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HEADER HYDROLASE 23-MAY-09 3A2N
TITLE CRYSTAL STRUCTURE OF DBJA (WILD TYPE TYPE II P21)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM JAPONICUM;
SOURCE 3 ORGANISM_TAXID: 375;
SOURCE 4 STRAIN: USDA110;
SOURCE 5 GENE: DBJA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PYBJA3
KEYWDS A/B-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SATO,T.SENDA
REVDAT 2 27-OCT-10 3A2N 1 JRNL
REVDAT 1 26-MAY-10 3A2N 0
JRNL AUTH Z.PROKOP,Y.SATO,J.BREZOVSKY,T.MOZGA,R.CHALOUPKOVA,
JRNL AUTH 2 T.KOUDELAKOVA,P.JERABEK,V.STEPANKOVA,R.NATSUME,
JRNL AUTH 3 J.G.VAN LEEUWEN,D.B.JANSSEN,J.FLORIAN,Y.NAGATA,T.SENDA,
JRNL AUTH 4 J.DAMBORSKY
JRNL TITL ENANTIOSELECTIVITY OF HALOALKANE DEHALOGENASES AND ITS
JRNL TITL 2 MODULATION BY SURFACE LOOP ENGINEERING
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 49 6111 2010
JRNL REFN ISSN 1433-7851
JRNL PMID 20645368
JRNL DOI 10.1002/ANIE.201001753
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 89306
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4717
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) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6326
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 374
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 489
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.613
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9584 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13055 ; 1.333 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1193 ; 5.395 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 454 ;33.653 ;21.938
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1408 ;14.541 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;20.431 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1388 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7604 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4774 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6551 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 603 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 131 ; 0.239 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.153 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6141 ; 0.694 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9579 ; 1.096 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3890 ; 1.845 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3476 ; 2.897 ; 4.500
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 : 16
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 10 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6225 4.7015 10.9510
REMARK 3 T TENSOR
REMARK 3 T11: -0.0492 T22: -0.0161
REMARK 3 T33: -0.0584 T12: -0.0081
REMARK 3 T13: 0.0046 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.0940 L22: 0.6194
REMARK 3 L33: 1.3282 L12: -0.3817
REMARK 3 L13: 0.6276 L23: -0.3063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0649 S12: -0.0102 S13: 0.2128
REMARK 3 S21: 0.0042 S22: -0.0434 S23: -0.0497
REMARK 3 S31: -0.1651 S32: -0.1397 S33: 0.1083
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 135 A 163
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0825 -20.3806 14.9031
REMARK 3 T TENSOR
REMARK 3 T11: 0.1336 T22: -0.1007
REMARK 3 T33: 0.1322 T12: -0.0715
REMARK 3 T13: -0.0059 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 8.8212 L22: 2.8965
REMARK 3 L33: 3.7428 L12: -2.1241
REMARK 3 L13: -1.5652 L23: 0.6468
REMARK 3 S TENSOR
REMARK 3 S11: -0.2960 S12: -0.3402 S13: -1.2338
REMARK 3 S21: 0.3766 S22: 0.2790 S23: -0.2527
REMARK 3 S31: 0.9261 S32: 0.0626 S33: 0.0170
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 164 A 180
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4108 -9.3387 17.9934
REMARK 3 T TENSOR
REMARK 3 T11: -0.1142 T22: 0.1345
REMARK 3 T33: -0.1148 T12: -0.1537
REMARK 3 T13: 0.0222 T23: 0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 10.4809 L22: 1.0017
REMARK 3 L33: 8.1633 L12: 0.1288
REMARK 3 L13: 3.0249 L23: -0.2975
REMARK 3 S TENSOR
REMARK 3 S11: 0.1218 S12: -0.5340 S13: -0.3564
REMARK 3 S21: 0.0225 S22: -0.1719 S23: -0.0291
REMARK 3 S31: 0.3880 S32: -0.5871 S33: 0.0501
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 181 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8943 -6.7628 15.3078
REMARK 3 T TENSOR
REMARK 3 T11: -0.0596 T22: -0.0380
REMARK 3 T33: -0.0977 T12: -0.0398
REMARK 3 T13: 0.0212 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 2.3434 L22: 0.6354
REMARK 3 L33: 1.2600 L12: 0.2124
REMARK 3 L13: 0.3748 L23: -0.1751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0472 S12: -0.2074 S13: -0.1969
REMARK 3 S21: 0.0104 S22: -0.0239 S23: -0.0501
REMARK 3 S31: 0.1664 S32: -0.1880 S33: -0.0232
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 10 B 134
REMARK 3 ORIGIN FOR THE GROUP (A): 49.0899 -3.6919 30.1528
REMARK 3 T TENSOR
REMARK 3 T11: 0.0008 T22: -0.0946
REMARK 3 T33: -0.0309 T12: 0.0103
REMARK 3 T13: 0.0250 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.1784 L22: 0.8599
REMARK 3 L33: 1.1293 L12: -0.0275
REMARK 3 L13: 0.0116 L23: -0.3633
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: 0.0967 S13: -0.0374
REMARK 3 S21: -0.0275 S22: -0.0435 S23: -0.0904
REMARK 3 S31: 0.1032 S32: 0.0720 S33: 0.0160
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 135 B 163
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8698 14.7360 48.2632
REMARK 3 T TENSOR
REMARK 3 T11: 0.0747 T22: -0.1136
REMARK 3 T33: -0.0199 T12: 0.0061
REMARK 3 T13: 0.0495 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 5.2886 L22: 3.3884
REMARK 3 L33: 5.3669 L12: -1.9696
REMARK 3 L13: 2.0111 L23: -1.3904
REMARK 3 S TENSOR
REMARK 3 S11: -0.0514 S12: -0.4342 S13: 0.3121
REMARK 3 S21: 0.2860 S22: 0.1030 S23: 0.2199
REMARK 3 S31: -0.5947 S32: -0.4360 S33: -0.0516
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 164 B 180
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7395 0.0993 53.8973
REMARK 3 T TENSOR
REMARK 3 T11: 0.0479 T22: -0.0602
REMARK 3 T33: -0.0963 T12: -0.0096
REMARK 3 T13: 0.0203 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 8.9939 L22: 1.4530
REMARK 3 L33: 4.5990 L12: -0.2183
REMARK 3 L13: 4.3969 L23: 0.6235
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: -0.1936 S13: 0.0273
REMARK 3 S21: 0.2351 S22: 0.0125 S23: 0.0314
REMARK 3 S31: -0.1150 S32: 0.0433 S33: 0.0453
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 181 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9010 4.5564 35.9628
REMARK 3 T TENSOR
REMARK 3 T11: -0.0115 T22: -0.1073
REMARK 3 T33: -0.0509 T12: 0.0093
REMARK 3 T13: 0.0321 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.0863 L22: 0.5991
REMARK 3 L33: 1.3220 L12: -0.0284
REMARK 3 L13: 0.1179 L23: -0.3088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: -0.0429 S13: 0.1087
REMARK 3 S21: 0.0897 S22: 0.0292 S23: 0.0136
REMARK 3 S31: -0.0827 S32: -0.0867 S33: -0.0243
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 : E 10 E 134
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5761 -0.9999 -31.8780
REMARK 3 T TENSOR
REMARK 3 T11: -0.1992 T22: 0.3974
REMARK 3 T33: 0.0807 T12: -0.0044
REMARK 3 T13: -0.0529 T23: -0.2857
REMARK 3 L TENSOR
REMARK 3 L11: 3.7370 L22: 2.5204
REMARK 3 L33: 3.6615 L12: -1.4769
REMARK 3 L13: -1.1497 L23: 0.5807
REMARK 3 S TENSOR
REMARK 3 S11: 0.1850 S12: 0.8795 S13: -0.8554
REMARK 3 S21: -0.1675 S22: -0.5237 S23: 0.6527
REMARK 3 S31: 0.1373 S32: -1.3356 S33: 0.3387
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 : E 135 E 163
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8264 17.9910 -48.5633
REMARK 3 T TENSOR
REMARK 3 T11: 0.0324 T22: 0.0725
REMARK 3 T33: 0.0062 T12: 0.3082
REMARK 3 T13: 0.0666 T23: 0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 3.8745 L22: 7.9236
REMARK 3 L33: 9.4451 L12: 3.6848
REMARK 3 L13: 1.8766 L23: 4.7010
REMARK 3 S TENSOR
REMARK 3 S11: 0.4433 S12: 0.7680 S13: 0.5257
REMARK 3 S21: -0.6642 S22: 0.0310 S23: -1.2701
REMARK 3 S31: -1.0755 S32: -0.9272 S33: -0.4743
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 : E 164 E 180
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2933 3.6846 -55.1559
REMARK 3 T TENSOR
REMARK 3 T11: 0.0780 T22: 0.0243
REMARK 3 T33: -0.0042 T12: 0.0322
REMARK 3 T13: -0.0496 T23: -0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 45.8756 L22: 3.5504
REMARK 3 L33: 89.5180 L12: -4.9862
REMARK 3 L13: 14.8698 L23: 14.3465
REMARK 3 S TENSOR
REMARK 3 S11: -0.4406 S12: 0.9609 S13: 2.0832
REMARK 3 S21: 0.0388 S22: -0.0707 S23: 0.1242
REMARK 3 S31: -0.2477 S32: 0.0965 S33: 0.5113
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 : E 181 E 300
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1481 7.3928 -36.7704
REMARK 3 T TENSOR
REMARK 3 T11: -0.0102 T22: 0.2922
REMARK 3 T33: -0.1110 T12: 0.1921
REMARK 3 T13: 0.0020 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 2.9150 L22: 0.9004
REMARK 3 L33: 2.8140 L12: -1.0882
REMARK 3 L13: -0.7732 L23: 0.7352
REMARK 3 S TENSOR
REMARK 3 S11: 0.4004 S12: 0.7871 S13: -0.0927
REMARK 3 S21: -0.2507 S22: -0.4010 S23: 0.0836
REMARK 3 S31: -0.2927 S32: -0.7843 S33: 0.0006
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 : F 10 F 134
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6705 4.7336 -11.0786
REMARK 3 T TENSOR
REMARK 3 T11: 0.0133 T22: -0.0747
REMARK 3 T33: -0.0293 T12: -0.0016
REMARK 3 T13: 0.0159 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.3297 L22: 0.4916
REMARK 3 L33: 0.6051 L12: 0.1094
REMARK 3 L13: 0.1040 L23: 0.4118
REMARK 3 S TENSOR
REMARK 3 S11: -0.0229 S12: -0.0069 S13: 0.0913
REMARK 3 S21: -0.0351 S22: -0.0143 S23: 0.0098
REMARK 3 S31: -0.0784 S32: -0.0329 S33: 0.0372
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 : F 135 F 163
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8989 -20.7211 -14.7964
REMARK 3 T TENSOR
REMARK 3 T11: 0.0581 T22: -0.1488
REMARK 3 T33: 0.0492 T12: 0.0043
REMARK 3 T13: 0.0355 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 6.5957 L22: 2.9031
REMARK 3 L33: 1.3598 L12: 2.4887
REMARK 3 L13: 1.8983 L23: 0.8855
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: 0.2221 S13: -0.6429
REMARK 3 S21: -0.0792 S22: 0.0312 S23: -0.0815
REMARK 3 S31: 0.2404 S32: 0.1092 S33: -0.1078
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 : F 164 F 180
REMARK 3 ORIGIN FOR THE GROUP (A): 67.5832 -10.8600 -17.5354
REMARK 3 T TENSOR
REMARK 3 T11: 0.0022 T22: -0.0654
REMARK 3 T33: -0.0089 T12: 0.0177
REMARK 3 T13: 0.0365 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 4.4949 L22: 0.8377
REMARK 3 L33: 4.0070 L12: -0.9036
REMARK 3 L13: 2.4786 L23: 0.6371
REMARK 3 S TENSOR
REMARK 3 S11: 0.1058 S12: 0.1522 S13: -0.2575
REMARK 3 S21: -0.0408 S22: 0.0015 S23: 0.0248
REMARK 3 S31: 0.1707 S32: 0.1299 S33: -0.1073
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 181 F 300
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5660 -6.5638 -15.4452
REMARK 3 T TENSOR
REMARK 3 T11: -0.0130 T22: -0.0854
REMARK 3 T33: -0.0458 T12: -0.0132
REMARK 3 T13: 0.0248 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.3581 L22: 0.6161
REMARK 3 L33: 0.7533 L12: -0.3397
REMARK 3 L13: 0.0430 L23: 0.1951
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.1249 S13: -0.1555
REMARK 3 S21: -0.0154 S22: -0.0216 S23: 0.0478
REMARK 3 S31: 0.0591 S32: -0.0260 S33: 0.0237
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3A2N COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB028734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94042
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 14.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3A2M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 7.9, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 23.88300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 ILE A 5
REMARK 465 GLU A 6
REMARK 465 ILE A 7
REMARK 465 GLU A 8
REMARK 465 ILE A 9
REMARK 465 LEU A 308
REMARK 465 ALA A 309
REMARK 465 ALA A 310
REMARK 465 VAL A 311
REMARK 465 ASP A 312
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 ILE B 5
REMARK 465 GLU B 6
REMARK 465 ILE B 7
REMARK 465 GLU B 8
REMARK 465 ILE B 9
REMARK 465 LEU B 308
REMARK 465 ALA B 309
REMARK 465 ALA B 310
REMARK 465 VAL B 311
REMARK 465 ASP B 312
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 LYS E 3
REMARK 465 PRO E 4
REMARK 465 ILE E 5
REMARK 465 GLU E 6
REMARK 465 ILE E 7
REMARK 465 GLU E 8
REMARK 465 ILE E 9
REMARK 465 LEU E 308
REMARK 465 ALA E 309
REMARK 465 ALA E 310
REMARK 465 VAL E 311
REMARK 465 ASP E 312
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 LYS F 3
REMARK 465 PRO F 4
REMARK 465 ILE F 5
REMARK 465 GLU F 6
REMARK 465 ILE F 7
REMARK 465 GLU F 8
REMARK 465 LEU F 308
REMARK 465 ALA F 309
REMARK 465 ALA F 310
REMARK 465 VAL F 311
REMARK 465 ASP F 312
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 ASP E 73 CG ASP E 73 OD1 0.234
REMARK 500 ASP E 73 CG ASP E 73 OD2 0.282
REMARK 500 TYR E 76 C TYR E 76 O 0.229
REMARK 500 HIS E 81 CG HIS E 81 CD2 0.072
REMARK 500 GLU E 167 CD GLU E 167 OE1 0.088
REMARK 500 ARG E 208 CZ ARG E 208 NH1 0.083
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ASP E 73 CB - CG - OD1 ANGL. DEV. = -10.4 DEGREES
REMARK 500 TYR E 76 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR E 76 CG - CD2 - CE2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP E 80 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG E 208 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
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 SER A 17 -153.59 -120.37
REMARK 500 ALA A 26 -143.52 -100.52
REMARK 500 GLN A 27 -34.98 -130.86
REMARK 500 PRO A 39 56.78 -106.51
REMARK 500 THR A 40 -156.99 -107.87
REMARK 500 LYS A 71 64.54 -118.81
REMARK 500 ASP A 103 -133.36 56.58
REMARK 500 ALA A 144 -120.68 -39.60
REMARK 500 GLU A 145 15.93 -69.40
REMARK 500 ALA A 253 -76.81 -139.25
REMARK 500 LEU A 279 -112.63 -118.91
REMARK 500 PRO A 306 107.33 -23.79
REMARK 500 SER B 17 -149.83 -118.08
REMARK 500 PRO B 39 53.95 -107.95
REMARK 500 THR B 40 -160.52 -105.02
REMARK 500 ASP B 103 -133.39 62.69
REMARK 500 ALA B 253 -74.05 -145.23
REMARK 500 LEU B 279 -112.72 -118.08
REMARK 500 ARG B 305 -154.44 -36.00
REMARK 500 PRO B 306 111.41 -21.37
REMARK 500 SER E 17 -161.81 -110.81
REMARK 500 PRO E 39 48.31 -101.07
REMARK 500 THR E 40 -155.96 -100.96
REMARK 500 ASP E 103 -135.49 60.85
REMARK 500 GLN E 136 34.66 -78.06
REMARK 500 ASP E 137 -7.43 -143.34
REMARK 500 GLN E 147 -79.15 -63.68
REMARK 500 ASP E 148 -68.27 -3.82
REMARK 500 PRO E 163 80.78 -68.36
REMARK 500 PRO E 204 -48.83 -24.93
REMARK 500 ALA E 253 -75.66 -148.00
REMARK 500 LEU E 279 -121.34 -126.14
REMARK 500 ARG E 305 -170.60 -24.04
REMARK 500 SER F 17 -150.59 -117.10
REMARK 500 PRO F 39 55.61 -106.20
REMARK 500 THR F 40 -161.82 -107.09
REMARK 500 ASP F 103 -131.92 58.79
REMARK 500 ARG F 179 -54.95 -126.22
REMARK 500 ALA F 253 -74.50 -138.45
REMARK 500 LEU F 279 -108.92 -120.81
REMARK 500 PRO F 306 96.73 -20.42
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 CL A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 313
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A1O RELATED DB: PDB
REMARK 900 HIS-DBJA
REMARK 900 RELATED ID: 3A2L RELATED DB: PDB
REMARK 900 MUTANT DBJA
REMARK 900 RELATED ID: 3A2M RELATED DB: PDB
REMARK 900 DBJA (WILD TYPE, TYPE I)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 VAL AND ASP WERE ADDED TO C-TERMINUS. THE DBJAWT CONSTRUCT CODES
REMARK 999 FOR RESIDUES 1-310 OF DBJA WITH C-TERMINUS FUSED TO A RESTRICTION
REMARK 999 SITE OF SAL I WITH SEQUENCE AVD, WHERE A IS RESIDUE 310 OF THE
REMARK 999 DBJAWT SEQUENCE.
DBREF 3A2N A 1 310 UNP P59337 DHAA_BRAJA 1 310
DBREF 3A2N B 1 310 UNP P59337 DHAA_BRAJA 1 310
DBREF 3A2N E 1 310 UNP P59337 DHAA_BRAJA 1 310
DBREF 3A2N F 1 310 UNP P59337 DHAA_BRAJA 1 310
SEQADV 3A2N VAL A 311 UNP P59337 SEE REMARK 999
SEQADV 3A2N ASP A 312 UNP P59337 SEE REMARK 999
SEQADV 3A2N VAL B 311 UNP P59337 SEE REMARK 999
SEQADV 3A2N ASP B 312 UNP P59337 SEE REMARK 999
SEQADV 3A2N VAL E 311 UNP P59337 SEE REMARK 999
SEQADV 3A2N ASP E 312 UNP P59337 SEE REMARK 999
SEQADV 3A2N VAL F 311 UNP P59337 SEE REMARK 999
SEQADV 3A2N ASP F 312 UNP P59337 SEE REMARK 999
SEQRES 1 A 312 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 A 312 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 A 312 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 312 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 A 312 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 312 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 A 312 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 A 312 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 A 312 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 A 312 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 312 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 A 312 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 A 312 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 A 312 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 A 312 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 A 312 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 A 312 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 A 312 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 A 312 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 A 312 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 A 312 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 A 312 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 A 312 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 A 312 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA VAL ASP
SEQRES 1 B 312 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 B 312 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 B 312 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 312 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 B 312 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 B 312 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 B 312 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 B 312 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 B 312 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 B 312 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 B 312 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 B 312 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 B 312 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 B 312 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 B 312 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 B 312 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 B 312 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 B 312 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 B 312 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 B 312 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 B 312 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 B 312 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 B 312 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 B 312 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA VAL ASP
SEQRES 1 E 312 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 E 312 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 E 312 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 E 312 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 E 312 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 E 312 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 E 312 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 E 312 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 E 312 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 E 312 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 E 312 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 E 312 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 E 312 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 E 312 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 E 312 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 E 312 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 E 312 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 E 312 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 E 312 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 E 312 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 E 312 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 E 312 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 E 312 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 E 312 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA VAL ASP
SEQRES 1 F 312 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 F 312 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 F 312 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 F 312 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 F 312 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 F 312 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 F 312 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 F 312 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 F 312 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 F 312 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 F 312 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 F 312 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 F 312 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 F 312 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 F 312 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 F 312 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 F 312 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 F 312 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 F 312 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 F 312 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 F 312 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 F 312 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 F 312 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 F 312 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA VAL ASP
HET CL A 313 1
HET CL B 313 1
HET CL F 313 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 3(CL 1-)
FORMUL 8 HOH *489(H2 O)
HELIX 1 1 SER A 41 ARG A 46 5 6
HELIX 2 2 ILE A 48 SER A 53 1 6
HELIX 3 3 ARG A 77 GLY A 93 1 17
HELIX 4 4 ASP A 103 ARG A 116 1 14
HELIX 5 5 THR A 134 PHE A 138 5 5
HELIX 6 6 GLU A 145 ARG A 161 1 17
HELIX 7 7 GLY A 164 LEU A 171 1 8
HELIX 8 8 ASN A 174 ARG A 179 1 6
HELIX 9 9 ARG A 179 GLY A 184 1 6
HELIX 10 10 GLY A 190 THR A 199 1 10
HELIX 11 11 PRO A 204 SER A 206 5 3
HELIX 12 12 ARG A 207 LEU A 217 1 11
HELIX 13 13 PRO A 223 SER A 240 1 18
HELIX 14 14 SER A 256 LEU A 267 1 12
HELIX 15 15 TYR A 281 ARG A 305 1 25
HELIX 16 16 SER B 41 ARG B 46 5 6
HELIX 17 17 ILE B 48 SER B 53 1 6
HELIX 18 18 ARG B 77 ARG B 92 1 16
HELIX 19 19 ASP B 103 ARG B 116 1 14
HELIX 20 20 THR B 134 PHE B 138 5 5
HELIX 21 21 VAL B 143 GLU B 145 5 3
HELIX 22 22 GLU B 146 THR B 162 1 17
HELIX 23 23 GLY B 164 LEU B 171 1 8
HELIX 24 24 ASN B 174 ARG B 179 1 6
HELIX 25 25 ARG B 179 GLY B 184 1 6
HELIX 26 26 GLY B 190 THR B 199 1 10
HELIX 27 27 PRO B 204 SER B 206 5 3
HELIX 28 28 ARG B 207 PHE B 213 1 7
HELIX 29 29 PRO B 214 LEU B 217 5 4
HELIX 30 30 PRO B 223 SER B 240 1 18
HELIX 31 31 SER B 256 LEU B 267 1 12
HELIX 32 32 TYR B 281 ARG B 305 1 25
HELIX 33 33 SER E 41 ARG E 46 5 6
HELIX 34 34 ILE E 48 SER E 53 1 6
HELIX 35 35 ARG E 77 ARG E 92 1 16
HELIX 36 36 ASP E 103 ARG E 116 1 14
HELIX 37 37 GLU E 146 ARG E 161 1 16
HELIX 38 38 GLY E 164 LEU E 171 1 8
HELIX 39 39 ASN E 174 ARG E 179 1 6
HELIX 40 40 ARG E 179 GLY E 184 1 6
HELIX 41 41 GLY E 190 THR E 199 1 10
HELIX 42 42 THR E 203 SER E 206 5 4
HELIX 43 43 ARG E 207 PHE E 213 1 7
HELIX 44 44 PRO E 223 SER E 240 1 18
HELIX 45 45 SER E 256 LEU E 267 1 12
HELIX 46 46 TYR E 281 ARG E 305 1 25
HELIX 47 47 SER F 41 ARG F 46 5 6
HELIX 48 48 ILE F 48 SER F 53 1 6
HELIX 49 49 ARG F 77 GLY F 93 1 17
HELIX 50 50 ASP F 103 ARG F 116 1 14
HELIX 51 51 THR F 134 PHE F 138 5 5
HELIX 52 52 VAL F 143 GLU F 145 5 3
HELIX 53 53 GLU F 146 ARG F 161 1 16
HELIX 54 54 GLY F 164 LEU F 171 1 8
HELIX 55 55 ASN F 174 ARG F 179 1 6
HELIX 56 56 ARG F 179 GLY F 184 1 6
HELIX 57 57 GLY F 190 THR F 199 1 10
HELIX 58 58 PRO F 204 SER F 206 5 3
HELIX 59 59 ARG F 207 LEU F 217 1 11
HELIX 60 60 PRO F 223 SER F 240 1 18
HELIX 61 61 SER F 256 SER F 266 1 11
HELIX 62 62 TYR F 281 ARG F 305 1 25
SHEET 1 A 8 ARG A 11 VAL A 14 0
SHEET 2 A 8 SER A 17 THR A 24 -1 O MET A 19 N ALA A 12
SHEET 3 A 8 HIS A 57 PRO A 61 -1 O CYS A 58 N THR A 24
SHEET 4 A 8 VAL A 31 LEU A 35 1 N VAL A 32 O ILE A 59
SHEET 5 A 8 ALA A 97 GLN A 102 1 O VAL A 100 N LEU A 35
SHEET 6 A 8 VAL A 120 MET A 126 1 O ALA A 124 N LEU A 99
SHEET 7 A 8 LYS A 244 PRO A 251 1 O LEU A 245 N PHE A 125
SHEET 8 A 8 CYS A 270 GLY A 278 1 O ALA A 271 N LEU A 246
SHEET 1 B 8 ARG B 11 VAL B 14 0
SHEET 2 B 8 SER B 17 THR B 24 -1 O SER B 17 N VAL B 14
SHEET 3 B 8 HIS B 57 PRO B 61 -1 O CYS B 58 N THR B 24
SHEET 4 B 8 VAL B 31 LEU B 35 1 N VAL B 32 O ILE B 59
SHEET 5 B 8 ALA B 97 GLN B 102 1 O TYR B 98 N LEU B 33
SHEET 6 B 8 VAL B 120 MET B 126 1 O ALA B 124 N LEU B 99
SHEET 7 B 8 LYS B 244 PRO B 251 1 O LEU B 245 N PHE B 125
SHEET 8 B 8 CYS B 270 GLY B 278 1 O LEU B 275 N THR B 248
SHEET 1 C 8 ARG E 11 VAL E 14 0
SHEET 2 C 8 SER E 17 THR E 24 -1 O SER E 17 N VAL E 14
SHEET 3 C 8 HIS E 57 PRO E 61 -1 O ALA E 60 N ARG E 22
SHEET 4 C 8 VAL E 31 LEU E 35 1 N VAL E 32 O ILE E 59
SHEET 5 C 8 ALA E 97 GLN E 102 1 O VAL E 100 N LEU E 35
SHEET 6 C 8 VAL E 120 MET E 126 1 O ALA E 124 N LEU E 99
SHEET 7 C 8 LYS E 244 PRO E 251 1 O LEU E 245 N PHE E 125
SHEET 8 C 8 CYS E 270 GLY E 278 1 O ILE E 273 N LEU E 246
SHEET 1 D 8 ARG F 10 VAL F 14 0
SHEET 2 D 8 SER F 17 THR F 24 -1 O MET F 19 N ALA F 12
SHEET 3 D 8 HIS F 57 PRO F 61 -1 O ALA F 60 N ARG F 22
SHEET 4 D 8 VAL F 31 LEU F 35 1 N VAL F 32 O ILE F 59
SHEET 5 D 8 ALA F 97 GLN F 102 1 O TYR F 98 N LEU F 33
SHEET 6 D 8 VAL F 120 MET F 126 1 O ALA F 124 N LEU F 99
SHEET 7 D 8 LYS F 244 PRO F 251 1 O LEU F 245 N PHE F 125
SHEET 8 D 8 CYS F 270 GLY F 278 1 O ILE F 273 N LEU F 246
CISPEP 1 ASN A 38 PRO A 39 0 -6.07
CISPEP 2 GLU A 222 PRO A 223 0 -1.76
CISPEP 3 GLU A 250 PRO A 251 0 2.40
CISPEP 4 ASN B 38 PRO B 39 0 -3.85
CISPEP 5 GLU B 222 PRO B 223 0 -4.51
CISPEP 6 GLU B 250 PRO B 251 0 5.05
CISPEP 7 ASN E 38 PRO E 39 0 -2.99
CISPEP 8 GLU E 222 PRO E 223 0 -4.80
CISPEP 9 GLU E 250 PRO E 251 0 1.13
CISPEP 10 ASN F 38 PRO F 39 0 -7.31
CISPEP 11 GLU F 222 PRO F 223 0 -8.36
CISPEP 12 GLU F 250 PRO F 251 0 4.87
SITE 1 AC1 4 ASN A 38 TRP A 104 PRO A 214 HOH A 409
SITE 1 AC2 3 ASN B 38 TRP B 104 PRO B 214
SITE 1 AC3 4 ASN F 38 TRP F 104 PHE F 213 PRO F 214
CRYST1 125.534 47.766 99.410 90.00 93.61 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007966 0.000000 0.000503 0.00000
SCALE2 0.000000 0.020935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010079 0.00000
TER 2321 GLN A 307
TER 4652 GLN B 307
TER 6973 GLN E 307
TER 9312 GLN F 307
MASTER 719 0 3 62 32 0 3 6 9780 4 0 96
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