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HEADER HYDROLASE 08-APR-09 2WFL
TITLE CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYNEURIDINE-ALDEHYDE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.78;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: POLYNEURIDINE-ALDEHYDE ESTERASE;
COMPND 8 CHAIN: B;
COMPND 9 EC: 3.1.1.78;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;
SOURCE 3 ORGANISM_COMMON: SERPENTWOOD;
SOURCE 4 ORGANISM_TAXID: 4060;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15PREP4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE-2;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;
SOURCE 12 ORGANISM_COMMON: SERPENTWOOD;
SOURCE 13 ORGANISM_TAXID: 4060;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: M15PREP4;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PQE-2
KEYWDS ALKALOID METABOLISM, MONOTERPENOID INDOLE ALKALOIDS, PNAE,
KEYWDS 2 HYDROLASE, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.YANG,M.HILL,S.PANJIKAR,M.WANG,J.STOECKIGT
REVDAT 1 18-AUG-09 2WFL 0
JRNL AUTH L.YANG,M.HILL,M.WANG,S.PANJIKAR,J.STOCKIGT
JRNL TITL STRUCTURAL BASIS AND ENZYMATIC MECHANISM OF THE
JRNL TITL 2 BIOSYNTHESIS OF C9- FROM C10-MONOTERPENOID INDOLE
JRNL TITL 3 ALKALOIDS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 48 5211 2009
JRNL REFN ISSN 1433-7851
JRNL PMID 19496101
JRNL DOI 10.1002/ANIE.200900150
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35684
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1046
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) : 2599
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.17000
REMARK 3 B22 (A**2) : -1.32000
REMARK 3 B33 (A**2) : -1.85000
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): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.780
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4146 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5566 ; 1.897 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 502 ; 7.550 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 176 ;34.099 ;24.659
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 741 ;15.995 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;20.104 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 590 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3072 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2548 ; 0.899 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4086 ; 1.626 ; 2.500
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1598 ; 3.630 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1480 ; 5.229 ;10.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 9 A 54 2
REMARK 3 1 B 9 B 54 2
REMARK 3 2 A 60 A 113 2
REMARK 3 2 B 60 B 113 2
REMARK 3 3 A 157 A 262 2
REMARK 3 3 B 157 B 262 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 820 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 820 ; 0.06 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 797 ; 0.22 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 797 ; 0.22 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 820 ; 0.22 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 820 ; 0.22 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 797 ; 0.30 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 797 ; 0.30 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 54
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3615 104.6133 18.9323
REMARK 3 T TENSOR
REMARK 3 T11: -0.1091 T22: -0.1664
REMARK 3 T33: -0.1489 T12: 0.0724
REMARK 3 T13: -0.0301 T23: -0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 3.2627 L22: 2.6489
REMARK 3 L33: 2.7434 L12: 0.6366
REMARK 3 L13: -0.2349 L23: -0.6094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0846 S12: 0.1758 S13: -0.3988
REMARK 3 S21: -0.3401 S22: -0.1053 S23: -0.1132
REMARK 3 S31: 0.3845 S32: 0.0049 S33: 0.0207
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 60 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0912 106.5370 9.0303
REMARK 3 T TENSOR
REMARK 3 T11: 0.0262 T22: -0.0420
REMARK 3 T33: -0.1585 T12: 0.1528
REMARK 3 T13: 0.0274 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 3.7223 L22: 3.7300
REMARK 3 L33: 3.8214 L12: 1.0544
REMARK 3 L13: 0.1782 L23: 1.8193
REMARK 3 S TENSOR
REMARK 3 S11: 0.1031 S12: 0.3797 S13: -0.2945
REMARK 3 S21: -0.4545 S22: -0.0530 S23: -0.3066
REMARK 3 S31: 0.4997 S32: 0.3896 S33: -0.0502
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 157 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4344 113.9559 10.5591
REMARK 3 T TENSOR
REMARK 3 T11: -0.0427 T22: -0.0870
REMARK 3 T33: -0.1386 T12: 0.0881
REMARK 3 T13: -0.0550 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 2.7187 L22: 2.0522
REMARK 3 L33: 2.5049 L12: -0.4033
REMARK 3 L13: -0.1870 L23: 0.0906
REMARK 3 S TENSOR
REMARK 3 S11: 0.2003 S12: 0.4894 S13: -0.0610
REMARK 3 S21: -0.5389 S22: -0.0689 S23: 0.1235
REMARK 3 S31: 0.1420 S32: -0.1995 S33: -0.1314
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 : B 9 B 54
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7378 115.6252 38.9784
REMARK 3 T TENSOR
REMARK 3 T11: -0.2079 T22: -0.2150
REMARK 3 T33: -0.1875 T12: 0.0329
REMARK 3 T13: 0.0060 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 6.5010 L22: 2.8942
REMARK 3 L33: 2.4192 L12: -1.2803
REMARK 3 L13: 1.0910 L23: 0.0314
REMARK 3 S TENSOR
REMARK 3 S11: -0.0669 S12: -0.0206 S13: 0.2493
REMARK 3 S21: 0.1103 S22: 0.0129 S23: 0.2217
REMARK 3 S31: -0.1706 S32: -0.2348 S33: 0.0540
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 60 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9437 117.9304 50.1232
REMARK 3 T TENSOR
REMARK 3 T11: -0.1109 T22: -0.1389
REMARK 3 T33: -0.1866 T12: 0.0574
REMARK 3 T13: 0.0136 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 4.5215 L22: 3.0241
REMARK 3 L33: 2.8976 L12: 0.0487
REMARK 3 L13: -0.4362 L23: 1.2552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: -0.2987 S13: 0.1972
REMARK 3 S21: 0.3201 S22: 0.0898 S23: 0.0239
REMARK 3 S31: -0.1515 S32: -0.0205 S33: -0.0508
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 157 B 262
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3270 104.0289 46.6786
REMARK 3 T TENSOR
REMARK 3 T11: -0.1122 T22: -0.1009
REMARK 3 T33: -0.0764 T12: 0.0103
REMARK 3 T13: 0.0351 T23: 0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 1.6015 L22: 2.4848
REMARK 3 L33: 2.0707 L12: -0.1884
REMARK 3 L13: 0.0305 L23: 0.5384
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.3765 S13: -0.1749
REMARK 3 S21: 0.4148 S22: 0.0590 S23: 0.3250
REMARK 3 S31: 0.2978 S32: -0.2524 S33: -0.0633
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2WFL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-09.
REMARK 100 THE PDBE ID CODE IS EBI-39424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : SILICON 111
REMARK 200 OPTICS : DOUBLE CRYSTAL SI 111
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36861
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.6
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 32.50
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.3
REMARK 200 R MERGE FOR SHELL (I) : 0.54
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW,MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1XKL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M BIS-TRIS, 0.25M LI2SO4,
REMARK 280 25%POLYETHYLENE GLYCOL 3350, PH6.30.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.37900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 88.45850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.37900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 88.45850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.37900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 88.45850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.37900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 88.45850
REMARK 290 SMTRY3 8 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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 MET A 1
REMARK 465 HIS A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ASN A 6
REMARK 465 ALA A 7
REMARK 465 LYS A 8
REMARK 465 SER A 264
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 ALA B 7
REMARK 465 LYS B 8
REMARK 465 SER B 264
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG B 54 - O HOH B 2035 1.87
REMARK 500 O LYS B 196 - O HOH B 2126 2.16
REMARK 500 O HOH A 2007 - O HOH A 2095 2.15
REMARK 500 O HOH A 2019 - O HOH A 2023 1.81
REMARK 500 O HOH A 2042 - O HOH A 2082 2.12
REMARK 500 O HOH A 2061 - O HOH A 2069 2.05
REMARK 500 O HOH B 2041 - O HOH B 2151 2.16
REMARK 500 O HOH B 2098 - O HOH B 2153 1.99
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 CA ALA A 134 O ALA B 73 6564 1.95
REMARK 500 CB ALA A 134 C ALA B 73 6564 1.74
REMARK 500 CB ALA A 134 O ALA B 73 6564 0.58
REMARK 500 ND2 ASN A 147 CD PRO A 148 3655 1.96
REMARK 500 CD PRO A 148 CD PRO A 148 3655 2.10
REMARK 500 CB MET A 153 OD2 ASP B 78 6564 1.68
REMARK 500 CG MET A 153 CG ASP B 78 6564 1.72
REMARK 500 CG MET A 153 OD2 ASP B 78 6564 0.53
REMARK 500 SD MET A 153 CG ASP B 78 6564 0.85
REMARK 500 SD MET A 153 OD1 ASP B 78 6564 0.94
REMARK 500 SD MET A 153 OD2 ASP B 78 6564 1.49
REMARK 500 CE MET A 153 CA ASP B 78 6564 1.84
REMARK 500 CE MET A 153 CB ASP B 78 6564 0.55
REMARK 500 CE MET A 153 CG ASP B 78 6564 1.22
REMARK 500 CE MET A 153 OD1 ASP B 78 6564 2.01
REMARK 500 CA SER A 199 OE1 GLU B 149 3655 1.73
REMARK 500 C SER A 199 CD GLU B 149 3655 1.92
REMARK 500 C SER A 199 OE1 GLU B 149 3655 1.41
REMARK 500 CB SER A 199 OE1 GLU B 149 3655 1.76
REMARK 500 N THR A 200 CD GLU B 149 3655 1.69
REMARK 500 N THR A 200 OE2 GLU B 149 3655 1.56
REMARK 500 N THR A 200 OE1 GLU B 149 3655 1.56
REMARK 500 CA THR A 200 CD GLU B 149 3655 2.16
REMARK 500 CA THR A 200 OE2 GLU B 149 3655 1.10
REMARK 500 C THR A 200 CD GLU B 149 3655 1.89
REMARK 500 C THR A 200 OE2 GLU B 149 3655 0.94
REMARK 500 C THR A 200 O HOH B 2094 3655 2.04
REMARK 500 O THR A 200 OE2 GLU B 149 3655 2.14
REMARK 500 O THR A 200 O HOH B 2094 3655 2.14
REMARK 500 CB THR A 200 O HOH B 2091 3655 1.77
REMARK 500 OG1 THR A 200 O HOH B 2091 3655 0.75
REMARK 500 N GLU A 201 CD GLU B 149 3655 1.32
REMARK 500 N GLU A 201 OE2 GLU B 149 3655 1.32
REMARK 500 N GLU A 201 CB GLU B 149 3655 2.15
REMARK 500 N GLU A 201 CG GLU B 149 3655 1.42
REMARK 500 CA GLU A 201 CB GLU B 149 3655 1.83
REMARK 500 CA GLU A 201 CG GLU B 149 3655 1.53
REMARK 500 C GLU A 201 CG GLU B 149 3655 2.01
REMARK 500 CB GLU A 201 CA GLU B 149 3655 1.05
REMARK 500 CB GLU A 201 C GLU B 149 3655 2.08
REMARK 500 CB GLU A 201 CB GLU B 149 3655 0.87
REMARK 500 CB GLU A 201 CG GLU B 149 3655 1.86
REMARK 500 CG GLU A 201 O GLU B 149 3655 1.67
REMARK 500 CG GLU A 201 CA GLU B 149 3655 1.30
REMARK 500 CG GLU A 201 C GLU B 149 3655 1.52
REMARK 500 CD GLU A 201 O GLU B 149 3655 1.25
REMARK 500 CD GLU A 201 CA GLU B 149 3655 1.83
REMARK 500 CD GLU A 201 C GLU B 149 3655 0.66
REMARK 500 CD GLU A 201 N ASN B 150 3655 1.44
REMARK 500 OE1 GLU A 201 O GLU B 149 3655 1.90
REMARK 500
REMARK 500 THIS ENTRY HAS 79 SYMMETRY CONTACTS
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 LYS A 30 CE LYS A 30 NZ -0.152
REMARK 500 VAL A 43 CB VAL A 43 CG2 -0.166
REMARK 500 ARG A 53 CG ARG A 53 CD -0.194
REMARK 500 GLU A 102 CD GLU A 102 OE1 -0.076
REMARK 500 VAL B 43 CB VAL B 43 CG2 -0.131
REMARK 500 ARG B 53 CD ARG B 53 NE -0.116
REMARK 500 ARG B 53 CG ARG B 53 CD -0.222
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 53 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 GLU A 102 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 VAL B 43 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 53 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ASP B 234 CB - CG - OD2 ANGL. DEV. = 7.3 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 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 21 -158.11 -121.06
REMARK 500 ASP A 56 2.97 -66.40
REMARK 500 SER A 87 -131.41 57.00
REMARK 500 LEU A 138 -119.58 60.73
REMARK 500 ASN A 150 69.93 -163.73
REMARK 500 LYS A 196 104.54 -3.15
REMARK 500 ARG A 202 -75.13 -108.80
REMARK 500 MET A 245 67.23 -107.09
REMARK 500 LEU B 21 -156.06 -117.05
REMARK 500 SER B 87 -129.59 48.76
REMARK 500 PRO B 133 143.86 -37.73
REMARK 500 ASP B 135 42.20 -108.45
REMARK 500 LEU B 138 -119.60 53.86
REMARK 500 ASN B 150 69.31 -152.62
REMARK 500 ARG B 202 -79.87 -107.70
REMARK 500 MET B 245 65.89 -108.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 195 LYS A 196 109.54
REMARK 500 ALA B 195 LYS B 196 70.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS B 256 -14.03
REMARK 500 CME B 257 -15.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1264
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WFM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE
REMARK 900 ESTERASE
DBREF 2WFL A 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
DBREF 2WFL B 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
SEQRES 1 A 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 A 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 A 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 A 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 A 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 A 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 A 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 A 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 A 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 A 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 A 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 A 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 A 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 A 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 A 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 A 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 A 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 A 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 A 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP HIS MET GLY MET
SEQRES 20 A 264 LEU SER GLN PRO ARG GLU VAL CME LYS CYS LEU LEU ASP
SEQRES 21 A 264 ILE SER ASP SER
SEQRES 1 B 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 B 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 B 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 B 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 B 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 B 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 B 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 B 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 B 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 B 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 B 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 B 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 B 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 B 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 B 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 B 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 B 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 B 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 B 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP HIS MET GLY MET
SEQRES 20 B 264 LEU SER GLN PRO ARG GLU VAL CME LYS CME LEU LEU ASP
SEQRES 21 B 264 ILE SER ASP SER
MODRES 2WFL CME A 255 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2WFL CME B 255 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2WFL CME B 257 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 255 10
HET CME B 255 10
HET CME B 257 10
HET SO4 B1264 5
HET SO4 A1264 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
FORMUL 3 CME 3(C5 H11 N O3 S2)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 HOH *303(H2 O1)
HELIX 1 1 GLY A 22 TYR A 27 5 6
HELIX 2 2 LYS A 28 ALA A 36 1 9
HELIX 3 3 ARG A 54 ILE A 58 5 5
HELIX 4 4 THR A 60 ILE A 75 1 16
HELIX 5 5 PHE A 88 TYR A 100 1 13
HELIX 6 6 THR A 122 CYS A 132 1 11
HELIX 7 7 GLY A 158 MET A 166 1 9
HELIX 8 8 SER A 171 THR A 182 1 12
HELIX 9 9 PHE A 188 ALA A 193 1 6
HELIX 10 10 ARG A 202 VAL A 206 5 5
HELIX 11 11 PRO A 220 GLY A 232 1 13
HELIX 12 12 MET A 245 GLN A 250 1 6
HELIX 13 13 LYS A 256 ASP A 263 1 8
HELIX 14 14 GLY B 22 TYR B 27 5 6
HELIX 15 15 LYS B 28 ALA B 36 1 9
HELIX 16 16 ARG B 54 ILE B 58 5 5
HELIX 17 17 THR B 60 ILE B 75 1 16
HELIX 18 18 PHE B 88 TYR B 100 1 13
HELIX 19 19 THR B 122 CYS B 132 1 11
HELIX 20 20 GLY B 158 MET B 166 1 9
HELIX 21 21 SER B 171 THR B 182 1 12
HELIX 22 22 PHE B 188 ALA B 193 1 6
HELIX 23 23 ARG B 202 VAL B 206 5 5
HELIX 24 24 PRO B 220 GLY B 232 1 13
HELIX 25 25 MET B 245 GLN B 250 1 6
HELIX 26 26 LEU B 258 ASP B 263 1 6
SHEET 1 AA 6 LYS A 39 VAL A 43 0
SHEET 2 AA 6 HIS A 12 VAL A 16 1 O PHE A 13 N THR A 41
SHEET 3 AA 6 VAL A 81 HIS A 86 1 O VAL A 82 N VAL A 14
SHEET 4 AA 6 ILE A 104 MET A 110 1 N SER A 105 O VAL A 81
SHEET 5 AA 6 ARG A 208 CYS A 213 1 O ALA A 209 N PHE A 109
SHEET 6 AA 6 LYS A 235 ILE A 239 1 O LYS A 235 N TYR A 210
SHEET 1 AB 3 GLN A 141 TYR A 145 0
SHEET 2 AB 3 GLY A 152 ILE A 156 -1 O GLY A 152 N TYR A 145
SHEET 3 AB 3 GLY A 185 SER A 186 -1 O GLY A 185 N MET A 155
SHEET 1 BA 6 LYS B 39 VAL B 43 0
SHEET 2 BA 6 HIS B 12 VAL B 16 1 O PHE B 13 N THR B 41
SHEET 3 BA 6 VAL B 81 HIS B 86 1 O VAL B 82 N VAL B 14
SHEET 4 BA 6 ILE B 104 MET B 110 1 N SER B 105 O VAL B 81
SHEET 5 BA 6 ARG B 208 CYS B 213 1 O ALA B 209 N PHE B 109
SHEET 6 BA 6 LYS B 235 ILE B 239 1 O LYS B 235 N TYR B 210
SHEET 1 BB 2 GLN B 141 TYR B 145 0
SHEET 2 BB 2 GLY B 152 ILE B 156 -1 O GLY B 152 N TYR B 145
LINK C VAL A 254 N CME A 255 1555 1555 1.28
LINK C CME A 255 N LYS A 256 1555 1555 1.27
LINK C VAL B 254 N CME B 255 1555 1555 1.29
LINK C CME B 255 N LYS B 256 1555 1555 1.29
LINK C LYS B 256 N CME B 257 1555 1555 1.28
LINK C CME B 257 N LEU B 258 1555 1555 1.26
SITE 1 AC1 10 GLY B 152 MET B 153 SER B 186 PHE B 188
SITE 2 AC1 10 PHE B 189 GLN B 190 HOH B2099 HOH B2151
SITE 3 AC1 10 HOH B2152 HOH B2153
SITE 1 AC2 5 SER A 87 SER A 218 HIS A 244 HOH A2001
SITE 2 AC2 5 HOH A2150
CRYST1 92.758 176.917 75.697 90.00 90.00 90.00 C 2 2 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 0.010781 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013211 0.00000
MTRIX1 1 0.708500 0.681800 0.182000 -73.44000 1
MTRIX2 1 0.685800 -0.726000 0.050360 173.20000 1
MTRIX3 1 0.166500 0.089170 -0.982000 43.62000 1
TER 2016 ASP A 263
TER 4036 ASP B 263
MASTER 627 0 5 26 17 0 5 9 4347 2 46 42
END |