HEADER HYDROLASE 07-SEP-12 4H0C
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE/CARBOXYLESTERASE FROM DYADOBACTER
TITLE 2 FERMENTANS DSM 18053
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE/CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DYADOBACTER FERMENTANS;
SOURCE 3 ORGANISM_TAXID: 471854;
SOURCE 4 STRAIN: DSM 18053;
SOURCE 5 GENE: DFER_0355;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG57
KEYWDS PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 2 PHOSPHOLIPASE/CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,J.HOLOWICKI,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 26-SEP-12 4H0C 0
JRNL AUTH C.CHANG,J.HOLOWICKI,S.CLANCY,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF PHOSPHOLIPASE/CARBOXYLESTERASE FROM
JRNL TITL 2 DYADOBACTER FERMENTANS DSM 18053
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 47507
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) : 0.139
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2412
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) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3089
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 249
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : -0.68000
REMARK 3 B33 (A**2) : 1.31000
REMARK 3 B12 (A**2) : 0.20000
REMARK 3 B13 (A**2) : -1.17000
REMARK 3 B23 (A**2) : -0.49000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.584
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3368 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4595 ; 1.293 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 437 ; 5.886 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;37.469 ;25.319
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 551 ;12.220 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;18.612 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 520 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2589 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3368 ; 2.361 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 87 ;29.274 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3461 ;13.473 ; 5.000
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 : 22
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 10
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7150 37.7285 52.0292
REMARK 3 T TENSOR
REMARK 3 T11: 0.0123 T22: 0.0212
REMARK 3 T33: 0.0025 T12: 0.0028
REMARK 3 T13: 0.0003 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.3441 L22: 1.0196
REMARK 3 L33: 1.3007 L12: -0.2993
REMARK 3 L13: 0.4899 L23: -1.0552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: -0.0025 S13: -0.0163
REMARK 3 S21: -0.0068 S22: 0.0233 S23: 0.0243
REMARK 3 S31: 0.0182 S32: -0.0352 S33: -0.0356
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 11 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1477 32.0813 62.9980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0120 T22: 0.0235
REMARK 3 T33: 0.0075 T12: 0.0025
REMARK 3 T13: 0.0023 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.0094 L22: 0.1096
REMARK 3 L33: 0.2735 L12: 0.0196
REMARK 3 L13: -0.0184 L23: -0.1656
REMARK 3 S TENSOR
REMARK 3 S11: 0.0058 S12: 0.0022 S13: -0.0009
REMARK 3 S21: 0.0009 S22: 0.0042 S23: 0.0043
REMARK 3 S31: 0.0063 S32: 0.0010 S33: -0.0100
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 34 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0022 29.1019 61.5555
REMARK 3 T TENSOR
REMARK 3 T11: 0.0131 T22: 0.0228
REMARK 3 T33: 0.0057 T12: 0.0025
REMARK 3 T13: 0.0038 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.6050 L22: 0.1407
REMARK 3 L33: 0.0443 L12: -0.2048
REMARK 3 L13: 0.0221 L23: -0.0628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0216 S13: -0.0123
REMARK 3 S21: -0.0017 S22: -0.0166 S23: -0.0048
REMARK 3 S31: -0.0001 S32: 0.0117 S33: 0.0084
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 47 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3280 41.6184 50.7468
REMARK 3 T TENSOR
REMARK 3 T11: 0.0118 T22: 0.0238
REMARK 3 T33: 0.0081 T12: 0.0040
REMARK 3 T13: 0.0032 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0058 L22: 0.0346
REMARK 3 L33: 0.0615 L12: 0.0141
REMARK 3 L13: -0.0186 L23: -0.0457
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: 0.0013 S13: 0.0013
REMARK 3 S21: 0.0008 S22: 0.0038 S23: 0.0041
REMARK 3 S31: 0.0009 S32: -0.0011 S33: -0.0035
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 70 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1743 44.0262 56.7343
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0212
REMARK 3 T33: 0.0079 T12: 0.0035
REMARK 3 T13: 0.0019 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.0151 L22: 0.4008
REMARK 3 L33: 1.2887 L12: -0.0710
REMARK 3 L13: 0.1038 L23: -0.6549
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: -0.0027 S13: -0.0045
REMARK 3 S21: 0.0009 S22: 0.0167 S23: 0.0144
REMARK 3 S31: 0.0003 S32: -0.0216 S33: -0.0198
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 90 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8581 38.9377 72.5881
REMARK 3 T TENSOR
REMARK 3 T11: 0.0131 T22: 0.0196
REMARK 3 T33: 0.0043 T12: 0.0035
REMARK 3 T13: 0.0025 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.5460 L22: 0.3280
REMARK 3 L33: 0.3920 L12: 0.4780
REMARK 3 L13: -0.6286 L23: -0.2771
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: -0.0365 S13: 0.0097
REMARK 3 S21: 0.0265 S22: -0.0156 S23: 0.0068
REMARK 3 S31: -0.0092 S32: 0.0159 S33: -0.0171
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 101 A 135
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3997 45.9091 58.5769
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0216
REMARK 3 T33: 0.0080 T12: 0.0028
REMARK 3 T13: 0.0028 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.0142 L22: 0.0405
REMARK 3 L33: 0.1240 L12: -0.0061
REMARK 3 L13: 0.0418 L23: -0.0143
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0001 S13: 0.0007
REMARK 3 S21: 0.0020 S22: -0.0014 S23: -0.0009
REMARK 3 S31: -0.0020 S32: -0.0020 S33: 0.0012
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 136 A 141
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1981 59.0851 54.1617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0094 T22: 0.0163
REMARK 3 T33: 0.0057 T12: 0.0029
REMARK 3 T13: 0.0024 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.1163 L22: 1.0555
REMARK 3 L33: 6.7597 L12: -0.0970
REMARK 3 L13: -3.5210 L23: 0.6165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0865 S12: -0.0050 S13: 0.0297
REMARK 3 S21: -0.0515 S22: -0.0046 S23: -0.0027
REMARK 3 S31: -0.1980 S32: -0.0155 S33: -0.0819
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 142 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5599 48.8731 58.6595
REMARK 3 T TENSOR
REMARK 3 T11: 0.0108 T22: 0.0194
REMARK 3 T33: 0.0074 T12: -0.0003
REMARK 3 T13: 0.0026 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.0691 L22: 0.0168
REMARK 3 L33: 0.2030 L12: -0.0329
REMARK 3 L13: -0.0125 L23: 0.0060
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: -0.0052 S13: 0.0046
REMARK 3 S21: -0.0001 S22: 0.0053 S23: -0.0023
REMARK 3 S31: 0.0066 S32: 0.0081 S33: -0.0022
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 : A 162 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1275 53.7419 57.7771
REMARK 3 T TENSOR
REMARK 3 T11: 0.0113 T22: 0.0202
REMARK 3 T33: 0.0061 T12: 0.0005
REMARK 3 T13: 0.0021 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.2384 L22: 0.0192
REMARK 3 L33: 0.5258 L12: -0.0648
REMARK 3 L13: -0.0047 L23: 0.0278
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: 0.0155 S13: 0.0064
REMARK 3 S21: -0.0019 S22: -0.0013 S23: -0.0011
REMARK 3 S31: -0.0209 S32: 0.0161 S33: -0.0046
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 : A 183 A 207
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3991 38.9674 57.2437
REMARK 3 T TENSOR
REMARK 3 T11: 0.0077 T22: 0.0229
REMARK 3 T33: 0.0060 T12: 0.0038
REMARK 3 T13: 0.0031 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.0984 L22: 0.1177
REMARK 3 L33: 0.6530 L12: 0.0247
REMARK 3 L13: -0.0344 L23: -0.0711
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: -0.0025 S13: -0.0074
REMARK 3 S21: -0.0051 S22: -0.0044 S23: -0.0074
REMARK 3 S31: 0.0203 S32: 0.0275 S33: 0.0040
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 -1 B 10
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5219 55.1508 27.6471
REMARK 3 T TENSOR
REMARK 3 T11: 0.0101 T22: 0.0251
REMARK 3 T33: 0.0084 T12: 0.0008
REMARK 3 T13: 0.0048 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.3781 L22: 0.9794
REMARK 3 L33: 1.1658 L12: -0.4243
REMARK 3 L13: -0.6181 L23: 0.9172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0287 S12: -0.0087 S13: 0.0286
REMARK 3 S21: 0.0127 S22: 0.0137 S23: -0.0509
REMARK 3 S31: -0.0130 S32: 0.0051 S33: -0.0424
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 11 B 33
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3795 43.4175 16.9076
REMARK 3 T TENSOR
REMARK 3 T11: 0.0119 T22: 0.0208
REMARK 3 T33: 0.0070 T12: 0.0043
REMARK 3 T13: 0.0019 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.0868 L22: 0.0388
REMARK 3 L33: 0.2709 L12: 0.0013
REMARK 3 L13: -0.1022 L23: 0.0747
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.0008 S13: 0.0012
REMARK 3 S21: -0.0019 S22: 0.0011 S23: 0.0000
REMARK 3 S31: -0.0013 S32: 0.0052 S33: -0.0002
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 34 B 46
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8406 35.2706 18.6211
REMARK 3 T TENSOR
REMARK 3 T11: 0.0129 T22: 0.0255
REMARK 3 T33: 0.0062 T12: 0.0047
REMARK 3 T13: 0.0011 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.1702 L22: 0.3974
REMARK 3 L33: 0.0257 L12: -0.0032
REMARK 3 L13: -0.0300 L23: -0.0884
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: -0.0042 S13: -0.0065
REMARK 3 S21: 0.0186 S22: 0.0037 S23: -0.0093
REMARK 3 S31: -0.0012 S32: 0.0027 S33: 0.0035
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 47 B 69
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7664 49.0299 29.4649
REMARK 3 T TENSOR
REMARK 3 T11: 0.0121 T22: 0.0250
REMARK 3 T33: 0.0055 T12: 0.0048
REMARK 3 T13: 0.0019 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.0823 L22: 0.0929
REMARK 3 L33: 0.0908 L12: 0.0276
REMARK 3 L13: -0.0668 L23: 0.0328
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: -0.0048 S13: 0.0103
REMARK 3 S21: 0.0050 S22: -0.0042 S23: -0.0006
REMARK 3 S31: -0.0124 S32: 0.0023 S33: -0.0113
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 70 B 89
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1796 54.2848 23.3120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0115 T22: 0.0208
REMARK 3 T33: 0.0066 T12: 0.0013
REMARK 3 T13: 0.0020 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.2283 L22: 0.1313
REMARK 3 L33: 1.1418 L12: -0.1426
REMARK 3 L13: -0.4646 L23: 0.2626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: -0.0031 S13: 0.0158
REMARK 3 S21: 0.0006 S22: 0.0099 S23: -0.0109
REMARK 3 S31: -0.0074 S32: 0.0051 S33: -0.0237
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 90 B 100
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3670 45.8982 7.6571
REMARK 3 T TENSOR
REMARK 3 T11: 0.0102 T22: 0.0225
REMARK 3 T33: 0.0057 T12: 0.0037
REMARK 3 T13: 0.0041 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.3687 L22: 0.8547
REMARK 3 L33: 0.2257 L12: 0.3140
REMARK 3 L13: -0.1430 L23: -0.4291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: 0.0294 S13: -0.0157
REMARK 3 S21: -0.0209 S22: -0.0045 S23: -0.0182
REMARK 3 S31: 0.0128 S32: -0.0016 S33: 0.0069
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 101 B 135
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6361 43.7009 22.3064
REMARK 3 T TENSOR
REMARK 3 T11: 0.0123 T22: 0.0227
REMARK 3 T33: 0.0079 T12: 0.0023
REMARK 3 T13: 0.0029 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.0058 L22: 0.0310
REMARK 3 L33: 0.0944 L12: -0.0127
REMARK 3 L13: -0.0015 L23: 0.0121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: 0.0025 S13: 0.0012
REMARK 3 S21: 0.0008 S22: 0.0004 S23: 0.0010
REMARK 3 S31: -0.0009 S32: 0.0012 S33: -0.0018
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 136 B 141
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6859 49.4725 27.0664
REMARK 3 T TENSOR
REMARK 3 T11: 0.0563 T22: 0.0915
REMARK 3 T33: 0.3005 T12: 0.0357
REMARK 3 T13: -0.0532 T23: -0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 0.7969 L22: 1.1029
REMARK 3 L33: 2.7185 L12: 0.9221
REMARK 3 L13: 1.4358 L23: 1.7302
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: -0.0984 S13: 0.1269
REMARK 3 S21: 0.1676 S22: -0.1115 S23: 0.0471
REMARK 3 S31: 0.2710 S32: -0.1296 S33: 0.0150
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 142 B 161
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5019 38.3100 22.7746
REMARK 3 T TENSOR
REMARK 3 T11: 0.0081 T22: 0.0205
REMARK 3 T33: 0.0075 T12: 0.0005
REMARK 3 T13: 0.0020 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.0686 L22: 0.1613
REMARK 3 L33: 0.3985 L12: -0.1033
REMARK 3 L13: 0.0807 L23: -0.0828
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0012 S13: -0.0012
REMARK 3 S21: 0.0062 S22: 0.0024 S23: 0.0015
REMARK 3 S31: 0.0080 S32: -0.0105 S33: 0.0009
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 162 B 182
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4229 37.9181 24.0255
REMARK 3 T TENSOR
REMARK 3 T11: 0.0121 T22: 0.0212
REMARK 3 T33: 0.0072 T12: 0.0019
REMARK 3 T13: 0.0037 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0946 L22: 0.1043
REMARK 3 L33: 0.3013 L12: 0.0024
REMARK 3 L13: 0.0709 L23: -0.0223
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: -0.0056 S13: -0.0098
REMARK 3 S21: 0.0100 S22: 0.0002 S23: 0.0035
REMARK 3 S31: 0.0056 S32: -0.0168 S33: -0.0062
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 183 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6200 28.5688 24.1659
REMARK 3 T TENSOR
REMARK 3 T11: 0.0103 T22: 0.0182
REMARK 3 T33: 0.0077 T12: 0.0020
REMARK 3 T13: 0.0028 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.1811 L22: 0.1374
REMARK 3 L33: 0.5427 L12: 0.0243
REMARK 3 L13: -0.1720 L23: -0.1814
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: -0.0012 S13: -0.0163
REMARK 3 S21: -0.0067 S22: -0.0014 S23: 0.0002
REMARK 3 S31: 0.0210 S32: 0.0121 S33: 0.0054
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4H0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074858.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47679
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 63.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 96.800
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.150
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, DM, SHELXDE, ARP/WARP, RESOLVE,
REMARK 200 COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI SODIUM CITRATE, 20% PEG4000,
REMARK 280 5% ISO-PROPANOL, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER B -2
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 SER A -2 OG
REMARK 470 ASN B -1 CG OD1 ND2
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 105 -119.70 57.13
REMARK 500 THR A 204 -88.05 -126.50
REMARK 500 SER B 105 -117.48 53.35
REMARK 500 THR B 129 68.23 60.81
REMARK 500 THR B 204 -86.11 -133.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 493 DISTANCE = 5.56 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 39 O
REMARK 620 2 HOH B 451 O 94.8
REMARK 620 3 HOH B 469 O 95.8 98.9
REMARK 620 4 HOH B 411 O 112.9 96.1 146.2
REMARK 620 5 LEU B 42 O 89.3 175.3 83.0 80.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 510 O
REMARK 620 2 HOH A 466 O 102.1
REMARK 620 3 ILE A 205 O 109.4 122.0
REMARK 620 4 LYS A 207 OXT 116.4 90.3 115.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC103406 RELATED DB: TARGETTRACK
DBREF 4H0C A 1 207 UNP C6VYE5 C6VYE5_DYAFD 1 207
DBREF 4H0C B 1 207 UNP C6VYE5 C6VYE5_DYAFD 1 207
SEQADV 4H0C SER A -2 UNP C6VYE5 EXPRESSION TAG
SEQADV 4H0C ASN A -1 UNP C6VYE5 EXPRESSION TAG
SEQADV 4H0C ALA A 0 UNP C6VYE5 EXPRESSION TAG
SEQADV 4H0C SER B -2 UNP C6VYE5 EXPRESSION TAG
SEQADV 4H0C ASN B -1 UNP C6VYE5 EXPRESSION TAG
SEQADV 4H0C ALA B 0 UNP C6VYE5 EXPRESSION TAG
SEQRES 1 A 210 SER ASN ALA MSE TYR THR HIS SER LYS GLN ILE ILE THR
SEQRES 2 A 210 SER GLY VAL PRO VAL GLN ARG ALA LYS LYS ALA VAL VAL
SEQRES 3 A 210 MSE LEU HIS GLY ARG GLY GLY THR ALA ALA ASP ILE ILE
SEQRES 4 A 210 SER LEU GLN LYS VAL LEU LYS LEU ASP GLU MSE ALA ILE
SEQRES 5 A 210 TYR ALA PRO GLN ALA THR ASN ASN SER TRP TYR PRO TYR
SEQRES 6 A 210 SER PHE MSE ALA PRO VAL GLN GLN ASN GLN PRO ALA LEU
SEQRES 7 A 210 ASP SER ALA LEU ALA LEU VAL GLY GLU VAL VAL ALA GLU
SEQRES 8 A 210 ILE GLU ALA GLN GLY ILE PRO ALA GLU GLN ILE TYR PHE
SEQRES 9 A 210 ALA GLY PHE SER GLN GLY ALA CYS LEU THR LEU GLU TYR
SEQRES 10 A 210 THR THR ARG ASN ALA ARG LYS TYR GLY GLY ILE ILE ALA
SEQRES 11 A 210 PHE THR GLY GLY LEU ILE GLY GLN GLU LEU ALA ILE GLY
SEQRES 12 A 210 ASN TYR LYS GLY ASP PHE LYS GLN THR PRO VAL PHE ILE
SEQRES 13 A 210 SER THR GLY ASN PRO ASP PRO HIS VAL PRO VAL SER ARG
SEQRES 14 A 210 VAL GLN GLU SER VAL THR ILE LEU GLU ASP MSE ASN ALA
SEQRES 15 A 210 ALA VAL SER GLN VAL VAL TYR PRO GLY ARG PRO HIS THR
SEQRES 16 A 210 ILE SER GLY ASP GLU ILE GLN LEU VAL ASN ASN THR ILE
SEQRES 17 A 210 LEU LYS
SEQRES 1 B 210 SER ASN ALA MSE TYR THR HIS SER LYS GLN ILE ILE THR
SEQRES 2 B 210 SER GLY VAL PRO VAL GLN ARG ALA LYS LYS ALA VAL VAL
SEQRES 3 B 210 MSE LEU HIS GLY ARG GLY GLY THR ALA ALA ASP ILE ILE
SEQRES 4 B 210 SER LEU GLN LYS VAL LEU LYS LEU ASP GLU MSE ALA ILE
SEQRES 5 B 210 TYR ALA PRO GLN ALA THR ASN ASN SER TRP TYR PRO TYR
SEQRES 6 B 210 SER PHE MSE ALA PRO VAL GLN GLN ASN GLN PRO ALA LEU
SEQRES 7 B 210 ASP SER ALA LEU ALA LEU VAL GLY GLU VAL VAL ALA GLU
SEQRES 8 B 210 ILE GLU ALA GLN GLY ILE PRO ALA GLU GLN ILE TYR PHE
SEQRES 9 B 210 ALA GLY PHE SER GLN GLY ALA CYS LEU THR LEU GLU TYR
SEQRES 10 B 210 THR THR ARG ASN ALA ARG LYS TYR GLY GLY ILE ILE ALA
SEQRES 11 B 210 PHE THR GLY GLY LEU ILE GLY GLN GLU LEU ALA ILE GLY
SEQRES 12 B 210 ASN TYR LYS GLY ASP PHE LYS GLN THR PRO VAL PHE ILE
SEQRES 13 B 210 SER THR GLY ASN PRO ASP PRO HIS VAL PRO VAL SER ARG
SEQRES 14 B 210 VAL GLN GLU SER VAL THR ILE LEU GLU ASP MSE ASN ALA
SEQRES 15 B 210 ALA VAL SER GLN VAL VAL TYR PRO GLY ARG PRO HIS THR
SEQRES 16 B 210 ILE SER GLY ASP GLU ILE GLN LEU VAL ASN ASN THR ILE
SEQRES 17 B 210 LEU LYS
MODRES 4H0C MSE A 1 MET SELENOMETHIONINE
MODRES 4H0C MSE A 24 MET SELENOMETHIONINE
MODRES 4H0C MSE A 47 MET SELENOMETHIONINE
MODRES 4H0C MSE A 65 MET SELENOMETHIONINE
MODRES 4H0C MSE A 177 MET SELENOMETHIONINE
MODRES 4H0C MSE B 1 MET SELENOMETHIONINE
MODRES 4H0C MSE B 24 MET SELENOMETHIONINE
MODRES 4H0C MSE B 47 MET SELENOMETHIONINE
MODRES 4H0C MSE B 65 MET SELENOMETHIONINE
MODRES 4H0C MSE B 177 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 24 8
HET MSE A 47 8
HET MSE A 65 8
HET MSE A 177 8
HET MSE B 1 8
HET MSE B 24 8
HET MSE B 47 8
HET MSE B 65 8
HET MSE B 177 8
HET CIT A 301 13
HET NA A 302 1
HET CIT B 301 13
HET NA B 302 1
HET GOL B 303 6
HETNAM MSE SELENOMETHIONINE
HETNAM CIT CITRIC ACID
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 3 CIT 2(C6 H8 O7)
FORMUL 4 NA 2(NA 1+)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *249(H2 O)
HELIX 1 1 THR A 31 SER A 37 1 7
HELIX 2 2 LEU A 38 VAL A 41 5 4
HELIX 3 3 ALA A 54 SER A 58 5 5
HELIX 4 4 PRO A 67 GLN A 72 5 6
HELIX 5 5 PRO A 73 GLN A 92 1 20
HELIX 6 6 PRO A 95 GLU A 97 5 3
HELIX 7 7 SER A 105 ASN A 118 1 14
HELIX 8 8 ALA A 138 TYR A 142 5 5
HELIX 9 9 PRO A 163 MSE A 177 1 15
HELIX 10 10 SER A 194 THR A 204 1 11
HELIX 11 11 PRO B 14 ALA B 18 5 5
HELIX 12 12 THR B 31 SER B 37 1 7
HELIX 13 13 LEU B 38 VAL B 41 5 4
HELIX 14 14 ALA B 54 SER B 58 5 5
HELIX 15 15 PRO B 67 GLN B 72 5 6
HELIX 16 16 PRO B 73 GLN B 92 1 20
HELIX 17 17 PRO B 95 GLU B 97 5 3
HELIX 18 18 SER B 105 ASN B 118 1 14
HELIX 19 19 ALA B 138 TYR B 142 5 5
HELIX 20 20 PRO B 163 MSE B 177 1 15
HELIX 21 21 SER B 194 ASN B 203 1 10
SHEET 1 A 7 ILE A 8 GLY A 12 0
SHEET 2 A 7 MSE A 47 PRO A 52 -1 O ALA A 51 N ILE A 9
SHEET 3 A 7 LYS A 20 LEU A 25 1 N VAL A 22 O TYR A 50
SHEET 4 A 7 ILE A 99 PHE A 104 1 O TYR A 100 N ALA A 21
SHEET 5 A 7 GLY A 124 PHE A 128 1 O ILE A 126 N PHE A 101
SHEET 6 A 7 PRO A 150 ASN A 157 1 O PHE A 152 N ALA A 127
SHEET 7 A 7 ALA A 180 PRO A 187 1 O SER A 182 N VAL A 151
SHEET 1 B 7 ILE B 8 GLY B 12 0
SHEET 2 B 7 MSE B 47 PRO B 52 -1 O ALA B 51 N ILE B 9
SHEET 3 B 7 LYS B 20 LEU B 25 1 N MSE B 24 O TYR B 50
SHEET 4 B 7 ILE B 99 PHE B 104 1 O TYR B 100 N ALA B 21
SHEET 5 B 7 GLY B 124 PHE B 128 1 O ILE B 126 N PHE B 101
SHEET 6 B 7 PRO B 150 ASN B 157 1 O PHE B 152 N ALA B 127
SHEET 7 B 7 ALA B 180 PRO B 187 1 O SER B 182 N VAL B 151
LINK C ALA A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N TYR A 2 1555 1555 1.33
LINK C VAL A 23 N MSE A 24 1555 1555 1.34
LINK C MSE A 24 N LEU A 25 1555 1555 1.33
LINK C GLU A 46 N MSE A 47 1555 1555 1.33
LINK C MSE A 47 N ALA A 48 1555 1555 1.33
LINK C PHE A 64 N MSE A 65 1555 1555 1.34
LINK C MSE A 65 N ALA A 66 1555 1555 1.33
LINK C ASP A 176 N MSE A 177 1555 1555 1.33
LINK C MSE A 177 N ASN A 178 1555 1555 1.34
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N TYR B 2 1555 1555 1.33
LINK C VAL B 23 N MSE B 24 1555 1555 1.33
LINK C MSE B 24 N LEU B 25 1555 1555 1.33
LINK C AGLU B 46 N MSE B 47 1555 1555 1.34
LINK C BGLU B 46 N MSE B 47 1555 1555 1.33
LINK C MSE B 47 N ALA B 48 1555 1555 1.33
LINK C PHE B 64 N MSE B 65 1555 1555 1.34
LINK C MSE B 65 N ALA B 66 1555 1555 1.34
LINK C ASP B 176 N MSE B 177 1555 1555 1.34
LINK C MSE B 177 N ASN B 178 1555 1555 1.34
LINK O GLN B 39 NA NA B 302 1555 1555 2.10
LINK NA NA B 302 O HOH B 451 1555 1555 2.15
LINK NA NA A 302 O HOH A 510 1555 1555 2.23
LINK NA NA B 302 O HOH B 469 1555 1555 2.42
LINK NA NA B 302 O HOH B 411 1555 1555 2.49
LINK O LEU B 42 NA NA B 302 1555 1555 2.52
LINK NA NA A 302 O HOH A 466 1555 1555 2.58
LINK O ILE A 205 NA NA A 302 1555 1555 2.75
LINK OXT LYS A 207 NA NA A 302 1555 1555 2.80
CISPEP 1 GLN A 72 PRO A 73 0 7.84
CISPEP 2 ASN A 157 PRO A 158 0 -7.17
CISPEP 3 GLN B 72 PRO B 73 0 6.24
CISPEP 4 ASN B 157 PRO B 158 0 -3.39
SITE 1 AC1 15 ARG A 28 TYR A 60 SER A 63 PHE A 64
SITE 2 AC1 15 SER A 105 GLN A 106 CYS A 109 THR A 129
SITE 3 AC1 15 GLY A 130 HIS A 161 VAL A 162 HIS A 191
SITE 4 AC1 15 HOH A 403 GOL B 303 HOH B 471
SITE 1 AC2 6 TYR A 100 ILE A 205 LEU A 206 LYS A 207
SITE 2 AC2 6 HOH A 466 HOH A 510
SITE 1 AC3 15 PRO A 160 ARG B 28 TYR B 60 SER B 63
SITE 2 AC3 15 PHE B 64 SER B 105 GLN B 106 CYS B 109
SITE 3 AC3 15 THR B 129 GLY B 130 HIS B 161 VAL B 162
SITE 4 AC3 15 HIS B 191 HOH B 462 HOH B 499
SITE 1 AC4 5 GLN B 39 LEU B 42 HOH B 411 HOH B 451
SITE 2 AC4 5 HOH B 469
SITE 1 AC5 7 ARG A 28 SER A 63 HIS A 161 CIT A 301
SITE 2 AC5 7 SER B 63 HOH B 419 HOH B 471
CRYST1 40.157 40.251 67.256 72.77 78.37 76.09 P 1 2
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 0.024902 -0.006168 -0.003644 0.00000
SCALE2 0.000000 0.025595 -0.006909 0.00000
SCALE3 0.000000 0.000000 0.015724 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
