THR
SEQRES 8 B 231 LEU THR VAL GLU ASP SER GLY ILE GLY MET THR LYS ALA
SEQRES 9 B 231 ASP LEU VAL ASN ASN LEU GLY THR ILE ALA ARG SER GLY
SEQRES 10 B 231 THR LYS SER PHE MET GLU ALA LEU GLU ALA GLY GLY ASP
SEQRES 11 B 231 MET SER MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER
SEQRES 12 B 231 ALA TYR LEU VAL ALA ASP ARG VAL THR VAL VAL SER LYS
SEQRES 13 B 231 ASN ASN GLU ASP ASP ALA TYR THR TRP GLU SER SER ALA
SEQRES 14 B 231 GLY GLY THR PHE THR VAL THR SER THR PRO ASP CYS ASP
SEQRES 15 B 231 LEU LYS ARG GLY THR ARG ILE VAL LEU HIS LEU LYS GLU
SEQRES 16 B 231 ASP GLN GLN GLU TYR LEU GLU GLU ARG ARG LEU LYS ASP
SEQRES 17 B 231 LEU ILE LYS LYS HIS SER GLU PHE ILE GLY TYR ASP ILE
SEQRES 18 B 231 GLU LEU MET VAL GLU ASN THR THR GLU LYS
HET IBD A 215 31
HET IBD B 215 31
HETNAM IBD 2-AMINO-4-{2,4-DICHLORO-5-[2-(DIETHYLAMINO)
HETNAM 2 IBD ETHOXY]PHENYL}-N-ETHYLTHIENO[2,3-D]PYRIMIDINE-6-
HETNAM 3 IBD CARBOXAMIDE
FORMUL 3 IBD 2(C21 H25 CL2 N5 O2 S)
FORMUL 5 HOH *96(H2 O)
HELIX 1 1 GLN A 9 THR A 22 1 14
HELIX 2 2 GLU A 28 ASN A 52 1 25
HELIX 3 3 THR A 85 GLY A 94 1 10
HELIX 4 4 ILE A 96 ALA A 110 1 15
HELIX 5 5 ASP A 113 GLY A 121 5 9
HELIX 6 6 VAL A 122 LEU A 129 5 8
HELIX 7 7 GLU A 178 LEU A 184 5 7
HELIX 8 8 GLU A 185 GLU A 198 1 14
HELIX 9 9 GLN B 9 THR B 22 1 14
HELIX 10 10 GLU B 28 ASN B 52 1 25
HELIX 11 11 GLN B 53 GLY B 57 5 5
HELIX 12 12 THR B 85 GLY B 94 1 10
HELIX 13 13 ILE B 96 GLU B 109 1 14
HELIX 14 14 ASP B 113 GLY B 121 5 9
HELIX 15 15 VAL B 122 LEU B 129 5 8
HELIX 16 16 GLN B 180 LEU B 184 5 5
HELIX 17 17 GLU B 185 LYS B 195 1 11
SHEET 1 A 8 THR A 3 ALA A 7 0
SHEET 2 A 8 THR A 155 SER A 160 -1 O PHE A 156 N PHE A 6
SHEET 3 A 8 TYR A 146 SER A 150 -1 N THR A 147 O THR A 159
SHEET 4 A 8 ALA A 131 LYS A 139 -1 N VAL A 136 O TRP A 148
SHEET 5 A 8 GLY A 169 LEU A 176 -1 O VAL A 173 N THR A 135
SHEET 6 A 8 THR A 74 ASP A 79 -1 N LEU A 75 O LEU A 174
SHEET 7 A 8 ARG A 63 ASP A 69 -1 N ARG A 65 O GLU A 78
SHEET 8 A 8 ASP A 203 LEU A 206 1 O GLU A 205 N ILE A 64
SHEET 1 B 8 THR B 3 ALA B 7 0
SHEET 2 B 8 THR B 155 SER B 160 -1 O PHE B 156 N PHE B 6
SHEET 3 B 8 TYR B 146 GLU B 149 -1 N GLU B 149 O THR B 157
SHEET 4 B 8 ALA B 131 LYS B 139 -1 N VAL B 136 O TRP B 148
SHEET 5 B 8 GLY B 169 LEU B 176 -1 O ARG B 171 N VAL B 137
SHEET 6 B 8 THR B 74 ASP B 79 -1 N LEU B 75 O LEU B 174
SHEET 7 B 8 ARG B 63 ASP B 69 -1 N ARG B 65 O GLU B 78
SHEET 8 B 8 ASP B 203 LEU B 206 1 O GLU B 205 N ILE B 64
SSBOND 1 CYS A 164 CYS B 164 1555 1455 2.94
SITE 1 AC1 18 SER A 38 ALA A 41 ASP A 79 ILE A 82
SITE 2 AC1 18 GLY A 83 MET A 84 ASP A 88 ASN A 92
SITE 3 AC1 18 GLY A 121 PHE A 124 THR A 170 HOH A 218
SITE 4 AC1 18 HOH A 227 HOH A 236 HOH A 268 GLN B 119
SITE 5 AC1 18 PHE B 120 GLY B 121
SITE 1 AC2 19 GLN A 119 PHE A 120 GLY A 121 ALA B 41
SITE 2 AC2 19 ASP B 79 GLY B 83 MET B 84 ASP B 88
SITE 3 AC2 19 ASN B 92 LEU B 93 ILE B 96 GLY B 121
SITE 4 AC2 19 PHE B 124 THR B 170 HOH B 218 HOH B 219
SITE 5 AC2 19 HOH B 221 HOH B 227 HOH B 230
CRYST1 60.044 60.941 126.996 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016409 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007874 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
