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HEADER HYDROLASE 08-APR-13 4K2A
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE DBEA FROM BRADYRHIZOBIUM
TITLE 2 ELKANI USDA94
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM ELKANII;
SOURCE 3 ORGANISM_TAXID: 29448;
SOURCE 4 STRAIN: USDA94;
SOURCE 5 GENE: DBEA, DHAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE, STRUCTURE 2 FUNCTION
KEYWDS 2 PROJECT, S2F, TWO DOMAIN ORGANIZATION, DIMER CATALYTIC PENTAD,
KEYWDS 3 HYDROLASE, HALOGEN BINDING,
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PRUDNIKOVA,R.CHALOUPKOVA,P.REZACOVA,T.MOZGA,T.KOUDELAKOVA,Y.SATO,
AUTHOR 2 M.KUTY,Y.NAGATA,J.DAMBORSKY,I.KUTA SMATANOVA,STRUCTURE 2 FUNCTION
AUTHOR 3 PROJECT (S2F)
REVDAT 1 25-JUN-14 4K2A 0
JRNL AUTH R.CHALOUPKOVA,T.PRUDNIKOVA,P.REZACOVA,Z.PROKOP,
JRNL AUTH 2 T.KOUDELAKOVA,L.DANIEL,J.BREZOVSKY,T.MOZGA,Y.SATO,M.KUTY,
JRNL AUTH 3 Y.NAGATA,I.KUTA SMATANOVA,J.DAMBORSKY
JRNL TITL ROLE OF THE SECOND HALIDE-BINDING SITE IN DETERMINING
JRNL TITL 2 ACTIVITY, SUBSTRATE SPECIFICITY AND STABILITY OF HALOALKANE
JRNL TITL 3 DEHALOGENASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 55927
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2945
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2690
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9048
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 749
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.269
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.561
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9499 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8987 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12964 ; 1.725 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20619 ; 0.888 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1228 ; 5.541 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 428 ;33.503 ;22.266
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1447 ;15.162 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 85 ;17.162 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1412 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10932 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2303 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4774 ; 0.827 ; 0.902
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4772 ; 0.820 ; 0.902
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5974 ; 1.372 ; 1.345
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5975 ; 1.305 ; 2.104
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4725 ; 1.189 ; 1.034
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4726 ; 1.176 ; 1.549
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6967 ; 1.893 ; 2.266
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11311 ; 5.004 ;12.185
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11083 ; 4.903 ;11.860
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 C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 297 5
REMARK 3 1 B 1 B 297 5
REMARK 3 1 C 1 C 297 5
REMARK 3 1 D 1 D 297 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1139 ; 0.15 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1139 ; 0.17 ; 0.00
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1139 ; 0.15 ; 0.00
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1139 ; 0.18 ; 0.00
REMARK 3 LOOSE POSITIONAL 1 A (A): 986 ; 0.43 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 A (A): 986 ; 0.46 ; 0.01
REMARK 3 LOOSE POSITIONAL 1 A (A): 986 ; 0.41 ; 0.00
REMARK 3 LOOSE POSITIONAL 1 A (A): 986 ; 0.44 ; 0.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1139 ; 0.58 ; 2.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1139 ; 0.60 ; 0.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1139 ; 0.58 ; 0.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1139 ; 0.55 ; 0.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 986 ; 0.77 ; 10.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 986 ; 0.80 ; 0.01
REMARK 3 LOOSE THERMAL 1 A (A**2): 986 ; 0.84 ; 0.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 986 ; 0.72 ; 0.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
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 6 A 10
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7946 -74.7529 44.4892
REMARK 3 T TENSOR
REMARK 3 T11: 0.1649 T22: 0.1241
REMARK 3 T33: 0.1686 T12: -0.0074
REMARK 3 T13: 0.0062 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 8.9349 L22: 2.0741
REMARK 3 L33: 3.9472 L12: 2.6003
REMARK 3 L13: 3.8529 L23: 0.8374
REMARK 3 S TENSOR
REMARK 3 S11: 0.1434 S12: 0.0475 S13: -0.2450
REMARK 3 S21: 0.2017 S22: -0.0072 S23: -0.0307
REMARK 3 S31: 0.2936 S32: -0.0719 S33: -0.1362
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 29
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9295 -69.9684 44.7072
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.1338
REMARK 3 T33: 0.2691 T12: 0.0269
REMARK 3 T13: 0.0037 T23: 0.0518
REMARK 3 L TENSOR
REMARK 3 L11: 1.4693 L22: 0.0267
REMARK 3 L33: 3.1119 L12: 0.0916
REMARK 3 L13: 2.1021 L23: 0.0910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: -0.0062 S13: -0.0324
REMARK 3 S21: -0.0113 S22: -0.0571 S23: -0.0274
REMARK 3 S31: 0.0267 S32: 0.0879 S33: 0.0736
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 30 A 117
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6192 -60.3976 43.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.1577 T22: 0.1027
REMARK 3 T33: 0.2047 T12: 0.0211
REMARK 3 T13: 0.0119 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.3316 L22: 0.2448
REMARK 3 L33: 0.7879 L12: 0.2268
REMARK 3 L13: 0.2846 L23: 0.0109
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: -0.0285 S13: -0.0732
REMARK 3 S21: 0.0018 S22: 0.0133 S23: -0.0210
REMARK 3 S31: -0.0148 S32: -0.0290 S33: -0.0466
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 118 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8340 -49.2012 36.9141
REMARK 3 T TENSOR
REMARK 3 T11: 0.1922 T22: 0.0671
REMARK 3 T33: 0.1993 T12: 0.0220
REMARK 3 T13: 0.0332 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.6113 L22: 0.1952
REMARK 3 L33: 2.0117 L12: 0.0857
REMARK 3 L13: 0.5071 L23: 0.6108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.1116 S13: -0.0245
REMARK 3 S21: -0.0395 S22: -0.0386 S23: 0.0182
REMARK 3 S31: -0.1047 S32: -0.0696 S33: 0.0420
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 135 A 169
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9087 -44.7407 55.5262
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.1763
REMARK 3 T33: 0.1552 T12: 0.0611
REMARK 3 T13: 0.0376 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 1.0783 L22: 1.6265
REMARK 3 L33: 2.1964 L12: 0.2965
REMARK 3 L13: 0.8314 L23: -0.9287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: -0.2781 S13: 0.1439
REMARK 3 S21: 0.0077 S22: 0.0143 S23: 0.1209
REMARK 3 S31: -0.1710 S32: -0.2211 S33: -0.0081
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 170 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6131 -59.5504 50.3718
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.2288
REMARK 3 T33: 0.1465 T12: 0.0110
REMARK 3 T13: 0.0462 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 4.3103 L22: 3.8065
REMARK 3 L33: 0.1035 L12: 0.7958
REMARK 3 L13: 0.5265 L23: -0.2650
REMARK 3 S TENSOR
REMARK 3 S11: 0.1212 S12: -0.5321 S13: 0.2052
REMARK 3 S21: -0.0645 S22: -0.1541 S23: 0.0786
REMARK 3 S31: 0.0240 S32: -0.0794 S33: 0.0328
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 186 A 231
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5923 -49.6157 50.9413
REMARK 3 T TENSOR
REMARK 3 T11: 0.1315 T22: 0.1528
REMARK 3 T33: 0.1532 T12: 0.0239
REMARK 3 T13: 0.0211 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.8613 L22: 0.6948
REMARK 3 L33: 0.4600 L12: 0.3142
REMARK 3 L13: -0.2393 L23: -0.2575
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: -0.1636 S13: 0.1049
REMARK 3 S21: 0.0009 S22: 0.0595 S23: -0.0066
REMARK 3 S31: -0.0725 S32: -0.0986 S33: -0.0365
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 232 A 253
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9316 -48.6342 32.8777
REMARK 3 T TENSOR
REMARK 3 T11: 0.1583 T22: 0.1196
REMARK 3 T33: 0.1804 T12: 0.0296
REMARK 3 T13: -0.0022 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 1.3867 L22: 0.6683
REMARK 3 L33: 0.3219 L12: 0.4924
REMARK 3 L13: -0.6577 L23: -0.1670
REMARK 3 S TENSOR
REMARK 3 S11: -0.0154 S12: 0.0350 S13: 0.1279
REMARK 3 S21: -0.1235 S22: 0.0763 S23: 0.0683
REMARK 3 S31: -0.0137 S32: -0.0182 S33: -0.0609
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 254 A 271
REMARK 3 ORIGIN FOR THE GROUP (A): 28.2852 -48.8585 29.8555
REMARK 3 T TENSOR
REMARK 3 T11: 0.1639 T22: 0.1257
REMARK 3 T33: 0.1564 T12: 0.0130
REMARK 3 T13: -0.0078 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 3.6698 L22: 0.9121
REMARK 3 L33: 1.1642 L12: 1.0379
REMARK 3 L13: -0.5580 L23: 0.6482
REMARK 3 S TENSOR
REMARK 3 S11: -0.1199 S12: 0.1846 S13: 0.2601
REMARK 3 S21: -0.1190 S22: 0.0903 S23: 0.1522
REMARK 3 S31: -0.0433 S32: 0.0047 S33: 0.0296
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 272 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8622 -62.3202 29.4414
REMARK 3 T TENSOR
REMARK 3 T11: 0.1513 T22: 0.1165
REMARK 3 T33: 0.1998 T12: -0.0008
REMARK 3 T13: 0.0143 T23: 0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.3449 L22: 0.0994
REMARK 3 L33: 2.0337 L12: -0.0968
REMARK 3 L13: 0.0504 L23: 0.3661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: -0.0196 S13: -0.1219
REMARK 3 S21: -0.0331 S22: 0.0271 S23: 0.0356
REMARK 3 S31: -0.1498 S32: 0.0830 S33: -0.0637
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 6 B 25
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4334 -19.0401 46.5749
REMARK 3 T TENSOR
REMARK 3 T11: 0.2028 T22: 0.0534
REMARK 3 T33: 0.1852 T12: 0.0357
REMARK 3 T13: 0.0055 T23: -0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 4.5212 L22: 1.1924
REMARK 3 L33: 6.3475 L12: 2.3192
REMARK 3 L13: -4.7133 L23: -2.3625
REMARK 3 S TENSOR
REMARK 3 S11: 0.0848 S12: -0.1813 S13: 0.0126
REMARK 3 S21: 0.0440 S22: -0.0956 S23: 0.0078
REMARK 3 S31: -0.3165 S32: 0.0495 S33: 0.0108
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 26 B 34
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5060 -20.4710 32.3470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1996 T22: 0.0194
REMARK 3 T33: 0.0703 T12: 0.0021
REMARK 3 T13: 0.0202 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 5.0774 L22: 6.5689
REMARK 3 L33: 8.2180 L12: -4.2436
REMARK 3 L13: 5.9578 L23: -3.0580
REMARK 3 S TENSOR
REMARK 3 S11: -0.4179 S12: 0.1445 S13: 0.1406
REMARK 3 S21: 0.2483 S22: 0.0514 S23: 0.2061
REMARK 3 S31: -0.5923 S32: 0.2727 S33: 0.3665
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 35 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9864 -28.7732 43.6116
REMARK 3 T TENSOR
REMARK 3 T11: 0.1648 T22: 0.0912
REMARK 3 T33: 0.2106 T12: 0.0206
REMARK 3 T13: 0.0058 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.3149 L22: 0.0325
REMARK 3 L33: 0.8167 L12: 0.0840
REMARK 3 L13: -0.0750 L23: -0.0606
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.0546 S13: 0.0345
REMARK 3 S21: -0.0143 S22: -0.0013 S23: 0.0331
REMARK 3 S31: -0.0091 S32: 0.0425 S33: 0.0164
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 115 B 138
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3154 -41.1294 38.2515
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.0866
REMARK 3 T33: 0.1887 T12: 0.0233
REMARK 3 T13: 0.0251 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.0614 L22: 0.7874
REMARK 3 L33: 0.7625 L12: -0.2691
REMARK 3 L13: 0.4063 L23: -0.7597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: 0.0727 S13: -0.0369
REMARK 3 S21: -0.0353 S22: 0.0524 S23: -0.0146
REMARK 3 S31: 0.0325 S32: -0.0128 S33: 0.0138
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 139 B 152
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5672 -47.0014 51.7571
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.1566
REMARK 3 T33: 0.1741 T12: 0.0799
REMARK 3 T13: 0.0021 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 1.8055 L22: 2.0486
REMARK 3 L33: 2.1308 L12: -0.5253
REMARK 3 L13: -0.0406 L23: 2.0210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0781 S12: -0.0973 S13: -0.0050
REMARK 3 S21: 0.0464 S22: 0.1930 S23: -0.2462
REMARK 3 S31: 0.0673 S32: 0.1763 S33: -0.2711
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 153 B 166
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3220 -40.2371 62.8244
REMARK 3 T TENSOR
REMARK 3 T11: 0.1333 T22: 0.2149
REMARK 3 T33: 0.2510 T12: 0.0913
REMARK 3 T13: -0.0696 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 1.1372 L22: 5.5166
REMARK 3 L33: 0.6865 L12: -0.7025
REMARK 3 L13: 0.3564 L23: -1.8188
REMARK 3 S TENSOR
REMARK 3 S11: -0.2513 S12: -0.2633 S13: -0.1387
REMARK 3 S21: 0.1683 S22: 0.3581 S23: -0.1361
REMARK 3 S31: -0.0223 S32: -0.0903 S33: -0.1068
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 167 B 177
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1455 -34.0209 51.1936
REMARK 3 T TENSOR
REMARK 3 T11: 0.1220 T22: 0.1650
REMARK 3 T33: 0.1626 T12: 0.0422
REMARK 3 T13: -0.0114 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 3.5881 L22: 2.3159
REMARK 3 L33: 6.1154 L12: 2.7412
REMARK 3 L13: -4.2338 L23: -2.7458
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: -0.0484 S13: -0.0479
REMARK 3 S21: -0.0240 S22: -0.0670 S23: -0.0242
REMARK 3 S31: 0.2005 S32: 0.0415 S33: 0.1414
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 178 B 210
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7883 -31.9470 54.9980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1445 T22: 0.1886
REMARK 3 T33: 0.1225 T12: 0.0005
REMARK 3 T13: 0.0106 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 0.9352 L22: 0.3171
REMARK 3 L33: 0.1865 L12: -0.4689
REMARK 3 L13: 0.0313 L23: 0.0750
REMARK 3 S TENSOR
REMARK 3 S11: -0.0562 S12: -0.2196 S13: 0.0285
REMARK 3 S21: 0.0393 S22: 0.0830 S23: 0.0135
REMARK 3 S31: 0.0088 S32: 0.0638 S33: -0.0268
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 211 B 289
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4746 -38.9830 34.0210
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.1004
REMARK 3 T33: 0.1822 T12: 0.0194
REMARK 3 T13: 0.0108 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.8007 L22: 0.5100
REMARK 3 L33: 0.5020 L12: 0.3579
REMARK 3 L13: -0.0691 L23: -0.2379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0499 S12: 0.0178 S13: -0.0751
REMARK 3 S21: -0.0688 S22: 0.0355 S23: -0.0483
REMARK 3 S31: 0.0597 S32: 0.0601 S33: 0.0143
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 290 B 296
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0878 -26.2143 20.5718
REMARK 3 T TENSOR
REMARK 3 T11: 0.1682 T22: 0.1822
REMARK 3 T33: 0.2127 T12: 0.0190
REMARK 3 T13: 0.0282 T23: 0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 1.2168 L22: 0.4013
REMARK 3 L33: 11.1332 L12: -0.1977
REMARK 3 L13: -1.5341 L23: 2.0876
REMARK 3 S TENSOR
REMARK 3 S11: 0.1727 S12: 0.3243 S13: 0.1261
REMARK 3 S21: 0.0304 S22: -0.0269 S23: -0.0001
REMARK 3 S31: 0.0403 S32: -0.2719 S33: -0.1458
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 : C 6 C 10
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5195 -36.6930 11.3938
REMARK 3 T TENSOR
REMARK 3 T11: 0.1609 T22: 0.1398
REMARK 3 T33: 0.1676 T12: 0.0187
REMARK 3 T13: 0.0119 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.0768 L22: 1.6048
REMARK 3 L33: 11.1047 L12: 1.2041
REMARK 3 L13: 1.7347 L23: 0.4788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0626 S12: -0.0659 S13: -0.0511
REMARK 3 S21: 0.0445 S22: -0.1249 S23: -0.0729
REMARK 3 S31: 0.2263 S32: 0.1214 S33: 0.0623
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 : C 11 C 26
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4061 -34.5589 2.9439
REMARK 3 T TENSOR
REMARK 3 T11: 0.1817 T22: 0.1301
REMARK 3 T33: 0.1915 T12: 0.0063
REMARK 3 T13: 0.0434 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 1.1972 L22: 0.1447
REMARK 3 L33: 4.2227 L12: 0.2427
REMARK 3 L13: -1.2680 L23: 0.2611
REMARK 3 S TENSOR
REMARK 3 S11: -0.1592 S12: 0.0981 S13: -0.2930
REMARK 3 S21: -0.0118 S22: 0.0095 S23: -0.0942
REMARK 3 S31: 0.2736 S32: -0.0497 S33: 0.1497
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 27 C 120
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0172 -26.2370 5.2299
REMARK 3 T TENSOR
REMARK 3 T11: 0.1673 T22: 0.1203
REMARK 3 T33: 0.1727 T12: -0.0118
REMARK 3 T13: 0.0044 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 0.9249 L22: 0.2486
REMARK 3 L33: 0.3587 L12: 0.2412
REMARK 3 L13: -0.2863 L23: -0.1297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0379 S12: 0.1371 S13: -0.0653
REMARK 3 S21: 0.0020 S22: 0.0105 S23: -0.0167
REMARK 3 S31: 0.0528 S32: -0.0051 S33: 0.0275
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 121 C 146
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5834 -7.7153 9.6770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1658 T22: 0.1149
REMARK 3 T33: 0.1605 T12: 0.0036
REMARK 3 T13: 0.0110 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.2647 L22: 1.8522
REMARK 3 L33: 0.7466 L12: 1.5229
REMARK 3 L13: -0.0187 L23: 0.0825
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: 0.0091 S13: 0.0321
REMARK 3 S21: 0.0280 S22: -0.0034 S23: 0.0583
REMARK 3 S31: -0.0977 S32: -0.0472 S33: -0.0249
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 147 C 167
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4405 -5.3010 2.0042
REMARK 3 T TENSOR
REMARK 3 T11: 0.1576 T22: 0.1399
REMARK 3 T33: 0.1549 T12: -0.0378
REMARK 3 T13: 0.0077 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.4232 L22: 2.8134
REMARK 3 L33: 1.2689 L12: -1.8263
REMARK 3 L13: -0.2413 L23: -1.1546
REMARK 3 S TENSOR
REMARK 3 S11: 0.0781 S12: 0.0593 S13: 0.0657
REMARK 3 S21: 0.0479 S22: -0.0971 S23: -0.0859
REMARK 3 S31: -0.1053 S32: 0.0566 S33: 0.0190
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 168 C 183
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3113 -14.7340 16.8696
REMARK 3 T TENSOR
REMARK 3 T11: 0.1336 T22: 0.1272
REMARK 3 T33: 0.1720 T12: -0.0379
REMARK 3 T13: -0.0066 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 1.2958 L22: 1.9528
REMARK 3 L33: 2.0810 L12: -0.4571
REMARK 3 L13: -0.2921 L23: -0.1794
REMARK 3 S TENSOR
REMARK 3 S11: 0.1325 S12: -0.1872 S13: 0.1311
REMARK 3 S21: -0.0957 S22: 0.0563 S23: 0.0530
REMARK 3 S31: -0.1406 S32: 0.2807 S33: -0.1889
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 184 C 219
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5002 -13.5073 1.4587
REMARK 3 T TENSOR
REMARK 3 T11: 0.1507 T22: 0.1410
REMARK 3 T33: 0.1447 T12: -0.0257
REMARK 3 T13: 0.0077 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 1.3476 L22: 0.6402
REMARK 3 L33: 0.3702 L12: -0.2922
REMARK 3 L13: -0.1195 L23: -0.0160
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.1971 S13: 0.0573
REMARK 3 S21: -0.0755 S22: 0.0525 S23: -0.1201
REMARK 3 S31: -0.0192 S32: 0.0243 S33: 0.0091
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 220 C 252
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5376 -13.9017 11.9151
REMARK 3 T TENSOR
REMARK 3 T11: 0.1638 T22: 0.1362
REMARK 3 T33: 0.1613 T12: 0.0048
REMARK 3 T13: -0.0298 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.3406 L22: 0.0076
REMARK 3 L33: 0.7043 L12: -0.0150
REMARK 3 L13: -0.2287 L23: -0.0584
REMARK 3 S TENSOR
REMARK 3 S11: -0.0258 S12: 0.0629 S13: 0.0939
REMARK 3 S21: 0.0213 S22: 0.0224 S23: 0.0033
REMARK 3 S31: -0.0906 S32: -0.1942 S33: 0.0034
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 253 C 271
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2544 -13.8285 17.6123
REMARK 3 T TENSOR
REMARK 3 T11: 0.1383 T22: 0.1233
REMARK 3 T33: 0.1456 T12: 0.0064
REMARK 3 T13: 0.0074 T23: -0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 3.8031 L22: 0.9977
REMARK 3 L33: 1.6442 L12: 1.1850
REMARK 3 L13: 1.7097 L23: 0.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: -0.0730 S13: -0.0173
REMARK 3 S21: 0.0526 S22: 0.0847 S23: 0.0241
REMARK 3 S31: -0.0730 S32: -0.1423 S33: -0.0005
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 272 C 304
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1712 -28.3971 19.1332
REMARK 3 T TENSOR
REMARK 3 T11: 0.1885 T22: 0.1461
REMARK 3 T33: 0.1730 T12: -0.0362
REMARK 3 T13: 0.0019 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.9868 L22: 0.1845
REMARK 3 L33: 0.4411 L12: 0.4048
REMARK 3 L13: -0.6559 L23: -0.2701
REMARK 3 S TENSOR
REMARK 3 S11: -0.1482 S12: 0.1210 S13: -0.0580
REMARK 3 S21: -0.0761 S22: 0.0866 S23: -0.0635
REMARK 3 S31: 0.0800 S32: -0.0711 S33: 0.0616
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 6 D 12
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3867 -51.2598 9.8810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1621 T22: 0.1378
REMARK 3 T33: 0.1741 T12: 0.0167
REMARK 3 T13: -0.0098 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 2.0705 L22: 0.6597
REMARK 3 L33: 7.7580 L12: 0.9509
REMARK 3 L13: 1.8004 L23: 1.9087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0458 S12: -0.0581 S13: 0.1262
REMARK 3 S21: 0.0136 S22: -0.0552 S23: 0.1081
REMARK 3 S31: -0.1081 S32: -0.1714 S33: 0.0094
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 13 D 34
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8581 -54.0263 7.8169
REMARK 3 T TENSOR
REMARK 3 T11: 0.1863 T22: 0.2315
REMARK 3 T33: 0.1446 T12: 0.0065
REMARK 3 T13: 0.0029 T23: 0.0781
REMARK 3 L TENSOR
REMARK 3 L11: 1.1122 L22: 0.0542
REMARK 3 L33: 1.4536 L12: -0.0118
REMARK 3 L13: 1.2666 L23: -0.0305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0729 S12: 0.2370 S13: 0.1691
REMARK 3 S21: 0.0116 S22: -0.0919 S23: 0.0161
REMARK 3 S31: -0.1064 S32: 0.2815 S33: 0.1647
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 35 D 103
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9753 -61.8797 6.6975
REMARK 3 T TENSOR
REMARK 3 T11: 0.1357 T22: 0.1593
REMARK 3 T33: 0.1441 T12: 0.0211
REMARK 3 T13: -0.0086 T23: 0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 1.0552 L22: 0.2823
REMARK 3 L33: 1.1318 L12: 0.1148
REMARK 3 L13: 0.6980 L23: 0.2688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: 0.1021 S13: 0.0433
REMARK 3 S21: 0.0074 S22: -0.0570 S23: 0.0297
REMARK 3 S31: -0.0168 S32: 0.0425 S33: 0.0249
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 104 D 129
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9743 -67.4915 5.8904
REMARK 3 T TENSOR
REMARK 3 T11: 0.1216 T22: 0.2314
REMARK 3 T33: 0.1565 T12: 0.0048
REMARK 3 T13: 0.0048 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.7728 L22: 1.1792
REMARK 3 L33: 2.1776 L12: 1.3214
REMARK 3 L13: -0.6789 L23: -1.0728
REMARK 3 S TENSOR
REMARK 3 S11: 0.0774 S12: 0.1700 S13: 0.0556
REMARK 3 S21: 0.0624 S22: -0.0080 S23: 0.1031
REMARK 3 S31: -0.0287 S32: 0.2418 S33: -0.0694
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 130 D 146
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4501 -87.0058 8.7283
REMARK 3 T TENSOR
REMARK 3 T11: 0.2230 T22: 0.1395
REMARK 3 T33: 0.1671 T12: -0.0454
REMARK 3 T13: -0.0755 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 1.6035 L22: 1.4504
REMARK 3 L33: 4.2959 L12: 1.4496
REMARK 3 L13: -2.5814 L23: -2.3737
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: -0.1640 S13: -0.0881
REMARK 3 S21: -0.0602 S22: -0.0727 S23: -0.1114
REMARK 3 S31: 0.0837 S32: 0.1993 S33: 0.0302
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 147 D 169
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6127 -81.2445 3.6355
REMARK 3 T TENSOR
REMARK 3 T11: 0.1493 T22: 0.1434
REMARK 3 T33: 0.1381 T12: -0.0691
REMARK 3 T13: -0.0845 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 1.9909 L22: 2.0056
REMARK 3 L33: 2.8626 L12: -0.6300
REMARK 3 L13: -0.8409 L23: 0.8675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0723 S12: 0.0029 S13: -0.1424
REMARK 3 S21: -0.0001 S22: -0.0526 S23: 0.1307
REMARK 3 S31: 0.2692 S32: -0.2375 S33: -0.0197
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 170 D 184
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6020 -72.7389 19.2753
REMARK 3 T TENSOR
REMARK 3 T11: 0.1371 T22: 0.2170
REMARK 3 T33: 0.1758 T12: -0.0120
REMARK 3 T13: 0.0267 T23: 0.0803
REMARK 3 L TENSOR
REMARK 3 L11: 0.2386 L22: 1.3769
REMARK 3 L33: 4.5708 L12: 0.0456
REMARK 3 L13: -0.0399 L23: -0.5154
REMARK 3 S TENSOR
REMARK 3 S11: -0.0800 S12: -0.1314 S13: -0.1604
REMARK 3 S21: 0.1171 S22: 0.2274 S23: 0.0151
REMARK 3 S31: 0.2609 S32: -0.4036 S33: -0.1474
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 185 D 239
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2145 -73.4832 4.4317
REMARK 3 T TENSOR
REMARK 3 T11: 0.1238 T22: 0.1726
REMARK 3 T33: 0.1070 T12: 0.0067
REMARK 3 T13: -0.0121 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.5547 L22: 0.5732
REMARK 3 L33: 0.7322 L12: -0.1437
REMARK 3 L13: 0.3303 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: 0.0852 S13: -0.0900
REMARK 3 S21: -0.0420 S22: -0.0136 S23: 0.0641
REMARK 3 S31: 0.1100 S32: 0.0491 S33: -0.0767
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 240 D 271
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8297 -77.7066 17.6646
REMARK 3 T TENSOR
REMARK 3 T11: 0.1449 T22: 0.1323
REMARK 3 T33: 0.1434 T12: 0.0358
REMARK 3 T13: 0.0017 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 3.2129 L22: 0.4859
REMARK 3 L33: 2.2686 L12: 0.9498
REMARK 3 L13: -1.2004 L23: -0.2537
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.0223 S13: -0.0795
REMARK 3 S21: 0.0120 S22: 0.0924 S23: 0.0078
REMARK 3 S31: 0.2681 S32: 0.1296 S33: -0.0717
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 272 D 297
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0690 -63.4985 20.9922
REMARK 3 T TENSOR
REMARK 3 T11: 0.1450 T22: 0.1559
REMARK 3 T33: 0.1846 T12: -0.0210
REMARK 3 T13: 0.0017 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.6680 L22: 0.1850
REMARK 3 L33: 0.7648 L12: 0.2876
REMARK 3 L13: 0.6237 L23: 0.1674
REMARK 3 S TENSOR
REMARK 3 S11: -0.0468 S12: 0.1489 S13: 0.0411
REMARK 3 S21: 0.0064 S22: 0.0980 S23: 0.0616
REMARK 3 S31: -0.0436 S32: 0.0456 S33: -0.0511
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 4K2A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : KMC-1
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73280
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.6400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.30700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS HCL, 20% (W/V) PEG 3350 OR
REMARK 280 4000 AND 150 MM CALCIUM ACETATE , PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.35100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.99600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.94400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.99600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.35100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.94400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 ALA A 5
REMARK 465 ALA A 302
REMARK 465 LEU A 303
REMARK 465 GLU A 304
REMARK 465 ALA B 5
REMARK 465 ALA B 297
REMARK 465 GLN B 298
REMARK 465 ARG B 299
REMARK 465 HIS B 300
REMARK 465 ALA B 301
REMARK 465 ALA B 302
REMARK 465 LEU B 303
REMARK 465 GLU B 304
REMARK 465 ALA C 5
REMARK 465 ALA D 5
REMARK 465 GLN D 298
REMARK 465 ARG D 299
REMARK 465 HIS D 300
REMARK 465 ALA D 301
REMARK 465 ALA D 302
REMARK 465 LEU D 303
REMARK 465 GLU D 304
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 GLN A 298 CG CD OE1 NE2
REMARK 470 ARG A 299 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 300 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 736 O HOH D 601 3555 1.85
REMARK 500 O HOH C 740 O HOH C 790 4545 2.02
REMARK 500
REMARK 500 REMARK: NULL
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 GLY C 155 C GLY C 155 O 0.099
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 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 28 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 86 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 86 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP C 86 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP C 86 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP C 216 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG D 22 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 VAL D 239 CB - CA - C ANGL. DEV. = -11.6 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 LEU A 15 -126.29 48.43
REMARK 500 SER A 17 -153.58 -156.73
REMARK 500 PRO A 39 52.89 -112.56
REMARK 500 THR A 40 -155.68 -99.51
REMARK 500 ASP A 103 -130.45 58.53
REMARK 500 HIS A 139 -170.60 68.28
REMARK 500 ARG A 170 -53.41 -122.71
REMARK 500 ALA A 244 -68.68 -133.88
REMARK 500 ARG A 299 -74.16 72.74
REMARK 500 LEU B 15 -127.28 47.41
REMARK 500 SER B 17 -149.57 -165.31
REMARK 500 PRO B 39 52.00 -107.59
REMARK 500 THR B 40 -153.20 -101.93
REMARK 500 ASP B 103 -133.41 58.64
REMARK 500 HIS B 139 -170.82 68.26
REMARK 500 ARG B 170 -57.98 -123.47
REMARK 500 ALA B 244 -71.73 -144.23
REMARK 500 SER C 17 -152.94 -116.67
REMARK 500 PRO C 39 52.44 -111.25
REMARK 500 THR C 40 -151.42 -103.09
REMARK 500 ASP C 103 -130.76 57.61
REMARK 500 HIS C 139 -159.47 61.14
REMARK 500 ARG C 170 -51.80 -123.65
REMARK 500 ALA C 244 -77.88 -139.46
REMARK 500 SER D 17 -151.56 -124.73
REMARK 500 PRO D 39 47.53 -104.31
REMARK 500 THR D 40 -155.71 -100.53
REMARK 500 ASP D 103 -128.54 63.30
REMARK 500 HIS D 139 -163.52 62.53
REMARK 500 ARG D 170 -54.92 -120.93
REMARK 500 ALA D 244 -75.99 -135.73
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A2M RELATED DB: PDB
REMARK 900 DBJA FROM BRADYRHIZOBIUM JAPONICUM - USED AS MR MODEL
REMARK 900 RELATED ID: 2BN6 RELATED DB: PDB
REMARK 900 DHAA FROM RHODOCOCCUS SP
REMARK 900 RELATED ID: 1CIJ RELATED DB: PDB
REMARK 900 DHLA FROM XANTHOBACTER AUTOTROPHICUS
REMARK 900 RELATED ID: 2QVB RELATED DB: PDB
REMARK 900 DMBA FROM MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: 1CV2 RELATED DB: PDB
REMARK 900 LINB FROM SPHINGOMONAS PAUCIMOBILIS
DBREF 4K2A A 5 302 UNP E2RV62 E2RV62_BRAEL 5 302
DBREF 4K2A B 5 302 UNP E2RV62 E2RV62_BRAEL 5 302
DBREF 4K2A C 5 302 UNP E2RV62 E2RV62_BRAEL 5 302
DBREF 4K2A D 5 302 UNP E2RV62 E2RV62_BRAEL 5 302
SEQADV 4K2A LEU A 303 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A GLU A 304 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A LEU B 303 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A GLU B 304 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A LEU C 303 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A GLU C 304 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A LEU D 303 UNP E2RV62 EXPRESSION TAG
SEQADV 4K2A GLU D 304 UNP E2RV62 EXPRESSION TAG
SEQRES 1 A 300 ALA ASP ILE SER LEU HIS HIS ARG ALA VAL LEU GLY SER
SEQRES 2 A 300 THR MET ALA TYR ARG GLU THR GLY ARG SER ASP ALA PRO
SEQRES 3 A 300 HIS VAL LEU PHE LEU HIS GLY ASN PRO THR SER SER TYR
SEQRES 4 A 300 ILE TRP ARG ASN ILE MET PRO LEU VAL ALA PRO VAL GLY
SEQRES 5 A 300 HIS CYS ILE ALA PRO ASP LEU ILE GLY TYR GLY GLN SER
SEQRES 6 A 300 GLY LYS PRO ASP ILE SER TYR ARG PHE PHE ASP GLN ALA
SEQRES 7 A 300 ASP TYR LEU ASP ALA LEU ILE ASP GLU LEU GLY ILE ALA
SEQRES 8 A 300 SER ALA TYR LEU VAL ALA GLN ASP TRP GLY THR ALA LEU
SEQRES 9 A 300 ALA PHE HIS LEU ALA ALA ARG ARG PRO GLN LEU VAL ARG
SEQRES 10 A 300 GLY LEU ALA PHE MET GLU PHE ILE ARG PRO MET ARG ASP
SEQRES 11 A 300 TRP SER ASP PHE HIS GLN HIS ASP ALA ALA ARG GLU THR
SEQRES 12 A 300 PHE ARG LYS PHE ARG THR PRO GLY VAL GLY GLU ALA MET
SEQRES 13 A 300 ILE LEU ASP ASN ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 14 A 300 GLY SER ILE LEU ARG THR LEU SER GLU GLU GLU MET ALA
SEQRES 15 A 300 ALA TYR ARG ALA PRO PHE ALA THR ARG GLU SER ARG MET
SEQRES 16 A 300 PRO THR LEU MET LEU PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 17 A 300 GLU PRO ALA ASP VAL THR GLN ALA LEU THR ALA ALA HIS
SEQRES 18 A 300 ALA ALA LEU ALA ALA SER THR TYR PRO LYS LEU LEU PHE
SEQRES 19 A 300 VAL GLY SER PRO GLY ALA LEU VAL SER PRO ALA PHE ALA
SEQRES 20 A 300 ALA GLU PHE ALA LYS THR LEU LYS HIS CYS ALA VAL ILE
SEQRES 21 A 300 GLN LEU GLY ALA GLY GLY HIS TYR LEU GLN GLU ASP HIS
SEQRES 22 A 300 PRO GLU ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 23 A 300 GLY ILE GLU ALA ALA SER ALA GLN ARG HIS ALA ALA LEU
SEQRES 24 A 300 GLU
SEQRES 1 B 300 ALA ASP ILE SER LEU HIS HIS ARG ALA VAL LEU GLY SER
SEQRES 2 B 300 THR MET ALA TYR ARG GLU THR GLY ARG SER ASP ALA PRO
SEQRES 3 B 300 HIS VAL LEU PHE LEU HIS GLY ASN PRO THR SER SER TYR
SEQRES 4 B 300 ILE TRP ARG ASN ILE MET PRO LEU VAL ALA PRO VAL GLY
SEQRES 5 B 300 HIS CYS ILE ALA PRO ASP LEU ILE GLY TYR GLY GLN SER
SEQRES 6 B 300 GLY LYS PRO ASP ILE SER TYR ARG PHE PHE ASP GLN ALA
SEQRES 7 B 300 ASP TYR LEU ASP ALA LEU ILE ASP GLU LEU GLY ILE ALA
SEQRES 8 B 300 SER ALA TYR LEU VAL ALA GLN ASP TRP GLY THR ALA LEU
SEQRES 9 B 300 ALA PHE HIS LEU ALA ALA ARG ARG PRO GLN LEU VAL ARG
SEQRES 10 B 300 GLY LEU ALA PHE MET GLU PHE ILE ARG PRO MET ARG ASP
SEQRES 11 B 300 TRP SER ASP PHE HIS GLN HIS ASP ALA ALA ARG GLU THR
SEQRES 12 B 300 PHE ARG LYS PHE ARG THR PRO GLY VAL GLY GLU ALA MET
SEQRES 13 B 300 ILE LEU ASP ASN ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 14 B 300 GLY SER ILE LEU ARG THR LEU SER GLU GLU GLU MET ALA
SEQRES 15 B 300 ALA TYR ARG ALA PRO PHE ALA THR ARG GLU SER ARG MET
SEQRES 16 B 300 PRO THR LEU MET LEU PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 17 B 300 GLU PRO ALA ASP VAL THR GLN ALA LEU THR ALA ALA HIS
SEQRES 18 B 300 ALA ALA LEU ALA ALA SER THR TYR PRO LYS LEU LEU PHE
SEQRES 19 B 300 VAL GLY SER PRO GLY ALA LEU VAL SER PRO ALA PHE ALA
SEQRES 20 B 300 ALA GLU PHE ALA LYS THR LEU LYS HIS CYS ALA VAL ILE
SEQRES 21 B 300 GLN LEU GLY ALA GLY GLY HIS TYR LEU GLN GLU ASP HIS
SEQRES 22 B 300 PRO GLU ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 23 B 300 GLY ILE GLU ALA ALA SER ALA GLN ARG HIS ALA ALA LEU
SEQRES 24 B 300 GLU
SEQRES 1 C 300 ALA ASP ILE SER LEU HIS HIS ARG ALA VAL LEU GLY SER
SEQRES 2 C 300 THR MET ALA TYR ARG GLU THR GLY ARG SER ASP ALA PRO
SEQRES 3 C 300 HIS VAL LEU PHE LEU HIS GLY ASN PRO THR SER SER TYR
SEQRES 4 C 300 ILE TRP ARG ASN ILE MET PRO LEU VAL ALA PRO VAL GLY
SEQRES 5 C 300 HIS CYS ILE ALA PRO ASP LEU ILE GLY TYR GLY GLN SER
SEQRES 6 C 300 GLY LYS PRO ASP ILE SER TYR ARG PHE PHE ASP GLN ALA
SEQRES 7 C 300 ASP TYR LEU ASP ALA LEU ILE ASP GLU LEU GLY ILE ALA
SEQRES 8 C 300 SER ALA TYR LEU VAL ALA GLN ASP TRP GLY THR ALA LEU
SEQRES 9 C 300 ALA PHE HIS LEU ALA ALA ARG ARG PRO GLN LEU VAL ARG
SEQRES 10 C 300 GLY LEU ALA PHE MET GLU PHE ILE ARG PRO MET ARG ASP
SEQRES 11 C 300 TRP SER ASP PHE HIS GLN HIS ASP ALA ALA ARG GLU THR
SEQRES 12 C 300 PHE ARG LYS PHE ARG THR PRO GLY VAL GLY GLU ALA MET
SEQRES 13 C 300 ILE LEU ASP ASN ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 14 C 300 GLY SER ILE LEU ARG THR LEU SER GLU GLU GLU MET ALA
SEQRES 15 C 300 ALA TYR ARG ALA PRO PHE ALA THR ARG GLU SER ARG MET
SEQRES 16 C 300 PRO THR LEU MET LEU PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 17 C 300 GLU PRO ALA ASP VAL THR GLN ALA LEU THR ALA ALA HIS
SEQRES 18 C 300 ALA ALA LEU ALA ALA SER THR TYR PRO LYS LEU LEU PHE
SEQRES 19 C 300 VAL GLY SER PRO GLY ALA LEU VAL SER PRO ALA PHE ALA
SEQRES 20 C 300 ALA GLU PHE ALA LYS THR LEU LYS HIS CYS ALA VAL ILE
SEQRES 21 C 300 GLN LEU GLY ALA GLY GLY HIS TYR LEU GLN GLU ASP HIS
SEQRES 22 C 300 PRO GLU ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 23 C 300 GLY ILE GLU ALA ALA SER ALA GLN ARG HIS ALA ALA LEU
SEQRES 24 C 300 GLU
SEQRES 1 D 300 ALA ASP ILE SER LEU HIS HIS ARG ALA VAL LEU GLY SER
SEQRES 2 D 300 THR MET ALA TYR ARG GLU THR GLY ARG SER ASP ALA PRO
SEQRES 3 D 300 HIS VAL LEU PHE LEU HIS GLY ASN PRO THR SER SER TYR
SEQRES 4 D 300 ILE TRP ARG ASN ILE MET PRO LEU VAL ALA PRO VAL GLY
SEQRES 5 D 300 HIS CYS ILE ALA PRO ASP LEU ILE GLY TYR GLY GLN SER
SEQRES 6 D 300 GLY LYS PRO ASP ILE SER TYR ARG PHE PHE ASP GLN ALA
SEQRES 7 D 300 ASP TYR LEU ASP ALA LEU ILE ASP GLU LEU GLY ILE ALA
SEQRES 8 D 300 SER ALA TYR LEU VAL ALA GLN ASP TRP GLY THR ALA LEU
SEQRES 9 D 300 ALA PHE HIS LEU ALA ALA ARG ARG PRO GLN LEU VAL ARG
SEQRES 10 D 300 GLY LEU ALA PHE MET GLU PHE ILE ARG PRO MET ARG ASP
SEQRES 11 D 300 TRP SER ASP PHE HIS GLN HIS ASP ALA ALA ARG GLU THR
SEQRES 12 D 300 PHE ARG LYS PHE ARG THR PRO GLY VAL GLY GLU ALA MET
SEQRES 13 D 300 ILE LEU ASP ASN ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 14 D 300 GLY SER ILE LEU ARG THR LEU SER GLU GLU GLU MET ALA
SEQRES 15 D 300 ALA TYR ARG ALA PRO PHE ALA THR ARG GLU SER ARG MET
SEQRES 16 D 300 PRO THR LEU MET LEU PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 17 D 300 GLU PRO ALA ASP VAL THR GLN ALA LEU THR ALA ALA HIS
SEQRES 18 D 300 ALA ALA LEU ALA ALA SER THR TYR PRO LYS LEU LEU PHE
SEQRES 19 D 300 VAL GLY SER PRO GLY ALA LEU VAL SER PRO ALA PHE ALA
SEQRES 20 D 300 ALA GLU PHE ALA LYS THR LEU LYS HIS CYS ALA VAL ILE
SEQRES 21 D 300 GLN LEU GLY ALA GLY GLY HIS TYR LEU GLN GLU ASP HIS
SEQRES 22 D 300 PRO GLU ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 23 D 300 GLY ILE GLU ALA ALA SER ALA GLN ARG HIS ALA ALA LEU
SEQRES 24 D 300 GLU
HET CL A 501 1
HET CL A 502 1
HET CL B 501 1
HET CL B 502 1
HET ACT B 503 4
HET CL C 501 1
HET CL C 502 1
HET ACT C 503 4
HET ACT C 504 4
HET CL D 501 1
HET CL D 502 1
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 5 CL 8(CL 1-)
FORMUL 9 ACT 3(C2 H3 O2 1-)
FORMUL 16 HOH *749(H2 O)
HELIX 1 37 SER A 41 ARG A 46 5 6
HELIX 2 38 ILE A 48 ALA A 53 1 6
HELIX 3 39 ARG A 77 LEU A 92 1 16
HELIX 4 40 ASP A 103 ARG A 116 1 14
HELIX 5 41 ASP A 134 PHE A 138 5 5
HELIX 6 42 HIS A 141 ARG A 152 1 12
HELIX 7 43 GLY A 155 LEU A 162 1 8
HELIX 8 44 ASN A 165 ARG A 170 1 6
HELIX 9 45 ARG A 170 SER A 175 1 6
HELIX 10 46 SER A 181 ALA A 190 1 10
HELIX 11 47 PRO A 191 ALA A 193 5 3
HELIX 12 48 ARG A 195 SER A 197 5 3
HELIX 13 49 ARG A 198 LEU A 208 1 11
HELIX 14 50 PRO A 214 SER A 231 1 18
HELIX 15 51 SER A 247 LYS A 256 1 10
HELIX 16 52 TYR A 272 ASP A 276 5 5
HELIX 17 53 HIS A 277 GLN A 298 1 22
HELIX 18 54 SER B 41 ARG B 46 5 6
HELIX 19 55 ILE B 48 ALA B 53 1 6
HELIX 20 56 ARG B 77 LEU B 92 1 16
HELIX 21 57 ASP B 103 ARG B 116 1 14
HELIX 22 58 ASP B 134 PHE B 138 5 5
HELIX 23 59 HIS B 141 ARG B 152 1 12
HELIX 24 60 GLY B 155 LEU B 162 1 8
HELIX 25 61 ASN B 165 ARG B 170 1 6
HELIX 26 62 ARG B 170 SER B 175 1 6
HELIX 27 63 SER B 181 ALA B 190 1 10
HELIX 28 64 PRO B 191 ALA B 193 5 3
HELIX 29 65 ARG B 195 SER B 197 5 3
HELIX 30 66 ARG B 198 LEU B 208 1 11
HELIX 31 67 PRO B 214 SER B 231 1 18
HELIX 32 68 SER B 247 THR B 257 1 11
HELIX 33 69 TYR B 272 ASP B 276 5 5
HELIX 34 70 HIS B 277 SER B 296 1 20
HELIX 35 1 SER C 41 ARG C 46 5 6
HELIX 36 2 ILE C 48 ALA C 53 1 6
HELIX 37 3 PRO C 54 GLY C 56 5 3
HELIX 38 4 ARG C 77 LEU C 92 1 16
HELIX 39 5 ASP C 103 ARG C 116 1 14
HELIX 40 6 ASP C 134 PHE C 138 5 5
HELIX 41 7 HIS C 141 ARG C 152 1 12
HELIX 42 8 GLY C 155 LEU C 162 1 8
HELIX 43 9 ASN C 165 ARG C 170 1 6
HELIX 44 10 ARG C 170 SER C 175 1 6
HELIX 45 11 SER C 181 ALA C 190 1 10
HELIX 46 12 PRO C 191 ALA C 193 5 3
HELIX 47 13 ARG C 195 SER C 197 5 3
HELIX 48 14 ARG C 198 LEU C 208 1 11
HELIX 49 15 PRO C 214 SER C 231 1 18
HELIX 50 16 SER C 247 THR C 257 1 11
HELIX 51 17 TYR C 272 HIS C 277 1 6
HELIX 52 18 HIS C 277 GLU C 304 1 28
HELIX 53 19 SER D 41 ARG D 46 5 6
HELIX 54 20 ILE D 48 ALA D 53 1 6
HELIX 55 21 PRO D 54 GLY D 56 5 3
HELIX 56 22 ARG D 77 LEU D 92 1 16
HELIX 57 23 ASP D 103 ARG D 116 1 14
HELIX 58 24 ASP D 134 PHE D 138 5 5
HELIX 59 25 HIS D 141 THR D 153 1 13
HELIX 60 26 GLY D 155 LEU D 162 1 8
HELIX 61 27 ASN D 165 ARG D 170 1 6
HELIX 62 28 ARG D 170 SER D 175 1 6
HELIX 63 29 SER D 181 ALA D 190 1 10
HELIX 64 30 PRO D 191 ALA D 193 5 3
HELIX 65 31 ARG D 195 SER D 197 5 3
HELIX 66 32 ARG D 198 LEU D 208 1 11
HELIX 67 33 PRO D 214 SER D 231 1 18
HELIX 68 34 SER D 247 THR D 257 1 11
HELIX 69 35 TYR D 272 ASP D 276 5 5
HELIX 70 36 HIS D 277 ALA D 297 1 21
SHEET 1 A 8 SER C 8 VAL C 14 0
SHEET 2 A 8 SER C 17 THR C 24 -1 O SER C 17 N VAL C 14
SHEET 3 A 8 HIS C 57 PRO C 61 -1 O ALA C 60 N ARG C 22
SHEET 4 A 8 HIS C 31 LEU C 35 1 N VAL C 32 O ILE C 59
SHEET 5 A 8 ALA C 97 GLN C 102 1 O TYR C 98 N LEU C 33
SHEET 6 A 8 VAL C 120 MET C 126 1 O ALA C 124 N LEU C 99
SHEET 7 A 8 LYS C 235 PRO C 242 1 O LEU C 236 N PHE C 125
SHEET 8 A 8 CYS C 261 GLY C 269 1 O LEU C 266 N VAL C 239
SHEET 1 B 8 SER D 8 VAL D 14 0
SHEET 2 B 8 SER D 17 THR D 24 -1 O TYR D 21 N HIS D 10
SHEET 3 B 8 HIS D 57 PRO D 61 -1 O ALA D 60 N ARG D 22
SHEET 4 B 8 HIS D 31 LEU D 35 1 N PHE D 34 O ILE D 59
SHEET 5 B 8 ALA D 97 GLN D 102 1 O TYR D 98 N LEU D 33
SHEET 6 B 8 VAL D 120 MET D 126 1 O ARG D 121 N ALA D 97
SHEET 7 B 8 LYS D 235 PRO D 242 1 O LEU D 236 N PHE D 125
SHEET 8 B 8 CYS D 261 GLY D 269 1 O LEU D 266 N VAL D 239
SHEET 1 C 8 SER A 8 VAL A 14 0
SHEET 2 C 8 SER A 17 THR A 24 -1 O SER A 17 N VAL A 14
SHEET 3 C 8 HIS A 57 PRO A 61 -1 O ALA A 60 N ARG A 22
SHEET 4 C 8 HIS A 31 LEU A 35 1 N VAL A 32 O ILE A 59
SHEET 5 C 8 ALA A 97 GLN A 102 1 O VAL A 100 N LEU A 35
SHEET 6 C 8 VAL A 120 MET A 126 1 O ALA A 124 N LEU A 99
SHEET 7 C 8 LYS A 235 PRO A 242 1 O LEU A 236 N PHE A 125
SHEET 8 C 8 CYS A 261 GLY A 269 1 O LEU A 266 N VAL A 239
SHEET 1 D 8 SER B 8 VAL B 14 0
SHEET 2 D 8 SER B 17 THR B 24 -1 O MET B 19 N ARG B 12
SHEET 3 D 8 HIS B 57 PRO B 61 -1 O ALA B 60 N ARG B 22
SHEET 4 D 8 HIS B 31 LEU B 35 1 N VAL B 32 O ILE B 59
SHEET 5 D 8 ALA B 97 GLN B 102 1 O TYR B 98 N LEU B 33
SHEET 6 D 8 VAL B 120 MET B 126 1 O ALA B 124 N LEU B 99
SHEET 7 D 8 LYS B 235 PRO B 242 1 O LEU B 236 N PHE B 125
SHEET 8 D 8 CYS B 261 GLY B 269 1 O ILE B 264 N LEU B 237
CISPEP 1 ASN A 38 PRO A 39 0 -1.19
CISPEP 2 GLU A 213 PRO A 214 0 -4.01
CISPEP 3 SER A 241 PRO A 242 0 3.33
CISPEP 4 ASN B 38 PRO B 39 0 -4.14
CISPEP 5 GLU B 213 PRO B 214 0 -6.43
CISPEP 6 SER B 241 PRO B 242 0 1.41
CISPEP 7 ASN C 38 PRO C 39 0 -0.17
CISPEP 8 GLU C 213 PRO C 214 0 -3.79
CISPEP 9 SER C 241 PRO C 242 0 1.51
CISPEP 10 ASN D 38 PRO D 39 0 -6.40
CISPEP 11 GLU D 213 PRO D 214 0 -2.68
CISPEP 12 SER D 241 PRO D 242 0 3.23
SITE 1 AC1 5 ASN A 38 TRP A 104 PHE A 167 PRO A 205
SITE 2 AC1 5 HOH A 746
SITE 1 AC2 4 GLY A 37 THR A 40 GLN A 102 GLN A 274
SITE 1 AC3 4 ASN B 38 TRP B 104 PHE B 167 PRO B 205
SITE 1 AC4 4 GLY B 37 THR B 40 GLN B 102 GLN B 274
SITE 1 AC5 6 HIS B 277 PRO B 278 GLU B 279 ALA B 280
SITE 2 AC5 6 HOH B 602 HOH B 662
SITE 1 AC6 5 ASN C 38 TRP C 104 PHE C 167 PRO C 205
SITE 2 AC6 5 HOH C 724
SITE 1 AC7 4 GLY C 37 THR C 40 GLN C 102 GLN C 274
SITE 1 AC8 8 ASP C 276 HIS C 277 PRO C 278 GLU C 279
SITE 2 AC8 8 ALA C 280 HOH C 688 HOH C 750 HOH C 769
SITE 1 AC9 6 GLN A 68 HOH A 676 HOH A 718 ILE C 176
SITE 2 AC9 6 LEU C 177 HOH C 784
SITE 1 BC1 4 ASN D 38 TRP D 104 PHE D 167 PRO D 205
SITE 1 BC2 4 GLY D 37 THR D 40 GLN D 102 GLN D 274
CRYST1 62.702 121.888 161.992 90.00 90.00 90.00 P 21 21 21 16
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 0.015948 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008204 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006173 0.00000
TER 2294 ALA A 301
TER 4589 SER B 296
TER 6930 GLU C 304
TER 9218 ALA D 297
MASTER 1207 0 11 70 32 0 16 6 9817 4 12 96
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