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HEADER HYDROLASE 29-OCT-13 4CCY
TITLE CRYSTAL STRUCTURE OF CARBOXYLESTERASE CESB (YBFK) FROM
TITLE 2 BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE YBFK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-296;
COMPND 5 SYNONYM: CARBOXYLESTERASE CESB;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CARBOXYLESTERASE YBFK;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 1-296;
COMPND 12 SYNONYM: CARBOXYLESTERASE CESB;
COMPND 13 EC: 3.1.1.1;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PBAD/MYC-HISA;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 10 ORGANISM_TAXID: 224308;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PBAD/MYC-HISA
KEYWDS HYDROLASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.ROZEBOOM,L.F.GODINHO,M.NARDINI,W.J.QUAX,B.W.DIJKSTRA
REVDAT 1 22-JAN-14 4CCY 0
JRNL AUTH H.J.ROZEBOOM,L.F.GODINHO,M.NARDINI,W.J.QUAX,B.W.DIJKSTRA
JRNL TITL CRYSTAL STRUCTURES OF TWO BACILLUS CARBOXYLESTERASES WITH
JRNL TITL 2 DIFFERENT ENATIOSELECTIVITIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.04 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 108.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.59
REMARK 3 NUMBER OF REFLECTIONS : 44660
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) : 0.20599
REMARK 3 R VALUE (WORKING SET) : 0.20362
REMARK 3 FREE R VALUE : 0.25013
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2395
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) : 2.038
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.091
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.277
REMARK 3 BIN FREE R VALUE SET COUNT : 132
REMARK 3 BIN FREE R VALUE : 0.309
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4494
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.127
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15
REMARK 3 B22 (A**2) : -0.22
REMARK 3 B33 (A**2) : 0.04
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.41
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.193
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.309
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4623 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6281 ; 1.159 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 568 ; 5.701 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;36.704 ;23.832
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 739 ;14.279 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.794 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 678 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3558 ; 0.005 ; 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 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 12 A 294 5
REMARK 3 1 B 12 B 294 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1128 ; 0.06 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 B (A): 1104 ; 0.40 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1128 ; 0.82 ; 2.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1104 ; 0.96 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 11 A 26
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3692 -16.3236 53.9956
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.0783
REMARK 3 T33: 0.0925 T12: -0.0594
REMARK 3 T13: 0.0267 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 18.0463 L22: 4.5645
REMARK 3 L33: 7.4375 L12: -0.8082
REMARK 3 L13: 7.3228 L23: 1.1563
REMARK 3 S TENSOR
REMARK 3 S11: 0.1234 S12: -0.0592 S13: -0.1982
REMARK 3 S21: 0.0762 S22: -0.2386 S23: 0.2620
REMARK 3 S31: 0.5325 S32: -0.5180 S33: 0.1152
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 27 A 102
REMARK 3 ORIGIN FOR THE GROUP (A): 57.8041 -4.3721 60.7859
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: 0.0399
REMARK 3 T33: 0.0360 T12: -0.0085
REMARK 3 T13: 0.0114 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 2.0674 L22: 1.1494
REMARK 3 L33: 0.8676 L12: -0.5337
REMARK 3 L13: 0.1034 L23: -0.0817
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: -0.1813 S13: -0.0461
REMARK 3 S21: 0.0939 S22: -0.0428 S23: -0.0077
REMARK 3 S31: 0.0540 S32: -0.0175 S33: 0.0294
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 103 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0165 7.3833 53.5169
REMARK 3 T TENSOR
REMARK 3 T11: 0.0101 T22: 0.0196
REMARK 3 T33: 0.0599 T12: 0.0041
REMARK 3 T13: -0.0046 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.4476 L22: 0.7171
REMARK 3 L33: 1.3166 L12: 0.0385
REMARK 3 L13: -0.4505 L23: 0.0328
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.0177 S13: 0.0916
REMARK 3 S21: -0.0022 S22: -0.0454 S23: 0.0391
REMARK 3 S31: -0.1007 S32: -0.0167 S33: 0.0605
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 167 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6022 -9.6901 36.4500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0702 T22: 0.0886
REMARK 3 T33: 0.0675 T12: 0.0196
REMARK 3 T13: -0.0390 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 6.0672 L22: 2.6164
REMARK 3 L33: 2.4283 L12: -1.2270
REMARK 3 L13: 0.1492 L23: -2.4262
REMARK 3 S TENSOR
REMARK 3 S11: -0.0248 S12: 0.2676 S13: -0.3240
REMARK 3 S21: -0.1886 S22: 0.0482 S23: 0.0802
REMARK 3 S31: 0.1912 S32: -0.1052 S33: -0.0235
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 186 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0840 -12.8865 46.1062
REMARK 3 T TENSOR
REMARK 3 T11: 0.0250 T22: 0.0280
REMARK 3 T33: 0.0749 T12: -0.0034
REMARK 3 T13: -0.0212 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 3.2882 L22: 2.7602
REMARK 3 L33: 1.7926 L12: -2.1518
REMARK 3 L13: 0.0340 L23: 0.5419
REMARK 3 S TENSOR
REMARK 3 S11: 0.1970 S12: 0.1558 S13: -0.1803
REMARK 3 S21: -0.0886 S22: -0.2183 S23: 0.0725
REMARK 3 S31: 0.0821 S32: -0.0571 S33: 0.0213
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 214 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): 69.7687 4.3155 47.0800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0072 T22: 0.0417
REMARK 3 T33: 0.0595 T12: -0.0030
REMARK 3 T13: 0.0123 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 1.1959 L22: 1.0787
REMARK 3 L33: 1.0898 L12: -0.3378
REMARK 3 L13: 0.3908 L23: -0.2442
REMARK 3 S TENSOR
REMARK 3 S11: 0.0164 S12: 0.0590 S13: 0.0328
REMARK 3 S21: -0.0740 S22: -0.0287 S23: -0.0935
REMARK 3 S31: -0.0123 S32: 0.0859 S33: 0.0123
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 11 B 26
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0540 16.0301 30.4807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1167 T22: 0.0901
REMARK 3 T33: 0.0783 T12: 0.0042
REMARK 3 T13: 0.0513 T23: -0.0651
REMARK 3 L TENSOR
REMARK 3 L11: 6.3057 L22: 6.0642
REMARK 3 L33: 18.3086 L12: -2.9610
REMARK 3 L13: 2.0804 L23: -3.3796
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.6393 S13: 0.3828
REMARK 3 S21: 0.3597 S22: 0.0287 S23: 0.3136
REMARK 3 S31: -0.2111 S32: -0.3016 S33: -0.0208
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 27 B 102
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7093 4.0445 19.4100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0548 T22: 0.0392
REMARK 3 T33: 0.0280 T12: 0.0321
REMARK 3 T13: 0.0085 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.9600 L22: 0.8593
REMARK 3 L33: 2.3062 L12: 0.0919
REMARK 3 L13: -0.3629 L23: -0.4830
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: 0.0372 S13: 0.0788
REMARK 3 S21: -0.0278 S22: 0.0059 S23: 0.1180
REMARK 3 S31: -0.0593 S32: -0.1864 S33: -0.0163
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 103 B 175
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2806 -6.0000 21.0776
REMARK 3 T TENSOR
REMARK 3 T11: 0.0883 T22: 0.0479
REMARK 3 T33: 0.0126 T12: 0.0152
REMARK 3 T13: 0.0054 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.8494 L22: 1.0534
REMARK 3 L33: 1.1630 L12: -0.0076
REMARK 3 L13: 0.0373 L23: 0.0083
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.0431 S13: -0.0952
REMARK 3 S21: 0.0734 S22: -0.0035 S23: 0.0066
REMARK 3 S31: 0.0514 S32: -0.0010 S33: 0.0143
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 176 B 195
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0811 13.8109 22.0400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1239 T22: 0.0654
REMARK 3 T33: 0.0914 T12: -0.0608
REMARK 3 T13: -0.0217 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 3.9395 L22: 5.5779
REMARK 3 L33: 8.6866 L12: -4.5605
REMARK 3 L13: 2.5036 L23: -1.4519
REMARK 3 S TENSOR
REMARK 3 S11: 0.0706 S12: 0.0981 S13: 0.0726
REMARK 3 S21: -0.0639 S22: -0.0328 S23: -0.1065
REMARK 3 S31: 0.0412 S32: 0.5186 S33: -0.0378
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 196 B 213
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7558 11.4496 31.5104
REMARK 3 T TENSOR
REMARK 3 T11: 0.1410 T22: 0.0604
REMARK 3 T33: 0.0289 T12: -0.0220
REMARK 3 T13: 0.0100 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 2.8713 L22: 4.4300
REMARK 3 L33: 4.1811 L12: 1.6105
REMARK 3 L13: -0.5191 L23: -2.3496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: -0.3071 S13: 0.1302
REMARK 3 S21: 0.2453 S22: -0.1489 S23: -0.1757
REMARK 3 S31: -0.1765 S32: -0.2076 S33: 0.1283
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 214 B 294
REMARK 3 ORIGIN FOR THE GROUP (A): 44.5716 -4.6005 12.3558
REMARK 3 T TENSOR
REMARK 3 T11: 0.0690 T22: 0.0376
REMARK 3 T33: 0.0100 T12: 0.0165
REMARK 3 T13: 0.0095 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.8970 L22: 1.0443
REMARK 3 L33: 1.4752 L12: 0.0109
REMARK 3 L13: 0.1947 L23: -0.1322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: 0.0384 S13: -0.0368
REMARK 3 S21: -0.0362 S22: -0.0688 S23: -0.0725
REMARK 3 S31: 0.0128 S32: 0.0971 S33: 0.0567
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4CCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-13.
REMARK 100 THE PDBE ID CODE IS EBI-58837.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
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 : BRUKER MICROSTARH
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : HELIOSMX
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE (MAR345DTB)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47148
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.04
REMARK 200 RESOLUTION RANGE LOW (A) : 46.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.90
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 4CCW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROPS WITH 20% PEG3350,
REMARK 280 0.2M SODIUM FLUORIDE, 100 MM BIS-TRIS PROPANE BUFFER
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2250 LIES ON A SPECIAL POSITION.
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 2
REMARK 465 ILE A 3
REMARK 465 GLN A 4
REMARK 465 ASP A 5
REMARK 465 SER A 6
REMARK 465 MET A 7
REMARK 465 GLN A 8
REMARK 465 PHE A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 LYS A 297
REMARK 465 MET B 2
REMARK 465 ILE B 3
REMARK 465 GLN B 4
REMARK 465 ASP B 5
REMARK 465 SER B 6
REMARK 465 MET B 7
REMARK 465 GLN B 8
REMARK 465 PHE B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 LYS B 297
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 LEU A 65 -15.88 78.52
REMARK 500 SER A 67 174.51 63.41
REMARK 500 ASN A 94 -164.26 -175.25
REMARK 500 SER A 99 -110.04 -102.04
REMARK 500 SER A 130 -119.95 58.62
REMARK 500 GLU A 148 -91.43 -80.37
REMARK 500 GLU A 157 -122.14 54.47
REMARK 500 ALA A 158 -55.55 74.98
REMARK 500 LEU B 65 -12.63 80.48
REMARK 500 SER B 67 173.67 65.80
REMARK 500 ASN B 94 -165.36 -173.58
REMARK 500 SER B 99 -100.92 -106.14
REMARK 500 SER B 130 -118.43 56.36
REMARK 500 GLU B 148 -86.96 -86.29
REMARK 500 GLU B 157 -119.35 61.16
REMARK 500 ALA B 158 -54.71 69.16
REMARK 500
REMARK 500 REMARK: NULL
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 A1297 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2144 O
REMARK 620 2 HOH A2224 O 82.7
REMARK 620 3 GLU A 245 O 83.1 165.2
REMARK 620 4 TYR A 248 O 80.3 89.7 83.7
REMARK 620 5 GLN A 250 OE1 164.5 89.9 102.8 86.1
REMARK 620 6 HOH A2219 O 103.0 85.7 101.6 174.0 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1297 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 248 O
REMARK 620 2 GLN B 250 OE1 83.8
REMARK 620 3 GLU B 245 O 84.9 98.6
REMARK 620 4 HOH B2171 O 91.4 87.3 172.7
REMARK 620 5 HOH B2112 O 77.6 161.3 81.9 91.1
REMARK 620 6 HOH B2167 O 171.1 90.9 103.0 81.2 107.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1298 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 187 OG1
REMARK 620 2 HOH A2164 O 88.0
REMARK 620 3 HOH A2170 O 84.9 103.3
REMARK 620 4 HOH A2171 O 169.6 102.2 94.4
REMARK 620 5 GLY A 188 O 88.7 76.2 173.6 92.0
REMARK 620 6 TYR A 191 O 85.8 165.2 89.6 83.8 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1298 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 191 O
REMARK 620 2 HOH B2133 O 87.9
REMARK 620 3 GLY B 188 O 90.3 171.1
REMARK 620 4 HOH B2134 O 81.0 101.7 86.6
REMARK 620 5 THR B 187 OG1 83.7 81.3 89.9 164.3
REMARK 620 6 HOH B2129 O 167.1 102.1 78.5 104.4 89.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1298
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CCW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NAPROXEN ESTERASE (CARBOXYLESTERASE
REMARK 900 NP) FROM BACILLUS SUBTILIS
DBREF 4CCY A 2 297 UNP O31452 YBFK_BACSU 1 296
DBREF 4CCY B 2 297 UNP O31452 YBFK_BACSU 1 296
SEQRES 1 A 296 MET ILE GLN ASP SER MET GLN PHE ALA ALA VAL GLU SER
SEQRES 2 A 296 GLY LEU ARG PHE TYR GLN ALA TYR ASP GLN SER LEU SER
SEQRES 3 A 296 LEU TRP PRO ILE GLU SER GLU ALA PHE TYR VAL SER THR
SEQRES 4 A 296 ARG PHE GLY LYS THR HIS ILE ILE ALA SER GLY PRO LYS
SEQRES 5 A 296 ASP ALA PRO SER LEU ILE LEU LEU HIS GLY GLY LEU PHE
SEQRES 6 A 296 SER SER ALA MET TRP TYR PRO ASN ILE ALA ALA TRP SER
SEQRES 7 A 296 SER GLN PHE ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 8 A 296 LYS ASN LYS SER ILE PRO SER ALA ALA MET GLU THR ARG
SEQRES 9 A 296 ALA ASP PHE ALA GLU TRP MET LYS ASP VAL PHE ASP SER
SEQRES 10 A 296 LEU GLY LEU GLU THR ALA HIS LEU ALA GLY LEU SER LEU
SEQRES 11 A 296 GLY GLY SER HIS ILE VAL ASN PHE LEU LEU ARG ALA PRO
SEQRES 12 A 296 GLU ARG VAL GLU ARG ALA VAL VAL ILE SER PRO ALA GLU
SEQRES 13 A 296 ALA PHE ILE SER PHE HIS PRO ASP VAL TYR LYS TYR ALA
SEQRES 14 A 296 ALA GLU LEU THR GLY ALA ARG GLY ALA GLU SER TYR ILE
SEQRES 15 A 296 LYS TRP ILE THR GLY ASP SER TYR ASP LEU HIS PRO LEU
SEQRES 16 A 296 LEU GLN ARG GLN ILE VAL ALA GLY VAL GLU TRP GLN ASP
SEQRES 17 A 296 GLU GLN ARG SER LEU LYS PRO THR GLU ASN GLY PHE PRO
SEQRES 18 A 296 TYR VAL PHE THR ASP GLN GLU LEU LYS SER ILE GLN VAL
SEQRES 19 A 296 PRO VAL LEU LEU MET PHE GLY GLU HIS GLU ALA MET TYR
SEQRES 20 A 296 HIS GLN GLN MET ALA PHE GLU ARG ALA SER VAL LEU VAL
SEQRES 21 A 296 PRO GLY ILE GLN ALA GLU ILE VAL LYS ASN ALA GLY HIS
SEQRES 22 A 296 LEU LEU SER LEU GLU GLN PRO GLU TYR VAL ASN GLN ARG
SEQRES 23 A 296 VAL LEU SER PHE LEU CSO GLY GLY ILE LYS
SEQRES 1 B 296 MET ILE GLN ASP SER MET GLN PHE ALA ALA VAL GLU SER
SEQRES 2 B 296 GLY LEU ARG PHE TYR GLN ALA TYR ASP GLN SER LEU SER
SEQRES 3 B 296 LEU TRP PRO ILE GLU SER GLU ALA PHE TYR VAL SER THR
SEQRES 4 B 296 ARG PHE GLY LYS THR HIS ILE ILE ALA SER GLY PRO LYS
SEQRES 5 B 296 ASP ALA PRO SER LEU ILE LEU LEU HIS GLY GLY LEU PHE
SEQRES 6 B 296 SER SER ALA MET TRP TYR PRO ASN ILE ALA ALA TRP SER
SEQRES 7 B 296 SER GLN PHE ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 8 B 296 LYS ASN LYS SER ILE PRO SER ALA ALA MET GLU THR ARG
SEQRES 9 B 296 ALA ASP PHE ALA GLU TRP MET LYS ASP VAL PHE ASP SER
SEQRES 10 B 296 LEU GLY LEU GLU THR ALA HIS LEU ALA GLY LEU SER LEU
SEQRES 11 B 296 GLY GLY SER HIS ILE VAL ASN PHE LEU LEU ARG ALA PRO
SEQRES 12 B 296 GLU ARG VAL GLU ARG ALA VAL VAL ILE SER PRO ALA GLU
SEQRES 13 B 296 ALA PHE ILE SER PHE HIS PRO ASP VAL TYR LYS TYR ALA
SEQRES 14 B 296 ALA GLU LEU THR GLY ALA ARG GLY ALA GLU SER TYR ILE
SEQRES 15 B 296 LYS TRP ILE THR GLY ASP SER TYR ASP LEU HIS PRO LEU
SEQRES 16 B 296 LEU GLN ARG GLN ILE VAL ALA GLY VAL GLU TRP GLN ASP
SEQRES 17 B 296 GLU GLN ARG SER LEU LYS PRO THR GLU ASN GLY PHE PRO
SEQRES 18 B 296 TYR VAL PHE THR ASP GLN GLU LEU LYS SER ILE GLN VAL
SEQRES 19 B 296 PRO VAL LEU LEU MET PHE GLY GLU HIS GLU ALA MET TYR
SEQRES 20 B 296 HIS GLN GLN MET ALA PHE GLU ARG ALA SER VAL LEU VAL
SEQRES 21 B 296 PRO GLY ILE GLN ALA GLU ILE VAL LYS ASN ALA GLY HIS
SEQRES 22 B 296 LEU LEU SER LEU GLU GLN PRO GLU TYR VAL ASN GLN ARG
SEQRES 23 B 296 VAL LEU SER PHE LEU CYS GLY GLY ILE LYS
MODRES 4CCY CSO A 293 CYS S-HYDROXYCYSTEINE
HET CSO A 293 7
HET NA A1297 1
HET NA A1298 1
HET NA B1297 1
HET NA B1298 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM NA SODIUM ION
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 2 NA 4(NA 1+)
FORMUL 3 HOH *454(H2 O)
HELIX 1 1 VAL A 12 LEU A 26 1 15
HELIX 2 2 SER A 27 TRP A 29 5 3
HELIX 3 3 SER A 67 MET A 70 5 4
HELIX 4 4 TRP A 71 PHE A 82 1 12
HELIX 5 5 THR A 104 GLY A 120 1 17
HELIX 6 6 SER A 130 ALA A 143 1 14
HELIX 7 7 PRO A 164 GLU A 172 1 9
HELIX 8 8 GLY A 175 GLY A 188 1 14
HELIX 9 9 HIS A 194 TRP A 207 1 14
HELIX 10 10 ASP A 209 SER A 213 5 5
HELIX 11 11 THR A 226 SER A 232 1 7
HELIX 12 12 HIS A 249 VAL A 261 1 13
HELIX 13 13 LEU A 275 GLN A 280 1 6
HELIX 14 14 GLN A 280 CSO A 293 1 14
HELIX 15 15 VAL B 12 LEU B 26 1 15
HELIX 16 16 SER B 27 TRP B 29 5 3
HELIX 17 17 SER B 67 TYR B 72 5 6
HELIX 18 18 ASN B 74 SER B 79 1 6
HELIX 19 19 THR B 104 GLY B 120 1 17
HELIX 20 20 SER B 130 ALA B 143 1 14
HELIX 21 21 PRO B 164 GLU B 172 1 9
HELIX 22 22 GLY B 175 GLY B 188 1 14
HELIX 23 23 HIS B 194 TRP B 207 1 14
HELIX 24 24 ASP B 209 SER B 213 5 5
HELIX 25 25 THR B 226 SER B 232 1 7
HELIX 26 26 HIS B 249 VAL B 261 1 13
HELIX 27 27 LEU B 275 GLN B 280 1 6
HELIX 28 28 GLN B 280 CYS B 293 1 14
SHEET 1 AA 2 GLU A 34 VAL A 38 0
SHEET 2 AA 2 GLY A 43 SER A 50 -1 O THR A 45 N VAL A 38
SHEET 1 AB 2 ILE A 97 PRO A 98 0
SHEET 2 AB 2 GLY A 43 SER A 50 1 O LYS A 44 N ILE A 97
SHEET 1 AC 8 GLN A 265 VAL A 269 0
SHEET 2 AC 8 VAL A 237 GLY A 242 1 O VAL A 237 N GLN A 265
SHEET 3 AC 8 VAL A 147 ILE A 153 1 O ALA A 150 N LEU A 238
SHEET 4 AC 8 ALA A 124 LEU A 129 1 O ALA A 124 N GLU A 148
SHEET 5 AC 8 SER A 57 LEU A 61 1 O SER A 57 N HIS A 125
SHEET 6 AC 8 ARG A 83 VAL A 87 1 O ARG A 83 N LEU A 58
SHEET 7 AC 8 GLY A 43 SER A 50 -1 O ILE A 48 N ALA A 86
SHEET 8 AC 8 ILE A 97 PRO A 98 1 O ILE A 97 N LYS A 44
SHEET 1 AD 8 GLN A 265 VAL A 269 0
SHEET 2 AD 8 VAL A 237 GLY A 242 1 O VAL A 237 N GLN A 265
SHEET 3 AD 8 VAL A 147 ILE A 153 1 O ALA A 150 N LEU A 238
SHEET 4 AD 8 ALA A 124 LEU A 129 1 O ALA A 124 N GLU A 148
SHEET 5 AD 8 SER A 57 LEU A 61 1 O SER A 57 N HIS A 125
SHEET 6 AD 8 ARG A 83 VAL A 87 1 O ARG A 83 N LEU A 58
SHEET 7 AD 8 GLY A 43 SER A 50 -1 O ILE A 48 N ALA A 86
SHEET 8 AD 8 GLU A 34 VAL A 38 -1 O GLU A 34 N ALA A 49
SHEET 1 BA 2 GLU B 34 VAL B 38 0
SHEET 2 BA 2 GLY B 43 SER B 50 -1 O THR B 45 N VAL B 38
SHEET 1 BB 2 ILE B 97 PRO B 98 0
SHEET 2 BB 2 GLY B 43 SER B 50 1 O LYS B 44 N ILE B 97
SHEET 1 BC 8 GLN B 265 VAL B 269 0
SHEET 2 BC 8 VAL B 237 GLY B 242 1 O VAL B 237 N GLN B 265
SHEET 3 BC 8 VAL B 147 ILE B 153 1 O ALA B 150 N LEU B 238
SHEET 4 BC 8 ALA B 124 LEU B 129 1 O ALA B 124 N GLU B 148
SHEET 5 BC 8 SER B 57 LEU B 61 1 O SER B 57 N HIS B 125
SHEET 6 BC 8 ARG B 83 VAL B 87 1 O ARG B 83 N LEU B 58
SHEET 7 BC 8 GLY B 43 SER B 50 -1 O ILE B 48 N ALA B 86
SHEET 8 BC 8 ILE B 97 PRO B 98 1 O ILE B 97 N LYS B 44
SHEET 1 BD 8 GLN B 265 VAL B 269 0
SHEET 2 BD 8 VAL B 237 GLY B 242 1 O VAL B 237 N GLN B 265
SHEET 3 BD 8 VAL B 147 ILE B 153 1 O ALA B 150 N LEU B 238
SHEET 4 BD 8 ALA B 124 LEU B 129 1 O ALA B 124 N GLU B 148
SHEET 5 BD 8 SER B 57 LEU B 61 1 O SER B 57 N HIS B 125
SHEET 6 BD 8 ARG B 83 VAL B 87 1 O ARG B 83 N LEU B 58
SHEET 7 BD 8 GLY B 43 SER B 50 -1 O ILE B 48 N ALA B 86
SHEET 8 BD 8 GLU B 34 VAL B 38 -1 O GLU B 34 N ALA B 49
LINK C LEU A 292 N CSO A 293 1555 1555 1.34
LINK C CSO A 293 N GLY A 294 1555 1555 1.33
LINK NA NA A1297 O HOH A2144 1555 1555 2.66
LINK NA NA A1297 O HOH A2224 1555 1555 2.53
LINK NA NA A1297 O GLU A 245 1555 1555 2.30
LINK NA NA A1297 O TYR A 248 1555 1555 2.64
LINK NA NA A1297 OE1 GLN A 250 1555 1555 2.31
LINK NA NA A1297 O HOH A2219 1555 1555 2.44
LINK NA NA A1298 O TYR A 191 1555 1555 2.43
LINK NA NA A1298 O GLY A 188 1555 1555 2.39
LINK NA NA A1298 O HOH A2171 1555 1555 2.29
LINK NA NA A1298 O HOH A2170 1555 1555 2.35
LINK NA NA A1298 O HOH A2164 1555 1555 2.21
LINK NA NA A1298 OG1 THR A 187 1555 1555 2.45
LINK NA NA B1297 O HOH B2167 1555 1555 2.47
LINK NA NA B1297 O HOH B2112 1555 1555 2.40
LINK NA NA B1297 O HOH B2171 1555 1555 2.52
LINK NA NA B1297 O GLU B 245 1555 1555 2.30
LINK NA NA B1297 OE1 GLN B 250 1555 1555 2.34
LINK NA NA B1297 O TYR B 248 1555 1555 2.69
LINK NA NA B1298 O HOH B2133 1555 1555 2.61
LINK NA NA B1298 O GLY B 188 1555 1555 2.28
LINK NA NA B1298 O HOH B2134 1555 1555 2.29
LINK NA NA B1298 OG1 THR B 187 1555 1555 2.54
LINK NA NA B1298 O HOH B2129 1555 1555 2.13
LINK NA NA B1298 O TYR B 191 1555 1555 2.44
CISPEP 1 PHE A 221 PRO A 222 0 -4.59
CISPEP 2 PHE B 221 PRO B 222 0 -3.64
SITE 1 AC1 6 GLU A 245 TYR A 248 GLN A 250 HOH A2144
SITE 2 AC1 6 HOH A2219 HOH A2224
SITE 1 AC2 7 THR A 187 GLY A 188 TYR A 191 ASP A 192
SITE 2 AC2 7 HOH A2164 HOH A2170 HOH A2171
SITE 1 AC3 6 GLU B 245 TYR B 248 GLN B 250 HOH B2112
SITE 2 AC3 6 HOH B2167 HOH B2171
SITE 1 AC4 7 THR B 187 GLY B 188 TYR B 191 ASP B 192
SITE 2 AC4 7 HOH B2129 HOH B2133 HOH B2134
CRYST1 82.110 44.010 108.660 90.00 91.87 90.00 P 1 2 1 4
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 0.012179 0.000000 0.000398 0.00000
SCALE2 0.000000 0.022722 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009208 0.00000
MTRIX1 1 0.314500 0.001922 -0.949300 67.49000 1
MTRIX2 1 0.003592 -1.000000 -0.000835 -0.41170 1
MTRIX3 1 -0.949300 -0.003147 -0.314500 93.20000 1
TER 2252 ILE A 296
TER 4503 ILE B 296
MASTER 604 0 5 28 40 0 8 9 4959 2 41 46
END |