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HEADER HYDROLASE 30-OCT-14 4RPC
TITLE CRYSTAL STRUCTURE OF THE PUTATIVE ALPHA/BETA HYDROLASE FAMILY PROTEIN
TITLE 2 FROM DESULFITOBACTERIUM HAFNIENSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFITOBACTERIUM HAFNIENSE;
SOURCE 3 ORGANISM_TAXID: 272564;
SOURCE 4 STRAIN: DCB-2;
SOURCE 5 GENE: DHAF_3963;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3) MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,Z.WAWRZAK,G.MINASOV,O.KIRYUKHINA,M.ENDRES,A.JOACHIMIAK,
AUTHOR 2 W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 12-NOV-14 4RPC 0
JRNL AUTH E.V.FILIPPOVA,Z.WAWRZAK,G.MINASOV,O.KIRYUKHINA,M.ENDRES,
JRNL AUTH 2 A.JOACHIMIAK,W.F.ANDERSON,
JRNL AUTH 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL CRYSTAL STRUCTURE OF THE PUTATIVE ALPHA/BETA HYDROLASE
JRNL TITL 2 FAMILY PROTEIN FROM DESULFITOBACTERIUM HAFNIENSE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 25718
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1362
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1755
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.93000
REMARK 3 B22 (A**2) : -0.83000
REMARK 3 B33 (A**2) : -1.09000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.38000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.258
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.213
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.171
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.071
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4027 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3948 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5442 ; 1.760 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9068 ; 0.854 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 498 ; 6.324 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 188 ;38.774 ;23.830
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 660 ;16.392 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;13.558 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 603 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4530 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 900 ; 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): 1999 ; 1.464 ; 2.057
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1997 ; 1.462 ; 2.055
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2494 ; 2.268 ; 3.076
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2495 ; 2.268 ; 3.078
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2028 ; 2.342 ; 2.474
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2028 ; 2.336 ; 2.474
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2949 ; 3.701 ; 3.566
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4682 ; 6.265 ;17.737
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4683 ; 6.265 ;17.742
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 : 10
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 9 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1145 25.4610 77.3079
REMARK 3 T TENSOR
REMARK 3 T11: 0.1721 T22: 0.0077
REMARK 3 T33: 0.0446 T12: -0.0040
REMARK 3 T13: 0.0272 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 6.4564 L22: 0.9165
REMARK 3 L33: 6.0534 L12: -0.6839
REMARK 3 L13: -5.1027 L23: -0.2055
REMARK 3 S TENSOR
REMARK 3 S11: -0.2859 S12: -0.1503 S13: -0.4088
REMARK 3 S21: 0.1055 S22: -0.0242 S23: 0.1387
REMARK 3 S31: 0.4957 S32: 0.1040 S33: 0.3101
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 34 A 101
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6687 28.1417 73.0672
REMARK 3 T TENSOR
REMARK 3 T11: 0.1624 T22: 0.0170
REMARK 3 T33: 0.0180 T12: -0.0182
REMARK 3 T13: 0.0048 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 2.4890 L22: 1.0632
REMARK 3 L33: 2.2947 L12: -0.3245
REMARK 3 L13: -1.2432 L23: -0.4475
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: -0.0579 S13: -0.1398
REMARK 3 S21: -0.0591 S22: -0.0126 S23: 0.1113
REMARK 3 S31: 0.2079 S32: -0.0368 S33: 0.0124
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 102 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8819 39.0188 71.0513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1137 T22: 0.0236
REMARK 3 T33: 0.0753 T12: 0.0169
REMARK 3 T13: 0.0290 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 8.2410 L22: 1.8671
REMARK 3 L33: 4.9986 L12: 1.0116
REMARK 3 L13: -1.6010 L23: -0.6262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0672 S12: 0.2629 S13: 0.0930
REMARK 3 S21: -0.1544 S22: 0.0890 S23: 0.1954
REMARK 3 S31: -0.2487 S32: -0.2843 S33: -0.1562
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 122 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5389 36.0418 67.4474
REMARK 3 T TENSOR
REMARK 3 T11: 0.1602 T22: 0.0539
REMARK 3 T33: 0.0222 T12: 0.0132
REMARK 3 T13: 0.0154 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 2.0363 L22: 0.7557
REMARK 3 L33: 1.8222 L12: -0.0081
REMARK 3 L13: -1.0565 L23: 0.0792
REMARK 3 S TENSOR
REMARK 3 S11: 0.1247 S12: -0.1750 S13: 0.1993
REMARK 3 S21: -0.0002 S22: -0.0088 S23: -0.0447
REMARK 3 S31: -0.0392 S32: 0.3040 S33: -0.1159
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 210 A 258
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3309 43.1646 79.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.2384 T22: 0.1092
REMARK 3 T33: 0.0687 T12: -0.0613
REMARK 3 T13: 0.0456 T23: -0.0681
REMARK 3 L TENSOR
REMARK 3 L11: 4.4216 L22: 1.9848
REMARK 3 L33: 2.6373 L12: -0.1665
REMARK 3 L13: -0.0584 L23: -0.6848
REMARK 3 S TENSOR
REMARK 3 S11: 0.2767 S12: -0.3644 S13: 0.4971
REMARK 3 S21: 0.2761 S22: -0.2024 S23: -0.0017
REMARK 3 S31: -0.3548 S32: 0.2654 S33: -0.0743
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 9 B 70
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5082 17.2149 41.3656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1028 T22: 0.0872
REMARK 3 T33: 0.0952 T12: -0.0058
REMARK 3 T13: 0.0180 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 1.8905 L22: 5.8649
REMARK 3 L33: 1.5806 L12: -0.5553
REMARK 3 L13: 0.4991 L23: 0.5106
REMARK 3 S TENSOR
REMARK 3 S11: -0.1276 S12: 0.2954 S13: 0.3213
REMARK 3 S21: -0.2869 S22: 0.0607 S23: -0.5306
REMARK 3 S31: -0.1055 S32: 0.1395 S33: 0.0669
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 71 B 83
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4265 14.0075 38.4550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0870 T22: 0.1018
REMARK 3 T33: 0.1509 T12: 0.0463
REMARK 3 T13: 0.0285 T23: 0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 1.2435 L22: 9.3588
REMARK 3 L33: 4.7832 L12: 2.6727
REMARK 3 L13: -0.1942 L23: -4.5381
REMARK 3 S TENSOR
REMARK 3 S11: -0.1241 S12: 0.0756 S13: -0.1046
REMARK 3 S21: -0.2549 S22: 0.2142 S23: -0.2004
REMARK 3 S31: 0.0427 S32: -0.0944 S33: -0.0901
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 84 B 125
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7336 13.3775 52.1420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.0602
REMARK 3 T33: 0.2112 T12: 0.0539
REMARK 3 T13: -0.1030 T23: -0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 2.8860 L22: 3.5932
REMARK 3 L33: 1.1865 L12: 0.7413
REMARK 3 L13: -0.4970 L23: -1.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.3214 S12: -0.2098 S13: 0.2783
REMARK 3 S21: 0.2660 S22: 0.1052 S23: -0.7104
REMARK 3 S31: 0.0837 S32: 0.0878 S33: 0.2162
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 126 B 209
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2143 6.4470 54.0266
REMARK 3 T TENSOR
REMARK 3 T11: 0.1778 T22: 0.0722
REMARK 3 T33: 0.0350 T12: 0.0533
REMARK 3 T13: 0.0071 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.4166 L22: 2.2753
REMARK 3 L33: 1.1003 L12: -0.5769
REMARK 3 L13: -0.2386 L23: 0.5011
REMARK 3 S TENSOR
REMARK 3 S11: -0.1997 S12: 0.0037 S13: -0.0459
REMARK 3 S21: 0.3332 S22: 0.0226 S23: 0.0567
REMARK 3 S31: 0.2077 S32: -0.0976 S33: 0.1771
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 210 B 258
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9074 20.0978 59.4872
REMARK 3 T TENSOR
REMARK 3 T11: 0.2295 T22: 0.1165
REMARK 3 T33: 0.1051 T12: 0.1078
REMARK 3 T13: -0.1363 T23: -0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 2.9484 L22: 3.5274
REMARK 3 L33: 0.9062 L12: -2.5358
REMARK 3 L13: -0.3262 L23: 0.7356
REMARK 3 S TENSOR
REMARK 3 S11: -0.3093 S12: -0.2500 S13: 0.3458
REMARK 3 S21: 0.7074 S22: 0.4130 S23: -0.5568
REMARK 3 S31: 0.0141 S32: 0.0544 S33: -0.1037
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 4RPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-14.
REMARK 100 THE RCSB ID CODE IS RCSB087629.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27123
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M BIS-
REMARK 280 TRIS, 25 % PEG3350, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 22.73650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 MSE A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 GLY A 6
REMARK 465 ASN A 7
REMARK 465 CYS A 8
REMARK 465 TYR A 259
REMARK 465 CYS A 260
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 SER B 2
REMARK 465 MSE B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 ASN B 7
REMARK 465 CYS B 8
REMARK 465 TYR B 259
REMARK 465 CYS B 260
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 MSE A 123 CG - SE - CE ANGL. DEV. = -13.9 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 93 -125.45 61.92
REMARK 500 ARG B 82 48.38 32.55
REMARK 500 SER B 93 -127.56 54.00
REMARK 500 ALA B 239 19.50 58.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC113091 RELATED DB: TARGETTRACK
DBREF 4RPC A 1 260 UNP B8FSW0 B8FSW0_DESHD 1 260
DBREF 4RPC B 1 260 UNP B8FSW0 B8FSW0_DESHD 1 260
SEQADV 4RPC SER A -2 UNP B8FSW0 EXPRESSION TAG
SEQADV 4RPC ASN A -1 UNP B8FSW0 EXPRESSION TAG
SEQADV 4RPC ALA A 0 UNP B8FSW0 EXPRESSION TAG
SEQADV 4RPC SER B -2 UNP B8FSW0 EXPRESSION TAG
SEQADV 4RPC ASN B -1 UNP B8FSW0 EXPRESSION TAG
SEQADV 4RPC ALA B 0 UNP B8FSW0 EXPRESSION TAG
SEQRES 1 A 263 SER ASN ALA MSE SER MSE LYS LYS GLY ASN CYS LYS LEU
SEQRES 2 A 263 HIS ARG MSE GLY GLU PRO HIS GLY PRO LYS VAL LEU LEU
SEQRES 3 A 263 ILE HIS GLY ALA GLY PHE TYR TRP GLN THR CYS PHE ALA
SEQRES 4 A 263 ARG ILE ILE ARG ASP LEU LYS ASP ARG TYR CYS LEU LEU
SEQRES 5 A 263 ILE PRO GLU LEU GLU GLY HIS THR ALA HIS PRO ARG GLU
SEQRES 6 A 263 TYR MSE VAL SER VAL GLU GLU THR ALA GLY LYS LEU GLY
SEQRES 7 A 263 GLU ALA LEU GLU GLU LEU ARG VAL ASP LYS VAL GLN ALA
SEQRES 8 A 263 ILE TYR GLY VAL SER LEU GLY ALA SER VAL ALA VAL GLU
SEQRES 9 A 263 MSE ALA ILE ARG GLY GLU ILE LYS VAL MSE ASN LEU LEU
SEQRES 10 A 263 LEU ASP GLY GLY GLN TYR GLU GLY MSE GLY GLU MSE THR
SEQRES 11 A 263 GLU GLN TYR ALA ASN ILE MSE ALA ASP ALA PHE LEU ASN
SEQRES 12 A 263 LEU LEU ALA GLY GLU HIS LEU PRO SER PRO VAL LYS GLU
SEQRES 13 A 263 ASN MSE GLY PHE ALA ALA ASN ASN ASP VAL GLU VAL LEU
SEQRES 14 A 263 GLN PRO LEU ILE TYR GLU HIS ILE THR ARG GLU ALA LEU
SEQRES 15 A 263 LEU HIS ALA LEU LEU ALA ALA TYR ARG TYR ASP LEU LYS
SEQRES 16 A 263 ALA LYS ASN ALA ARG VAL ASP ALA ARG VAL SER VAL LEU
SEQRES 17 A 263 ILE GLY GLY ASN GLU ILE TYR GLY ALA GLN PHE THR PRO
SEQRES 18 A 263 LEU LEU ALA GLU ILE SER ARG HIS PRO LEU ASP ILE TYR
SEQRES 19 A 263 GLU PHE PRO ASN ARG GLY HIS ALA GLU VAL LEU SER LYS
SEQRES 20 A 263 GLU PRO GLU LYS ILE SER ARG LEU ILE ARG GLU ILE LEU
SEQRES 21 A 263 ASN TYR CYS
SEQRES 1 B 263 SER ASN ALA MSE SER MSE LYS LYS GLY ASN CYS LYS LEU
SEQRES 2 B 263 HIS ARG MSE GLY GLU PRO HIS GLY PRO LYS VAL LEU LEU
SEQRES 3 B 263 ILE HIS GLY ALA GLY PHE TYR TRP GLN THR CYS PHE ALA
SEQRES 4 B 263 ARG ILE ILE ARG ASP LEU LYS ASP ARG TYR CYS LEU LEU
SEQRES 5 B 263 ILE PRO GLU LEU GLU GLY HIS THR ALA HIS PRO ARG GLU
SEQRES 6 B 263 TYR MSE VAL SER VAL GLU GLU THR ALA GLY LYS LEU GLY
SEQRES 7 B 263 GLU ALA LEU GLU GLU LEU ARG VAL ASP LYS VAL GLN ALA
SEQRES 8 B 263 ILE TYR GLY VAL SER LEU GLY ALA SER VAL ALA VAL GLU
SEQRES 9 B 263 MSE ALA ILE ARG GLY GLU ILE LYS VAL MSE ASN LEU LEU
SEQRES 10 B 263 LEU ASP GLY GLY GLN TYR GLU GLY MSE GLY GLU MSE THR
SEQRES 11 B 263 GLU GLN TYR ALA ASN ILE MSE ALA ASP ALA PHE LEU ASN
SEQRES 12 B 263 LEU LEU ALA GLY GLU HIS LEU PRO SER PRO VAL LYS GLU
SEQRES 13 B 263 ASN MSE GLY PHE ALA ALA ASN ASN ASP VAL GLU VAL LEU
SEQRES 14 B 263 GLN PRO LEU ILE TYR GLU HIS ILE THR ARG GLU ALA LEU
SEQRES 15 B 263 LEU HIS ALA LEU LEU ALA ALA TYR ARG TYR ASP LEU LYS
SEQRES 16 B 263 ALA LYS ASN ALA ARG VAL ASP ALA ARG VAL SER VAL LEU
SEQRES 17 B 263 ILE GLY GLY ASN GLU ILE TYR GLY ALA GLN PHE THR PRO
SEQRES 18 B 263 LEU LEU ALA GLU ILE SER ARG HIS PRO LEU ASP ILE TYR
SEQRES 19 B 263 GLU PHE PRO ASN ARG GLY HIS ALA GLU VAL LEU SER LYS
SEQRES 20 B 263 GLU PRO GLU LYS ILE SER ARG LEU ILE ARG GLU ILE LEU
SEQRES 21 B 263 ASN TYR CYS
MODRES 4RPC MSE A 13 MET SELENOMETHIONINE
MODRES 4RPC MSE A 64 MET SELENOMETHIONINE
MODRES 4RPC MSE A 102 MET SELENOMETHIONINE
MODRES 4RPC MSE A 111 MET SELENOMETHIONINE
MODRES 4RPC MSE A 123 MET SELENOMETHIONINE
MODRES 4RPC MSE A 126 MET SELENOMETHIONINE
MODRES 4RPC MSE A 134 MET SELENOMETHIONINE
MODRES 4RPC MSE A 155 MET SELENOMETHIONINE
MODRES 4RPC MSE B 13 MET SELENOMETHIONINE
MODRES 4RPC MSE B 64 MET SELENOMETHIONINE
MODRES 4RPC MSE B 102 MET SELENOMETHIONINE
MODRES 4RPC MSE B 111 MET SELENOMETHIONINE
MODRES 4RPC MSE B 123 MET SELENOMETHIONINE
MODRES 4RPC MSE B 126 MET SELENOMETHIONINE
MODRES 4RPC MSE B 134 MET SELENOMETHIONINE
MODRES 4RPC MSE B 155 MET SELENOMETHIONINE
HET MSE A 13 8
HET MSE A 64 8
HET MSE A 102 8
HET MSE A 111 8
HET MSE A 123 8
HET MSE A 126 8
HET MSE A 134 8
HET MSE A 155 8
HET MSE B 13 8
HET MSE B 64 8
HET MSE B 102 8
HET MSE B 111 8
HET MSE B 123 8
HET MSE B 126 8
HET MSE B 134 8
HET MSE B 155 8
HET PG4 A 301 7
HET TRS A 302 8
HETNAM MSE SELENOMETHIONINE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 TRS C4 H12 N O3 1+
FORMUL 5 HOH *233(H2 O)
HELIX 1 1 TYR A 30 PHE A 35 1 6
HELIX 2 2 PHE A 35 LYS A 43 1 9
HELIX 3 3 SER A 66 LEU A 81 1 16
HELIX 4 4 SER A 93 GLY A 106 1 14
HELIX 5 5 MSE A 123 GLU A 125 5 3
HELIX 6 6 MSE A 126 ALA A 143 1 18
HELIX 7 7 PRO A 150 MSE A 155 1 6
HELIX 8 8 ASN A 161 GLN A 167 1 7
HELIX 9 9 PRO A 168 ILE A 170 5 3
HELIX 10 10 THR A 175 TYR A 189 1 15
HELIX 11 11 LEU A 191 ASN A 195 5 5
HELIX 12 12 PHE A 216 SER A 224 1 9
HELIX 13 13 ALA A 239 GLU A 245 1 7
HELIX 14 14 GLU A 245 LEU A 257 1 13
HELIX 15 15 TYR B 30 LYS B 43 1 14
HELIX 16 16 SER B 66 LEU B 81 1 16
HELIX 17 17 SER B 93 GLY B 106 1 14
HELIX 18 18 MSE B 123 GLU B 125 5 3
HELIX 19 19 MSE B 126 ALA B 143 1 18
HELIX 20 20 PRO B 150 MSE B 155 1 6
HELIX 21 21 ASN B 161 GLN B 167 1 7
HELIX 22 22 PRO B 168 ILE B 170 5 3
HELIX 23 23 THR B 175 TYR B 189 1 15
HELIX 24 24 ASP B 190 ASN B 195 1 6
HELIX 25 25 GLY B 213 GLN B 215 5 3
HELIX 26 26 PHE B 216 SER B 224 1 9
HELIX 27 27 ALA B 239 GLU B 245 1 7
HELIX 28 28 GLU B 245 LEU B 257 1 13
SHEET 1 A 7 LEU A 10 GLY A 14 0
SHEET 2 A 7 CYS A 47 PRO A 51 -1 O ILE A 50 N HIS A 11
SHEET 3 A 7 LYS A 20 ILE A 24 1 N VAL A 21 O CYS A 47
SHEET 4 A 7 ALA A 88 VAL A 92 1 O ALA A 88 N LEU A 22
SHEET 5 A 7 ASN A 112 ASP A 116 1 O LEU A 114 N ILE A 89
SHEET 6 A 7 ARG A 201 GLY A 207 1 O SER A 203 N LEU A 113
SHEET 7 A 7 ASP A 229 PHE A 233 1 O TYR A 231 N VAL A 204
SHEET 1 B 2 LYS A 85 VAL A 86 0
SHEET 2 B 2 LYS A 109 VAL A 110 1 O LYS A 109 N VAL A 86
SHEET 1 C 7 LEU B 10 GLY B 14 0
SHEET 2 C 7 CYS B 47 PRO B 51 -1 O ILE B 50 N HIS B 11
SHEET 3 C 7 LYS B 20 ILE B 24 1 N VAL B 21 O CYS B 47
SHEET 4 C 7 LYS B 85 VAL B 92 1 O TYR B 90 N ILE B 24
SHEET 5 C 7 LYS B 109 ASP B 116 1 O LEU B 114 N ILE B 89
SHEET 6 C 7 ARG B 201 GLY B 207 1 O SER B 203 N LEU B 113
SHEET 7 C 7 ASP B 229 PHE B 233 1 O TYR B 231 N VAL B 204
LINK C ARG A 12 N MSE A 13 1555 1555 1.31
LINK C MSE A 13 N GLY A 14 1555 1555 1.33
LINK C TYR A 63 N MSE A 64 1555 1555 1.32
LINK C MSE A 64 N VAL A 65 1555 1555 1.33
LINK C GLU A 101 N MSE A 102 1555 1555 1.31
LINK C MSE A 102 N ALA A 103 1555 1555 1.34
LINK C VAL A 110 N MSE A 111 1555 1555 1.32
LINK C MSE A 111 N ASN A 112 1555 1555 1.33
LINK C GLY A 122 N MSE A 123 1555 1555 1.31
LINK C MSE A 123 N GLY A 124 1555 1555 1.31
LINK C GLU A 125 N MSE A 126 1555 1555 1.35
LINK C MSE A 126 N THR A 127 1555 1555 1.33
LINK C ILE A 133 N MSE A 134 1555 1555 1.31
LINK C MSE A 134 N ALA A 135 1555 1555 1.34
LINK C ASN A 154 N MSE A 155 1555 1555 1.33
LINK C MSE A 155 N GLY A 156 1555 1555 1.34
LINK C ARG B 12 N MSE B 13 1555 1555 1.32
LINK C MSE B 13 N GLY B 14 1555 1555 1.32
LINK C TYR B 63 N MSE B 64 1555 1555 1.33
LINK C MSE B 64 N VAL B 65 1555 1555 1.32
LINK C GLU B 101 N MSE B 102 1555 1555 1.32
LINK C MSE B 102 N ALA B 103 1555 1555 1.32
LINK C VAL B 110 N MSE B 111 1555 1555 1.35
LINK C MSE B 111 N ASN B 112 1555 1555 1.34
LINK C GLY B 122 N MSE B 123 1555 1555 1.33
LINK C MSE B 123 N GLY B 124 1555 1555 1.33
LINK C GLU B 125 N MSE B 126 1555 1555 1.33
LINK C MSE B 126 N THR B 127 1555 1555 1.33
LINK C ILE B 133 N MSE B 134 1555 1555 1.33
LINK C MSE B 134 N ALA B 135 1555 1555 1.33
LINK C ASN B 154 N MSE B 155 1555 1555 1.33
LINK C MSE B 155 N GLY B 156 1555 1555 1.33
CISPEP 1 SER A 149 PRO A 150 0 2.33
CISPEP 2 SER B 149 PRO B 150 0 1.53
SITE 1 AC1 1 TRS A 302
SITE 1 AC2 4 SER A 149 PRO A 150 PG4 A 301 TYR B 212
CRYST1 61.661 45.473 82.787 90.00 90.56 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016218 0.000000 0.000159 0.00000
SCALE2 0.000000 0.021991 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012080 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.931942 -0.258140 0.254652 49.14965 1
MTRIX2 2 0.261715 0.007228 0.965118 -26.30386 1
MTRIX3 2 -0.250976 0.966080 0.060823 67.89312 1
TER 1969 ASN A 258
TER 3938 ASN B 258
MASTER 509 0 18 28 16 0 2 12 4184 2 175 42
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