HEADER TRANSFERASE 08-MAY-12 4F36
TITLE CRYSTAL STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE B FROM TRYPANOSOMA
TITLE 2 BRUCEI, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOSIDE DIPHOSPHATE KINASE;
COMPND 3 CHAIN: A, C, B, D, E, F;
COMPND 4 SYNONYM: NUCLEOSIDE DIPHOSPHATE KINASE B;
COMPND 5 EC: 2.7.4.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;
SOURCE 3 ORGANISM_TAXID: 999953;
SOURCE 4 STRAIN: 927/4 GUTAT10.1;
SOURCE 5 GENE: TB11.01.7800;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS SSGCID, NIH, NIAID, SBRI, EMERALD BIOSTRUCTURES, STRUCTURAL GENOMICS,
KEYWDS 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 13-SEP-23 4F36 1 REMARK SEQADV
REVDAT 1 16-MAY-12 4F36 0
JRNL AUTH SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 2 (SSGCID),A.S.GARDBERG,T.E.EDWARDS,B.STAKER,L.STEWART
JRNL TITL CRYSTAL STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE B FROM
JRNL TITL 2 TRYPANOSOMA BRUCEI, APO FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 42483
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2144
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2541
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.63000
REMARK 3 B22 (A**2) : -1.89000
REMARK 3 B33 (A**2) : 2.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.320
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.223
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.043
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6442 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4316 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8728 ; 1.411 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10478 ; 1.232 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 830 ; 6.082 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 263 ;28.429 ;23.384
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1004 ;13.369 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;24.369 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 976 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7270 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1364 ; 0.007 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 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 3 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8340 13.7170 -31.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.0884
REMARK 3 T33: 0.1509 T12: -0.0142
REMARK 3 T13: -0.0925 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.3902 L22: 1.3394
REMARK 3 L33: 0.5480 L12: -0.4413
REMARK 3 L13: 0.1005 L23: -0.3089
REMARK 3 S TENSOR
REMARK 3 S11: 0.0322 S12: 0.0803 S13: -0.0713
REMARK 3 S21: -0.1244 S22: 0.0560 S23: -0.0159
REMARK 3 S31: -0.0546 S32: -0.0195 S33: -0.0882
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 40 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4170 31.0040 -32.6280
REMARK 3 T TENSOR
REMARK 3 T11: 0.2512 T22: 0.2142
REMARK 3 T33: 0.2748 T12: 0.1077
REMARK 3 T13: -0.0166 T23: 0.1446
REMARK 3 L TENSOR
REMARK 3 L11: 7.4028 L22: 1.9782
REMARK 3 L33: 9.5511 L12: -1.6897
REMARK 3 L13: -2.7973 L23: -1.3931
REMARK 3 S TENSOR
REMARK 3 S11: 0.3817 S12: 0.2300 S13: 0.6845
REMARK 3 S21: 0.1313 S22: 0.3602 S23: 0.2143
REMARK 3 S31: -0.9947 S32: -1.2989 S33: -0.7420
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 151
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5180 13.1070 -34.5430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.1046
REMARK 3 T33: 0.1718 T12: -0.0037
REMARK 3 T13: -0.1350 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 1.4848 L22: 1.4220
REMARK 3 L33: 1.3167 L12: 0.0627
REMARK 3 L13: -0.2104 L23: -0.1652
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.2269 S13: 0.1033
REMARK 3 S21: -0.2003 S22: 0.1184 S23: 0.2486
REMARK 3 S31: -0.0839 S32: -0.0890 S33: -0.1049
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 2 B 22
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3960 -13.8660 -15.9280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1421 T22: 0.0637
REMARK 3 T33: 0.3481 T12: 0.0066
REMARK 3 T13: -0.1854 T23: -0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 2.3091 L22: 2.0441
REMARK 3 L33: 3.7037 L12: -0.6298
REMARK 3 L13: -1.2200 L23: 0.7250
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: -0.1022 S13: -0.2182
REMARK 3 S21: 0.1138 S22: 0.2950 S23: -0.1769
REMARK 3 S31: 0.3899 S32: -0.0350 S33: -0.2859
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 23 B 87
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3960 -16.9560 -16.7100
REMARK 3 T TENSOR
REMARK 3 T11: 0.1407 T22: 0.0610
REMARK 3 T33: 0.3496 T12: 0.0438
REMARK 3 T13: -0.1788 T23: -0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 2.9227 L22: 1.8982
REMARK 3 L33: 1.5740 L12: -0.3464
REMARK 3 L13: -0.8463 L23: -0.3075
REMARK 3 S TENSOR
REMARK 3 S11: 0.0300 S12: -0.2215 S13: -0.4792
REMARK 3 S21: 0.2192 S22: 0.0872 S23: -0.1815
REMARK 3 S31: 0.2108 S32: 0.2353 S33: -0.1171
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 88 B 152
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2010 -13.1830 -19.4350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0633 T22: 0.0626
REMARK 3 T33: 0.3585 T12: 0.0277
REMARK 3 T13: -0.1313 T23: -0.0697
REMARK 3 L TENSOR
REMARK 3 L11: 1.3536 L22: 2.1507
REMARK 3 L33: 1.1860 L12: -0.3496
REMARK 3 L13: 0.2889 L23: 0.1741
REMARK 3 S TENSOR
REMARK 3 S11: 0.0363 S12: -0.0140 S13: -0.3445
REMARK 3 S21: 0.1159 S22: 0.0876 S23: -0.3426
REMARK 3 S31: 0.0417 S32: 0.1464 S33: -0.1239
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 3 C 87
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1380 13.4120 -32.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0959 T22: 0.1410
REMARK 3 T33: 0.2291 T12: -0.0158
REMARK 3 T13: -0.0498 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.9083 L22: 2.9222
REMARK 3 L33: 2.5784 L12: 1.2560
REMARK 3 L13: 1.4568 L23: 1.5771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0969 S12: 0.3942 S13: -0.0155
REMARK 3 S21: -0.2180 S22: 0.1006 S23: -0.4128
REMARK 3 S31: -0.1543 S32: 0.3578 S33: -0.0037
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 88 C 128
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8790 7.5320 -29.3770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0585 T22: 0.1912
REMARK 3 T33: 0.3042 T12: -0.0158
REMARK 3 T13: -0.0547 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.7841 L22: 2.8866
REMARK 3 L33: 1.9978 L12: -0.6388
REMARK 3 L13: -0.2087 L23: -0.4064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: 0.1916 S13: -0.0101
REMARK 3 S21: -0.0524 S22: -0.0817 S23: -0.5176
REMARK 3 S31: 0.0377 S32: 0.4257 S33: 0.0907
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 129 C 153
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1880 25.9590 -27.8070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1697 T22: 0.0751
REMARK 3 T33: 0.2317 T12: -0.0841
REMARK 3 T13: -0.0915 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 2.1380 L22: 0.7678
REMARK 3 L33: 4.8625 L12: -0.3554
REMARK 3 L13: -0.9461 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.1186 S12: 0.2126 S13: 0.2776
REMARK 3 S21: -0.0709 S22: 0.0348 S23: -0.2206
REMARK 3 S31: -0.4148 S32: 0.2602 S33: 0.0838
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 3 D 26
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1030 -11.1910 -23.9330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0883 T22: 0.0458
REMARK 3 T33: 0.3018 T12: 0.0162
REMARK 3 T13: -0.1303 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 2.8073 L22: 1.8336
REMARK 3 L33: 3.8985 L12: 0.6691
REMARK 3 L13: -1.8256 L23: -0.3780
REMARK 3 S TENSOR
REMARK 3 S11: -0.1634 S12: 0.0988 S13: -0.2173
REMARK 3 S21: -0.1137 S22: 0.1626 S23: 0.0768
REMARK 3 S31: 0.1671 S32: 0.0337 S33: 0.0008
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 27 D 125
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5910 -12.2890 -25.4810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.0814
REMARK 3 T33: 0.3037 T12: -0.0153
REMARK 3 T13: -0.1461 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.8456 L22: 2.4769
REMARK 3 L33: 1.1864 L12: -0.4295
REMARK 3 L13: 0.2200 L23: -0.8822
REMARK 3 S TENSOR
REMARK 3 S11: 0.1231 S12: 0.0952 S13: -0.2950
REMARK 3 S21: -0.2161 S22: 0.0045 S23: 0.2203
REMARK 3 S31: 0.1407 S32: -0.0456 S33: -0.1276
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 126 D 152
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8600 -20.1710 -12.8810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1610 T22: 0.0236
REMARK 3 T33: 0.4627 T12: -0.0458
REMARK 3 T13: -0.1184 T23: 0.0838
REMARK 3 L TENSOR
REMARK 3 L11: 2.4544 L22: 4.1359
REMARK 3 L33: 3.4558 L12: 0.2555
REMARK 3 L13: 0.6531 L23: 3.1806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.0253 S13: -0.5546
REMARK 3 S21: 0.2770 S22: 0.0964 S23: 0.3629
REMARK 3 S31: 0.1397 S32: 0.0564 S33: -0.1309
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 0 E 25
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1190 9.7340 -3.5420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1469 T22: 0.1003
REMARK 3 T33: 0.1122 T12: 0.0283
REMARK 3 T13: -0.0341 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 1.8283 L22: 5.2078
REMARK 3 L33: 1.8899 L12: -1.4800
REMARK 3 L13: 1.2047 L23: -2.4326
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: -0.2291 S13: -0.1543
REMARK 3 S21: 0.4998 S22: 0.1891 S23: 0.2375
REMARK 3 S31: -0.0470 S32: -0.2095 S33: -0.1240
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 26 E 87
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3320 9.2580 0.9580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2114 T22: 0.1905
REMARK 3 T33: 0.2195 T12: 0.0444
REMARK 3 T13: 0.0048 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 2.6169 L22: 3.2377
REMARK 3 L33: 2.7056 L12: -1.1426
REMARK 3 L13: 1.0427 L23: -1.3328
REMARK 3 S TENSOR
REMARK 3 S11: -0.0180 S12: -0.5121 S13: -0.3787
REMARK 3 S21: 0.5147 S22: 0.2971 S23: 0.5596
REMARK 3 S31: 0.0250 S32: -0.4860 S33: -0.2791
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 88 E 153
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2090 12.1580 -5.1320
REMARK 3 T TENSOR
REMARK 3 T11: 0.1296 T22: 0.1303
REMARK 3 T33: 0.1371 T12: 0.0644
REMARK 3 T13: -0.0191 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 1.2000 L22: 2.1179
REMARK 3 L33: 1.2102 L12: 0.1205
REMARK 3 L13: 0.3993 L23: 0.0359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: -0.2828 S13: -0.0026
REMARK 3 S21: 0.3225 S22: 0.0351 S23: 0.2890
REMARK 3 S31: -0.0287 S32: -0.2774 S33: -0.0268
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 3 F 25
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7440 13.3080 -3.1630
REMARK 3 T TENSOR
REMARK 3 T11: 0.1404 T22: 0.0870
REMARK 3 T33: 0.1587 T12: 0.0263
REMARK 3 T13: -0.1179 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 1.0329 L22: 4.8749
REMARK 3 L33: 2.2350 L12: -0.5908
REMARK 3 L13: 0.8564 L23: -1.3521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0210 S12: 0.0414 S13: 0.1039
REMARK 3 S21: 0.2657 S22: -0.0218 S23: -0.1811
REMARK 3 S31: -0.0281 S32: 0.0993 S33: 0.0008
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 26 F 53
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5930 15.2540 4.6460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3559 T22: 0.0985
REMARK 3 T33: 0.2146 T12: 0.0175
REMARK 3 T13: -0.0987 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 2.6171 L22: 2.7408
REMARK 3 L33: 1.0659 L12: 2.2387
REMARK 3 L13: 0.3609 L23: 1.2205
REMARK 3 S TENSOR
REMARK 3 S11: 0.3062 S12: -0.1290 S13: 0.3922
REMARK 3 S21: 0.2747 S22: -0.1742 S23: 0.2043
REMARK 3 S31: 0.0622 S32: -0.0391 S33: -0.1320
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 54 F 151
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6720 9.9320 0.6150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2221 T22: 0.1059
REMARK 3 T33: 0.1829 T12: 0.0242
REMARK 3 T13: -0.1840 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 1.3130 L22: 1.4039
REMARK 3 L33: 0.6079 L12: 0.4517
REMARK 3 L13: -0.0535 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: 0.0411 S12: -0.2272 S13: 0.0353
REMARK 3 S21: 0.3356 S22: 0.0299 S23: -0.2117
REMARK 3 S31: -0.0444 S32: 0.1241 S33: -0.0710
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: U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4F36 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0331710
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL, ASYMMETRIC CUT
REMARK 200 4.9650 DEGREES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.11
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 3R9L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EBS INTERNAL TRACKING NUMBER 233837B2:
REMARK 280 JCSG B2, PROTEIN: 20.2 MG/ML TRBRA.00438.A.B1 PS01459 IN 25 MM
REMARK 280 HEPES, PH 7.0, 500 MM SODIUM CHLORIDE, 2 MM DTT, 0.025% SODIUM
REMARK 280 AZIDE, 5% GLYCEROL, CRYSTALLANT: 20% PEG3350, 200 MM SODIUM
REMARK 280 ISOTHIOCYANATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 26.23000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.68000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.68000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.23000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.83500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E, 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 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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 TYR A 51
REMARK 465 ILE A 52
REMARK 465 ASP A 53
REMARK 465 LEU A 54
REMARK 465 ALA A 55
REMARK 465 SER A 56
REMARK 465 LYS A 57
REMARK 465 PRO A 58
REMARK 465 ARG A 152
REMARK 465 ALA A 153
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 TYR C 51
REMARK 465 ILE C 52
REMARK 465 ASP C 53
REMARK 465 LEU C 54
REMARK 465 ALA C 55
REMARK 465 SER C 56
REMARK 465 LYS C 57
REMARK 465 PRO C 58
REMARK 465 PHE C 59
REMARK 465 TYR C 60
REMARK 465 SER C 61
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 TYR B 51
REMARK 465 ILE B 52
REMARK 465 ASP B 53
REMARK 465 LEU B 54
REMARK 465 ALA B 55
REMARK 465 SER B 56
REMARK 465 LYS B 57
REMARK 465 PRO B 58
REMARK 465 PHE B 59
REMARK 465 TYR B 60
REMARK 465 SER B 61
REMARK 465 ALA B 153
REMARK 465 GLY D -3
REMARK 465 PRO D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 GLN D 49
REMARK 465 HIS D 50
REMARK 465 TYR D 51
REMARK 465 ILE D 52
REMARK 465 ASP D 53
REMARK 465 LEU D 54
REMARK 465 ALA D 55
REMARK 465 SER D 56
REMARK 465 LYS D 57
REMARK 465 PRO D 58
REMARK 465 PHE D 59
REMARK 465 TYR D 60
REMARK 465 SER D 61
REMARK 465 ALA D 153
REMARK 465 GLY E -3
REMARK 465 PRO E -2
REMARK 465 GLY E -1
REMARK 465 ILE E 52
REMARK 465 ASP E 53
REMARK 465 LEU E 54
REMARK 465 ALA E 55
REMARK 465 SER E 56
REMARK 465 LYS E 57
REMARK 465 PRO E 58
REMARK 465 GLY F -3
REMARK 465 PRO F -2
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 MET F 1
REMARK 465 PRO F 2
REMARK 465 LYS F 57
REMARK 465 PRO F 58
REMARK 465 PHE F 59
REMARK 465 TYR F 60
REMARK 465 SER F 61
REMARK 465 GLY F 62
REMARK 465 LEU F 63
REMARK 465 VAL F 64
REMARK 465 SER F 65
REMARK 465 TYR F 66
REMARK 465 PHE F 67
REMARK 465 SER F 68
REMARK 465 SER F 69
REMARK 465 ARG F 152
REMARK 465 ALA F 153
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 LYS A 48 CG CD CE NZ
REMARK 470 GLN A 49 CG CD OE1 NE2
REMARK 470 PHE A 59 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 63 CG CD1 CD2
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 GLU C 44 CG CD OE1 OE2
REMARK 470 GLU C 45 CG CD OE1 OE2
REMARK 470 LYS C 48 CG CD CE NZ
REMARK 470 GLN C 49 CG CD OE1 NE2
REMARK 470 LEU C 63 CG CD1 CD2
REMARK 470 SER C 65 OG
REMARK 470 GLU C 123 CG CD OE1 OE2
REMARK 470 LYS C 134 CG CD CE NZ
REMARK 470 LYS C 147 CG CD CE NZ
REMARK 470 ARG C 152 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 GLU B 45 CG CD OE1 OE2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 GLN B 49 CG CD OE1 NE2
REMARK 470 LEU B 63 CG CD1 CD2
REMARK 470 LYS B 84 CG CD CE NZ
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 ARG B 152 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 LEU D 63 CG CD1 CD2
REMARK 470 LYS D 84 CG CD CE NZ
REMARK 470 GLU D 123 CG CD OE1 OE2
REMARK 470 LYS D 134 CG CD CE NZ
REMARK 470 LYS D 147 CG CD CE NZ
REMARK 470 ARG D 152 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 44 CG CD OE1 OE2
REMARK 470 LYS E 48 CG CD CE NZ
REMARK 470 GLN E 49 CG CD OE1 NE2
REMARK 470 PHE E 59 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR E 60 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER E 61 OG
REMARK 470 LEU E 63 CG CD1 CD2
REMARK 470 GLU E 123 CG CD OE1 OE2
REMARK 470 LYS E 134 CG CD CE NZ
REMARK 470 GLU E 136 CG CD OE1 OE2
REMARK 470 LYS E 147 CG CD CE NZ
REMARK 470 ARG E 152 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 41 CG CD OE1 NE2
REMARK 470 GLU F 44 CG CD OE1 OE2
REMARK 470 GLU F 45 CG CD OE1 OE2
REMARK 470 LYS F 84 CG CD CE NZ
REMARK 470 GLU F 123 CG CD OE1 OE2
REMARK 470 LYS F 134 CG CD CE NZ
REMARK 470 LYS F 147 CG CD CE NZ
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 HIS A 117 CG HIS A 117 CD2 0.058
REMARK 500 HIS C 50 CG HIS C 50 CD2 0.057
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 VAL A 115 -33.80 76.18
REMARK 500 VAL C 115 -35.30 76.87
REMARK 500 VAL B 115 -34.65 74.77
REMARK 500 VAL D 115 -33.90 75.58
REMARK 500 VAL E 115 -32.01 75.59
REMARK 500 VAL F 115 -34.61 77.46
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 SCN F 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-TRBRA.00438.A RELATED DB: TARGETTRACK
DBREF 4F36 A 1 153 UNP Q381H3 Q381H3_TRYB2 1 153
DBREF 4F36 C 1 153 UNP Q381H3 Q381H3_TRYB2 1 153
DBREF 4F36 B 1 153 UNP Q381H3 Q381H3_TRYB2 1 153
DBREF 4F36 D 1 153 UNP Q381H3 Q381H3_TRYB2 1 153
DBREF 4F36 E 1 153 UNP Q381H3 Q381H3_TRYB2 1 153
DBREF 4F36 F 1 153 UNP Q381H3 Q381H3_TRYB2 1 153
SEQADV 4F36 GLY A -3 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 PRO A -2 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY A -1 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 SER A 0 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY C -3 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 PRO C -2 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY C -1 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 SER C 0 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY B -3 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 PRO B -2 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY B -1 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 SER B 0 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY D -3 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 PRO D -2 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY D -1 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 SER D 0 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY E -3 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 PRO E -2 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY E -1 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 SER E 0 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY F -3 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 PRO F -2 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 GLY F -1 UNP Q381H3 EXPRESSION TAG
SEQADV 4F36 SER F 0 UNP Q381H3 EXPRESSION TAG
SEQRES 1 A 157 GLY PRO GLY SER MET PRO SER GLU ARG THR PHE ILE ALA
SEQRES 2 A 157 VAL LYS PRO ASP GLY VAL GLN ARG ASN LEU VAL GLY GLU
SEQRES 3 A 157 ILE ILE LYS ARG PHE GLU ASN LYS GLY TYR LYS LEU VAL
SEQRES 4 A 157 GLY LEU LYS LEU LEU GLN PRO THR GLU GLU GLN ALA LYS
SEQRES 5 A 157 GLN HIS TYR ILE ASP LEU ALA SER LYS PRO PHE TYR SER
SEQRES 6 A 157 GLY LEU VAL SER TYR PHE SER SER GLY PRO ILE VAL GLY
SEQRES 7 A 157 MET VAL TRP GLU GLY LEU GLY VAL VAL LYS GLY GLY ARG
SEQRES 8 A 157 VAL LEU LEU GLY ALA THR ASN PRO ALA ASP SER LEU PRO
SEQRES 9 A 157 GLY THR ILE ARG GLY ASP PHE ALA VAL ASP VAL GLY ARG
SEQRES 10 A 157 ASN VAL CYS HIS GLY SER ASP SER VAL GLU SER ALA LYS
SEQRES 11 A 157 ARG GLU ILE ALA PHE TRP PHE LYS ALA GLU GLU LEU VAL
SEQRES 12 A 157 SER TRP THR SER HIS SER VAL LYS GLN ILE TYR GLU ARG
SEQRES 13 A 157 ALA
SEQRES 1 C 157 GLY PRO GLY SER MET PRO SER GLU ARG THR PHE ILE ALA
SEQRES 2 C 157 VAL LYS PRO ASP GLY VAL GLN ARG ASN LEU VAL GLY GLU
SEQRES 3 C 157 ILE ILE LYS ARG PHE GLU ASN LYS GLY TYR LYS LEU VAL
SEQRES 4 C 157 GLY LEU LYS LEU LEU GLN PRO THR GLU GLU GLN ALA LYS
SEQRES 5 C 157 GLN HIS TYR ILE ASP LEU ALA SER LYS PRO PHE TYR SER
SEQRES 6 C 157 GLY LEU VAL SER TYR PHE SER SER GLY PRO ILE VAL GLY
SEQRES 7 C 157 MET VAL TRP GLU GLY LEU GLY VAL VAL LYS GLY GLY ARG
SEQRES 8 C 157 VAL LEU LEU GLY ALA THR ASN PRO ALA ASP SER LEU PRO
SEQRES 9 C 157 GLY THR ILE ARG GLY ASP PHE ALA VAL ASP VAL GLY ARG
SEQRES 10 C 157 ASN VAL CYS HIS GLY SER ASP SER VAL GLU SER ALA LYS
SEQRES 11 C 157 ARG GLU ILE ALA PHE TRP PHE LYS ALA GLU GLU LEU VAL
SEQRES 12 C 157 SER TRP THR SER HIS SER VAL LYS GLN ILE TYR GLU ARG
SEQRES 13 C 157 ALA
SEQRES 1 B 157 GLY PRO GLY SER MET PRO SER GLU ARG THR PHE ILE ALA
SEQRES 2 B 157 VAL LYS PRO ASP GLY VAL GLN ARG ASN LEU VAL GLY GLU
SEQRES 3 B 157 ILE ILE LYS ARG PHE GLU ASN LYS GLY TYR LYS LEU VAL
SEQRES 4 B 157 GLY LEU LYS LEU LEU GLN PRO THR GLU GLU GLN ALA LYS
SEQRES 5 B 157 GLN HIS TYR ILE ASP LEU ALA SER LYS PRO PHE TYR SER
SEQRES 6 B 157 GLY LEU VAL SER TYR PHE SER SER GLY PRO ILE VAL GLY
SEQRES 7 B 157 MET VAL TRP GLU GLY LEU GLY VAL VAL LYS GLY GLY ARG
SEQRES 8 B 157 VAL LEU LEU GLY ALA THR ASN PRO ALA ASP SER LEU PRO
SEQRES 9 B 157 GLY THR ILE ARG GLY ASP PHE ALA VAL ASP VAL GLY ARG
SEQRES 10 B 157 ASN VAL CYS HIS GLY SER ASP SER VAL GLU SER ALA LYS
SEQRES 11 B 157 ARG GLU ILE ALA PHE TRP PHE LYS ALA GLU GLU LEU VAL
SEQRES 12 B 157 SER TRP THR SER HIS SER VAL LYS GLN ILE TYR GLU ARG
SEQRES 13 B 157 ALA
SEQRES 1 D 157 GLY PRO GLY SER MET PRO SER GLU ARG THR PHE ILE ALA
SEQRES 2 D 157 VAL LYS PRO ASP GLY VAL GLN ARG ASN LEU VAL GLY GLU
SEQRES 3 D 157 ILE ILE LYS ARG PHE GLU ASN LYS GLY TYR LYS LEU VAL
SEQRES 4 D 157 GLY LEU LYS LEU LEU GLN PRO THR GLU GLU GLN ALA LYS
SEQRES 5 D 157 GLN HIS TYR ILE ASP LEU ALA SER LYS PRO PHE TYR SER
SEQRES 6 D 157 GLY LEU VAL SER TYR PHE SER SER GLY PRO ILE VAL GLY
SEQRES 7 D 157 MET VAL TRP GLU GLY LEU GLY VAL VAL LYS GLY GLY ARG
SEQRES 8 D 157 VAL LEU LEU GLY ALA THR ASN PRO ALA ASP SER LEU PRO
SEQRES 9 D 157 GLY THR ILE ARG GLY ASP PHE ALA VAL ASP VAL GLY ARG
SEQRES 10 D 157 ASN VAL CYS HIS GLY SER ASP SER VAL GLU SER ALA LYS
SEQRES 11 D 157 ARG GLU ILE ALA PHE TRP PHE LYS ALA GLU GLU LEU VAL
SEQRES 12 D 157 SER TRP THR SER HIS SER VAL LYS GLN ILE TYR GLU ARG
SEQRES 13 D 157 ALA
SEQRES 1 E 157 GLY PRO GLY SER MET PRO SER GLU ARG THR PHE ILE ALA
SEQRES 2 E 157 VAL LYS PRO ASP GLY VAL GLN ARG ASN LEU VAL GLY GLU
SEQRES 3 E 157 ILE ILE LYS ARG PHE GLU ASN LYS GLY TYR LYS LEU VAL
SEQRES 4 E 157 GLY LEU LYS LEU LEU GLN PRO THR GLU GLU GLN ALA LYS
SEQRES 5 E 157 GLN HIS TYR ILE ASP LEU ALA SER LYS PRO PHE TYR SER
SEQRES 6 E 157 GLY LEU VAL SER TYR PHE SER SER GLY PRO ILE VAL GLY
SEQRES 7 E 157 MET VAL TRP GLU GLY LEU GLY VAL VAL LYS GLY GLY ARG
SEQRES 8 E 157 VAL LEU LEU GLY ALA THR ASN PRO ALA ASP SER LEU PRO
SEQRES 9 E 157 GLY THR ILE ARG GLY ASP PHE ALA VAL ASP VAL GLY ARG
SEQRES 10 E 157 ASN VAL CYS HIS GLY SER ASP SER VAL GLU SER ALA LYS
SEQRES 11 E 157 ARG GLU ILE ALA PHE TRP PHE LYS ALA GLU GLU LEU VAL
SEQRES 12 E 157 SER TRP THR SER HIS SER VAL LYS GLN ILE TYR GLU ARG
SEQRES 13 E 157 ALA
SEQRES 1 F 157 GLY PRO GLY SER MET PRO SER GLU ARG THR PHE ILE ALA
SEQRES 2 F 157 VAL LYS PRO ASP GLY VAL GLN ARG ASN LEU VAL GLY GLU
SEQRES 3 F 157 ILE ILE LYS ARG PHE GLU ASN LYS GLY TYR LYS LEU VAL
SEQRES 4 F 157 GLY LEU LYS LEU LEU GLN PRO THR GLU GLU GLN ALA LYS
SEQRES 5 F 157 GLN HIS TYR ILE ASP LEU ALA SER LYS PRO PHE TYR SER
SEQRES 6 F 157 GLY LEU VAL SER TYR PHE SER SER GLY PRO ILE VAL GLY
SEQRES 7 F 157 MET VAL TRP GLU GLY LEU GLY VAL VAL LYS GLY GLY ARG
SEQRES 8 F 157 VAL LEU LEU GLY ALA THR ASN PRO ALA ASP SER LEU PRO
SEQRES 9 F 157 GLY THR ILE ARG GLY ASP PHE ALA VAL ASP VAL GLY ARG
SEQRES 10 F 157 ASN VAL CYS HIS GLY SER ASP SER VAL GLU SER ALA LYS
SEQRES 11 F 157 ARG GLU ILE ALA PHE TRP PHE LYS ALA GLU GLU LEU VAL
SEQRES 12 F 157 SER TRP THR SER HIS SER VAL LYS GLN ILE TYR GLU ARG
SEQRES 13 F 157 ALA
HET SCN F 201 3
HETNAM SCN THIOCYANATE ION
FORMUL 7 SCN C N S 1-
FORMUL 8 HOH *286(H2 O)
HELIX 1 1 LYS A 11 ARG A 17 1 7
HELIX 2 2 LEU A 19 GLY A 31 1 13
HELIX 3 3 THR A 43 HIS A 50 1 8
HELIX 4 4 TYR A 60 SER A 68 1 9
HELIX 5 5 GLY A 81 GLY A 91 1 11
HELIX 6 6 ASN A 94 SER A 98 5 5
HELIX 7 7 THR A 102 ALA A 108 1 7
HELIX 8 8 ASP A 110 ASN A 114 5 5
HELIX 9 9 SER A 121 PHE A 133 1 13
HELIX 10 10 LYS A 134 LEU A 138 5 5
HELIX 11 11 SER A 145 TYR A 150 1 6
HELIX 12 12 LYS C 11 ARG C 17 1 7
HELIX 13 13 LEU C 19 GLY C 31 1 13
HELIX 14 14 THR C 43 HIS C 50 1 8
HELIX 15 15 LEU C 63 SER C 68 1 6
HELIX 16 16 GLY C 81 GLY C 91 1 11
HELIX 17 17 ASN C 94 SER C 98 5 5
HELIX 18 18 THR C 102 ALA C 108 1 7
HELIX 19 19 ASP C 110 ASN C 114 5 5
HELIX 20 20 SER C 121 PHE C 133 1 13
HELIX 21 21 LYS C 134 LEU C 138 5 5
HELIX 22 22 SER C 145 TYR C 150 1 6
HELIX 23 23 LYS B 11 ARG B 17 1 7
HELIX 24 24 LEU B 19 GLY B 31 1 13
HELIX 25 25 THR B 43 HIS B 50 1 8
HELIX 26 26 LEU B 63 SER B 68 1 6
HELIX 27 27 GLY B 81 GLY B 91 1 11
HELIX 28 28 ASN B 94 SER B 98 5 5
HELIX 29 29 THR B 102 ALA B 108 1 7
HELIX 30 30 ASP B 110 ASN B 114 5 5
HELIX 31 31 SER B 121 PHE B 133 1 13
HELIX 32 32 LYS B 134 LEU B 138 5 5
HELIX 33 33 SER B 145 TYR B 150 1 6
HELIX 34 34 LYS D 11 ARG D 17 1 7
HELIX 35 35 LEU D 19 GLY D 31 1 13
HELIX 36 36 THR D 43 LYS D 48 1 6
HELIX 37 37 LEU D 63 SER D 68 1 6
HELIX 38 38 GLY D 81 GLY D 91 1 11
HELIX 39 39 ASN D 94 SER D 98 5 5
HELIX 40 40 THR D 102 ALA D 108 1 7
HELIX 41 41 ASP D 110 ASN D 114 5 5
HELIX 42 42 SER D 121 PHE D 133 1 13
HELIX 43 43 LYS D 134 LEU D 138 5 5
HELIX 44 44 SER D 145 TYR D 150 1 6
HELIX 45 45 LYS E 11 ARG E 17 1 7
HELIX 46 46 LEU E 19 GLY E 31 1 13
HELIX 47 47 THR E 43 TYR E 51 1 9
HELIX 48 48 SER E 61 SER E 68 1 8
HELIX 49 49 GLY E 81 GLY E 91 1 11
HELIX 50 50 ASN E 94 SER E 98 5 5
HELIX 51 51 THR E 102 ALA E 108 1 7
HELIX 52 52 ASP E 110 ASN E 114 5 5
HELIX 53 53 SER E 121 PHE E 133 1 13
HELIX 54 54 LYS E 134 LEU E 138 5 5
HELIX 55 55 SER E 145 TYR E 150 1 6
HELIX 56 56 LYS F 11 ARG F 17 1 7
HELIX 57 57 LEU F 19 GLY F 31 1 13
HELIX 58 58 THR F 43 LEU F 54 1 12
HELIX 59 59 GLY F 81 GLY F 91 1 11
HELIX 60 60 ASN F 94 SER F 98 5 5
HELIX 61 61 THR F 102 ALA F 108 1 7
HELIX 62 62 ASP F 110 ASN F 114 5 5
HELIX 63 63 SER F 121 PHE F 133 1 13
HELIX 64 64 LYS F 134 LEU F 138 5 5
HELIX 65 65 SER F 145 TYR F 150 1 6
SHEET 1 A 4 LYS A 33 LEU A 40 0
SHEET 2 A 4 ILE A 72 GLU A 78 -1 O ILE A 72 N LEU A 40
SHEET 3 A 4 ARG A 5 VAL A 10 -1 N VAL A 10 O VAL A 73
SHEET 4 A 4 CYS A 116 GLY A 118 -1 O HIS A 117 N ALA A 9
SHEET 1 B 4 LYS C 33 LEU C 40 0
SHEET 2 B 4 ILE C 72 GLU C 78 -1 O ILE C 72 N LEU C 40
SHEET 3 B 4 ARG C 5 VAL C 10 -1 N VAL C 10 O VAL C 73
SHEET 4 B 4 CYS C 116 GLY C 118 -1 O HIS C 117 N ALA C 9
SHEET 1 C 4 LYS B 33 LEU B 40 0
SHEET 2 C 4 ILE B 72 GLU B 78 -1 O ILE B 72 N LEU B 40
SHEET 3 C 4 ARG B 5 VAL B 10 -1 N ILE B 8 O MET B 75
SHEET 4 C 4 CYS B 116 GLY B 118 -1 O HIS B 117 N ALA B 9
SHEET 1 D 4 LYS D 33 LEU D 40 0
SHEET 2 D 4 ILE D 72 GLU D 78 -1 O ILE D 72 N LEU D 40
SHEET 3 D 4 ARG D 5 VAL D 10 -1 N ILE D 8 O MET D 75
SHEET 4 D 4 CYS D 116 GLY D 118 -1 O HIS D 117 N ALA D 9
SHEET 1 E 4 LYS E 33 LEU E 40 0
SHEET 2 E 4 ILE E 72 GLU E 78 -1 O ILE E 72 N LEU E 40
SHEET 3 E 4 ARG E 5 VAL E 10 -1 N VAL E 10 O VAL E 73
SHEET 4 E 4 CYS E 116 GLY E 118 -1 O HIS E 117 N ALA E 9
SHEET 1 F 4 LYS F 33 LEU F 40 0
SHEET 2 F 4 ILE F 72 GLU F 78 -1 O GLY F 74 N LYS F 38
SHEET 3 F 4 ARG F 5 VAL F 10 -1 N ILE F 8 O MET F 75
SHEET 4 F 4 CYS F 116 GLY F 118 -1 O HIS F 117 N ALA F 9
CISPEP 1 GLY F 70 PRO F 71 0 -2.41
SITE 1 AC1 2 LYS F 33 SER F 143
CRYST1 52.460 123.670 145.360 90.00 90.00 90.00 P 21 21 21 24
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 0.019062 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008086 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
