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HEADER HYDROLASE 26-APR-19 6RJ8
TITLE STRUCTURE OF THE ALPHA-BETA HYDROLASE CORS FROM TABERNATHE IBOGA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BETA HYDROLASE CORS;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.105;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TABERNANTHE IBOGA;
SOURCE 3 ORGANISM_TAXID: 141617;
SOURCE 4 GENE: CORS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: SOLUBL21
KEYWDS ALKALOID, IBOGA, CORONARIDINE, NATURAL PRODUCT, BIOSYNTHESIS,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.FARROW,L.CAPUTI,M.O.KAMILEEN,K.BUSSEY,C.E.M.STEVENSON,J.MUNDY,
AUTHOR 2 D.M.LAWSON,S.E.O'CONNOR
REVDAT 1 04-MAR-20 6RJ8 0
JRNL AUTH L.CAPUTI,J.FRANKE,K.BUSSEY,S.C.FARROW,I.J.C.VIEIRA,
JRNL AUTH 2 C.E.M.STEVENSON,D.M.LAWSON,S.E.O'CONNOR
JRNL TITL STRUCTURAL BASIS OF CYCLOADDITION IN BIOSYNTHESIS OF IBOGA
JRNL TITL 2 AND ASPIDOSPERMA ALKALOIDS.
JRNL REF NAT.CHEM.BIOL. 2020
JRNL REFN ESSN 1552-4469
JRNL PMID 32066966
JRNL DOI 10.1038/S41589-019-0460-X
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 90713
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4757
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6590
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 340
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2491
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 347
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 0.55000
REMARK 3 B12 (A**2) : -0.09000
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): 0.048
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.032
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.821
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2666 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2435 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3615 ; 1.500 ; 1.640
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5660 ; 1.405 ; 1.573
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 329 ; 7.177 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;32.572 ;22.362
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 413 ;11.616 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.383 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 326 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2975 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 569 ; 0.002 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5098 ; 1.584 ; 3.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6RJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101988.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS 1.5.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95612
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
REMARK 200 RESOLUTION RANGE LOW (A) : 71.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 37.10
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 37.80
REMARK 200 R MERGE FOR SHELL (I) : 1.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.7.17
REMARK 200 STARTING MODEL: 2O7R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, PH 6, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 165.03733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 82.51867
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 123.77800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.25933
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 206.29667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 165.03733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 82.51867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 41.25933
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 123.77800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 206.29667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 5770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 22.0 KCAL/MOL
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 BIOMT1 2 0.500000 0.866025 0.000000 41.41900
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -71.73981
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -41.25933
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 610 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 638 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 790 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 PRO A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
REMARK 465 GLU A 325
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 ASP A 9 CG OD1 OD2
REMARK 470 LYS A 23 CG CD CE NZ
REMARK 470 ILE A 67 CG1 CG2 CD1
REMARK 470 GLU A 71 CD OE1 OE2
REMARK 470 LYS A 72 CD CE NZ
REMARK 470 LYS A 150 NZ
REMARK 470 LYS A 249 CD CE NZ
REMARK 470 LYS A 284 NZ
REMARK 470 LYS A 324 CE NZ
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 ALA A 84 67.36 77.20
REMARK 500 GLU A 89 -171.07 71.21
REMARK 500 LYS A 108 71.36 63.37
REMARK 500 SER A 174 -128.73 53.71
REMARK 500 ILE A 222 -75.87 -118.61
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 946 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 948 DISTANCE = 6.26 ANGSTROMS
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
DBREF 6RJ8 A 0 325 PDB 6RJ8 6RJ8 0 325
SEQRES 1 A 326 GLY PRO ALA ASN SER THR ALA ASN SER ASP GLU ILE VAL
SEQRES 2 A 326 PHE ASP LEU HIS PRO TYR ILE ARG VAL PHE LYS ASN GLY
SEQRES 3 A 326 LYS VAL GLU ARG LEU HIS ASP THR PRO TYR VAL PRO PRO
SEQRES 4 A 326 SER LEU GLU ASP PRO ALA THR GLY VAL SER TRP LYS ASP
SEQRES 5 A 326 VAL PRO ILE SER SER ASP VAL SER ALA ARG VAL TYR LEU
SEQRES 6 A 326 PRO LYS ILE SER GLU ALA GLU LYS LYS LYS LEU PRO ILE
SEQRES 7 A 326 PHE VAL TYR PHE HIS GLY ALA GLY PHE CYS LEU GLU SER
SEQRES 8 A 326 ALA PHE LYS SER PHE PHE HIS THR TYR VAL LYS HIS VAL
SEQRES 9 A 326 VAL ALA GLU THR LYS ALA VAL GLY VAL SER VAL GLU TYR
SEQRES 10 A 326 ARG LEU ALA PRO GLU HIS PRO LEU PRO ALA ALA TYR GLU
SEQRES 11 A 326 ASP CYS TRP THR ALA LEU GLN TRP VAL ALA SER HIS VAL
SEQRES 12 A 326 GLY LEU ASP ASN SER SER LEU LYS ASN ALA ILE ASP LYS
SEQRES 13 A 326 GLU PRO TRP ILE ILE ASN HIS GLY ASP LEU ASN LYS LEU
SEQRES 14 A 326 TYR LEU GLY GLY ASP SER PRO GLY GLY ASN ILE VAL HIS
SEQRES 15 A 326 ASN VAL LEU ILE ARG ALA GLY LYS GLU SER LEU HIS GLY
SEQRES 16 A 326 GLY VAL LYS ILE ARG GLY ALA ILE LEU TYR TYR PRO TYR
SEQRES 17 A 326 PHE LEU ILE ARG THR SER LYS ARG GLN SER ASP TYR MET
SEQRES 18 A 326 GLU ILE ASP TYR ARG GLY TYR TRP LYS LEU ALA TYR PRO
SEQRES 19 A 326 SER ALA PRO GLY GLY THR ASP ASN PRO MET ILE ASN PRO
SEQRES 20 A 326 VAL ALA LYS ASN ALA PRO ASP LEU ALA GLY TYR GLY CYS
SEQRES 21 A 326 SER ARG LEU LEU VAL SER MET VAL SER ASP GLU THR ARG
SEQRES 22 A 326 ASP ILE THR LEU LEU TYR LEU GLU ALA LEU LYS LYS SER
SEQRES 23 A 326 GLY TRP LYS GLY GLU LEU GLU VAL GLY ASP TYR GLU ALA
SEQRES 24 A 326 HIS PHE PHE ASP LEU PHE SER PRO GLU ASN GLU VAL GLY
SEQRES 25 A 326 LYS THR TRP ILE LYS ARG SER SER ASP PHE ILE ASN LYS
SEQRES 26 A 326 GLU
HET PG4 A 501 13
HET PG4 A 502 13
HET PEG A 503 7
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET EDO A 508 4
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 PG4 2(C8 H18 O5)
FORMUL 4 PEG C4 H10 O3
FORMUL 5 EDO 5(C2 H6 O2)
FORMUL 10 HOH *347(H2 O)
HELIX 1 AA1 LYS A 93 LYS A 108 1 16
HELIX 2 AA2 PRO A 125 SER A 140 1 16
HELIX 3 AA3 ASP A 145 ASN A 151 5 7
HELIX 4 AA4 GLU A 156 HIS A 162 1 7
HELIX 5 AA5 SER A 174 GLU A 190 1 17
HELIX 6 AA6 LEU A 192 VAL A 196 5 5
HELIX 7 AA7 SER A 217 ILE A 222 1 6
HELIX 8 AA8 ILE A 222 TYR A 232 1 11
HELIX 9 AA9 GLY A 237 ASN A 241 5 5
HELIX 10 AB1 ASP A 253 TYR A 257 5 5
HELIX 11 AB2 GLU A 270 SER A 285 1 16
HELIX 12 AB3 HIS A 299 SER A 305 5 7
HELIX 13 AB4 ASN A 308 LYS A 324 1 17
SHEET 1 AA1 3 ILE A 11 LEU A 15 0
SHEET 2 AA1 3 ILE A 19 PHE A 22 -1 O VAL A 21 N PHE A 13
SHEET 3 AA1 3 VAL A 27 GLU A 28 -1 O GLU A 28 N ARG A 20
SHEET 1 AA2 8 SER A 48 PRO A 53 0
SHEET 2 AA2 8 SER A 59 LEU A 64 -1 O VAL A 62 N LYS A 50
SHEET 3 AA2 8 VAL A 110 GLU A 115 -1 O SER A 113 N ARG A 61
SHEET 4 AA2 8 LEU A 75 PHE A 81 1 N PHE A 78 O VAL A 110
SHEET 5 AA2 8 GLY A 163 ASP A 173 1 O ASP A 164 N LEU A 75
SHEET 6 AA2 8 GLY A 200 TYR A 204 1 O TYR A 204 N GLY A 172
SHEET 7 AA2 8 ARG A 261 VAL A 267 1 O LEU A 263 N LEU A 203
SHEET 8 AA2 8 GLU A 290 TYR A 296 1 O GLU A 292 N LEU A 262
CISPEP 1 HIS A 16 PRO A 17 0 -3.60
CISPEP 2 ALA A 119 PRO A 120 0 -1.62
CISPEP 3 LEU A 124 PRO A 125 0 11.08
SITE 1 AC1 7 TYR A 18 HIS A 31 ALA A 84 PHE A 95
SITE 2 AC1 7 TYR A 227 PHE A 301 HOH A 617
SITE 1 AC2 7 GLU A 41 ASP A 42 PRO A 43 THR A 45
SITE 2 AC2 7 GLY A 46 LYS A 66 LYS A 214
SITE 1 AC3 6 ASN A 151 ARG A 211 THR A 212 SER A 213
SITE 2 AC3 6 ARG A 215 HOH A 701
SITE 1 AC4 6 ILE A 210 ARG A 211 ARG A 225 THR A 239
SITE 2 AC4 6 ASP A 240 HOH A 711
SITE 1 AC5 3 GLY A 85 PRO A 175 TYR A 224
SITE 1 AC6 5 TYR A 35 SER A 90 LYS A 93 HOH A 610
SITE 2 AC6 5 HOH A 839
SITE 1 AC7 3 ASN A 166 GLY A 194 HOH A 749
SITE 1 AC8 5 HIS A 102 ALA A 105 PRO A 306 HOH A 618
SITE 2 AC8 5 HOH A 827
CRYST1 82.838 82.838 247.556 90.00 90.00 120.00 P 65 2 2 12
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 0.012072 0.006970 0.000000 0.00000
SCALE2 0.000000 0.013939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004039 0.00000
TER 2540 LYS A 324
MASTER 385 0 8 13 11 0 14 6 2891 1 53 26
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