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HEADER HYDROLASE 09-JUN-23 8PC7
TITLE STRUCTURE OF ESTER-HYDROLASE EH3 FROM THE METAGENOME OF MARINE
TITLE 2 SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY) COMPLEXED WITH A
TITLE 3 DERIVATIVE OF BIPYRIDINE PHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1211845;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PBXNH3
KEYWDS ESTER HYDROLASE, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 19-JUL-23 8PC7 0
JRNL AUTH L.FERNANDEZ-LOPEZ,I.CEA-RAMA,J.ALVAREZ-MALMAGRO,
JRNL AUTH 2 A.K.RESSMANN,J.L.GONZALEZ-ALFONSO,C.COSCOLIN,P.SHAHGALDIAN,
JRNL AUTH 3 F.J.PLOU,J.MODREGGER,M.PITA,J.SANZ-APARICIO,M.FERRER
JRNL TITL TRANSFORMING AN ESTERASE INTO AN ENANTIOSELECTIVE
JRNL TITL 2 CATECHOLASE THROUGH BIOCONJUGATION OF A VERSATILE
JRNL TITL 3 METAL-CHELATING INHIBITOR.
JRNL REF CHEM.COMMUN.(CAMB.) 2023
JRNL REFN ESSN 1364-548X
JRNL PMID 37376994
JRNL DOI 10.1039/D3CC01946B
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54940
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2927
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4030
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 228
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 127
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 25.04000
REMARK 3 B22 (A**2) : -5.38000
REMARK 3 B33 (A**2) : -19.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.31000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.057
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.229
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.650
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.898
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10508 ; 0.005 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 9892 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14218 ; 1.440 ; 1.654
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22823 ; 1.193 ; 1.593
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1336 ; 6.888 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 526 ;34.617 ;23.384
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1724 ;16.463 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;20.604 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1370 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12074 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2322 ; 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): 5365 ; 1.829 ; 4.483
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5363 ; 1.829 ; 4.483
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6694 ; 3.039 ; 6.720
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6694 ; 3.039 ; 6.720
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5143 ; 1.441 ; 4.623
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5144 ; 1.441 ; 4.623
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7525 ; 2.411 ; 6.884
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11626 ; 5.449 ;53.848
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11625 ; 5.447 ;53.853
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A B 10597 0.08 0.05
REMARK 3 2 A C 10565 0.09 0.05
REMARK 3 3 A D 10619 0.08 0.05
REMARK 3 4 B C 10624 0.07 0.05
REMARK 3 5 B D 10651 0.06 0.05
REMARK 3 6 C D 10608 0.07 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 8PC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1292131051.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979181
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL-CUT, CRYOCOOLED
REMARK 200 OPTICS : KB FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57906
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 47.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.04
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PLAQUE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG3350, 0.1M BIS-TRIS PH 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 94.69500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -56.75500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 56.75500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 LEU A -7
REMARK 465 GLU A -6
REMARK 465 VAL A -5
REMARK 465 LEU A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 PRO A 0
REMARK 465 SER A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 SER A 6
REMARK 465 LEU A 7
REMARK 465 ASN A 8
REMARK 465 MET A 28
REMARK 465 MET A 29
REMARK 465 GLU A 30
REMARK 465 GLY A 348
REMARK 465 ALA A 349
REMARK 465 MET B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 LEU B -7
REMARK 465 GLU B -6
REMARK 465 VAL B -5
REMARK 465 LEU B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 SER B 1
REMARK 465 PRO B 2
REMARK 465 ASP B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 SER B 6
REMARK 465 LEU B 7
REMARK 465 ASN B 8
REMARK 465 MET B 28
REMARK 465 MET B 29
REMARK 465 GLU B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 GLY B 348
REMARK 465 ALA B 349
REMARK 465 MET C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 LEU C -7
REMARK 465 GLU C -6
REMARK 465 VAL C -5
REMARK 465 LEU C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 GLY C -1
REMARK 465 PRO C 0
REMARK 465 SER C 1
REMARK 465 PRO C 2
REMARK 465 ASP C 3
REMARK 465 THR C 4
REMARK 465 THR C 5
REMARK 465 SER C 6
REMARK 465 LEU C 7
REMARK 465 ASN C 8
REMARK 465 ILE C 9
REMARK 465 GLY C 348
REMARK 465 ALA C 349
REMARK 465 MET D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 LEU D -7
REMARK 465 GLU D -6
REMARK 465 VAL D -5
REMARK 465 LEU D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 GLY D -1
REMARK 465 PRO D 0
REMARK 465 SER D 1
REMARK 465 PRO D 2
REMARK 465 ASP D 3
REMARK 465 THR D 4
REMARK 465 THR D 5
REMARK 465 SER D 6
REMARK 465 LEU D 7
REMARK 465 ASN D 8
REMARK 465 MET D 28
REMARK 465 MET D 29
REMARK 465 GLU D 30
REMARK 465 GLN D 31
REMARK 465 GLY D 348
REMARK 465 ALA D 349
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 SER A 192 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 SER C 192 N - CA - CB ANGL. DEV. = -9.7 DEGREES
REMARK 500 SER D 192 N - CA - CB ANGL. DEV. = -9.2 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 ALA A 10 33.05 -89.23
REMARK 500 PHE A 34 -48.46 -132.15
REMARK 500 GLN A 35 -16.22 76.92
REMARK 500 MET A 115 -53.86 -124.99
REMARK 500 MET A 117 157.01 80.97
REMARK 500 ASN A 145 -179.15 -66.34
REMARK 500 LEU A 147 -68.20 -133.62
REMARK 500 PRO A 157 -166.09 -75.59
REMARK 500 PRO A 159 39.95 -88.60
REMARK 500 SER A 192 -129.31 64.06
REMARK 500 CYS A 221 59.97 26.11
REMARK 500 TYR A 223 79.39 -112.13
REMARK 500 MET A 243 -45.89 62.36
REMARK 500 HIS A 321 124.64 -38.33
REMARK 500 ALA A 322 19.83 52.86
REMARK 500 ALA B 25 40.49 -98.02
REMARK 500 MET B 115 -50.66 -129.24
REMARK 500 MET B 117 156.98 80.98
REMARK 500 ASN B 145 -176.49 -69.86
REMARK 500 LEU B 147 -70.59 -129.98
REMARK 500 PRO B 157 -167.04 -74.41
REMARK 500 PRO B 159 38.57 -88.26
REMARK 500 SER B 192 -130.38 67.61
REMARK 500 CYS B 221 60.35 25.93
REMARK 500 MET B 243 -47.10 62.94
REMARK 500 HIS B 321 125.01 -37.00
REMARK 500 ALA B 322 17.98 53.41
REMARK 500 ALA C 25 41.27 -97.62
REMARK 500 PRO C 27 96.62 -68.03
REMARK 500 GLN C 32 -134.95 47.12
REMARK 500 ASP C 61 -6.40 -59.20
REMARK 500 MET C 115 -54.34 -126.78
REMARK 500 MET C 117 156.93 80.63
REMARK 500 LEU C 147 -68.86 -129.30
REMARK 500 PRO C 157 -164.82 -78.77
REMARK 500 PRO C 159 39.66 -88.92
REMARK 500 ALA C 160 -70.30 -67.05
REMARK 500 SER C 192 -127.89 63.60
REMARK 500 CYS C 221 60.25 26.58
REMARK 500 TYR C 223 78.95 -111.57
REMARK 500 MET C 243 -46.37 63.38
REMARK 500 HIS C 321 125.48 -36.53
REMARK 500 ALA C 322 18.29 52.75
REMARK 500 MET D 115 -52.10 -126.80
REMARK 500 MET D 117 156.29 80.38
REMARK 500 LEU D 147 -71.74 -133.13
REMARK 500 PRO D 157 -165.39 -76.93
REMARK 500 PRO D 159 38.80 -88.29
REMARK 500 SER D 192 -129.26 64.19
REMARK 500 CYS D 221 60.84 25.63
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6SXP RELATED DB: PDB
REMARK 900 RELATED ID: 6SYL RELATED DB: PDB
REMARK 900 RELATED ID: 6SXY RELATED DB: PDB
REMARK 900 RELATED ID: 6SYA RELATED DB: PDB
DBREF1 8PC7 A 2 348 UNP A0A2K8JN75_9BACT
DBREF2 8PC7 A A0A2K8JN75 2 348
DBREF1 8PC7 B 2 348 UNP A0A2K8JN75_9BACT
DBREF2 8PC7 B A0A2K8JN75 2 348
DBREF1 8PC7 C 2 348 UNP A0A2K8JN75_9BACT
DBREF2 8PC7 C A0A2K8JN75 2 348
DBREF1 8PC7 D 2 348 UNP A0A2K8JN75_9BACT
DBREF2 8PC7 D A0A2K8JN75 2 348
SEQADV 8PC7 MET A -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 8PC7 HIS A -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS A -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU A -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLU A -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 VAL A -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU A -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PHE A -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLN A -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLY A -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PRO A 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 SER A 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 ALA A 349 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 MET B -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 8PC7 HIS B -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS B -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU B -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLU B -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 VAL B -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU B -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PHE B -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLN B -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLY B -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PRO B 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 SER B 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 ALA B 349 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 MET C -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 8PC7 HIS C -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS C -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU C -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLU C -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 VAL C -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU C -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PHE C -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLN C -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLY C -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PRO C 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 SER C 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 ALA C 349 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 MET D -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 8PC7 HIS D -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 HIS D -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU D -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLU D -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 VAL D -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 LEU D -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PHE D -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLN D -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 GLY D -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 PRO D 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 SER D 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 8PC7 ALA D 349 UNP A0A2K8JN7 EXPRESSION TAG
SEQRES 1 A 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 A 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 A 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 A 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 A 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 A 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 A 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 A 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 A 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 A 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 A 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 A 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 A 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 A 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 A 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 A 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 A 368 GLY GLU SER GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 A 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 A 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 A 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 A 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 A 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 A 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 A 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 A 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 A 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 A 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 A 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 A 368 LYS GLY GLY ALA
SEQRES 1 B 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 B 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 B 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 B 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 B 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 B 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 B 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 B 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 B 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 B 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 B 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 B 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 B 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 B 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 B 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 B 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 B 368 GLY GLU SER GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 B 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 B 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 B 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 B 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 B 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 B 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 B 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 B 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 B 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 B 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 B 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 B 368 LYS GLY GLY ALA
SEQRES 1 C 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 C 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 C 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 C 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 C 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 C 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 C 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 C 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 C 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 C 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 C 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 C 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 C 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 C 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 C 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 C 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 C 368 GLY GLU SER GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 C 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 C 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 C 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 C 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 C 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 C 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 C 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 C 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 C 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 C 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 C 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 C 368 LYS GLY GLY ALA
SEQRES 1 D 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 D 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 D 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 D 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 D 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 D 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 D 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 D 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 D 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 D 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 D 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 D 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 D 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 D 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 D 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 D 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 D 368 GLY GLU SER GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 D 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 D 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 D 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 D 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 D 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 D 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 D 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 D 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 D 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 D 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 D 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 D 368 LYS GLY GLY ALA
HET PEG A 401 7
HET ZK8 A 402 22
HET PEG B 401 7
HET ZK8 B 402 22
HET PEG C 401 7
HET GOL C 402 6
HET GOL C 403 6
HET ZK8 C 404 22
HET GOL D 401 6
HET ZK8 D 402 22
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ZK8 HEXYL-[2-(3-OXIDANYLPYRIDIN-2-YL)PYRIDIN-3-YL]OXY-
HETNAM 2 ZK8 PHOSPHINIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 PEG 3(C4 H10 O3)
FORMUL 6 ZK8 4(C16 H21 N2 O4 P)
FORMUL 10 GOL 3(C3 H8 O3)
FORMUL 15 HOH *122(H2 O)
HELIX 1 AA1 ASP A 16 ALA A 25 1 10
HELIX 2 AA2 THR A 36 ALA A 44 1 9
HELIX 3 AA3 GLU A 48 ASP A 61 1 14
HELIX 4 AA4 GLY A 111 MET A 115 5 5
HELIX 5 AA5 TYR A 121 ASN A 133 1 13
HELIX 6 AA6 PRO A 159 ASN A 175 1 17
HELIX 7 AA7 ASN A 175 SER A 180 1 6
HELIX 8 AA8 SER A 192 GLN A 207 1 16
HELIX 9 AA9 ASP A 208 GLY A 209 5 2
HELIX 10 AB1 ASN A 210 VAL A 214 5 5
HELIX 11 AB2 PRO A 234 ASN A 239 1 6
HELIX 12 AB3 ASN A 249 GLY A 256 1 8
HELIX 13 AB4 GLY A 256 ALA A 262 1 7
HELIX 14 AB5 TRP A 268 ALA A 272 5 5
HELIX 15 AB6 SER A 273 GLN A 278 1 6
HELIX 16 AB7 LEU A 293 ALA A 307 1 15
HELIX 17 AB8 ALA A 322 PHE A 326 5 5
HELIX 18 AB9 ILE A 330 LYS A 346 1 17
HELIX 19 AC1 ASP B 16 ALA B 25 1 10
HELIX 20 AC2 THR B 36 ASN B 45 1 10
HELIX 21 AC3 GLU B 48 ASP B 61 1 14
HELIX 22 AC4 GLY B 111 MET B 115 5 5
HELIX 23 AC5 TYR B 121 ASN B 133 1 13
HELIX 24 AC6 PRO B 159 ASN B 175 1 17
HELIX 25 AC7 ASN B 175 SER B 180 1 6
HELIX 26 AC8 SER B 192 GLN B 207 1 16
HELIX 27 AC9 ASP B 208 GLY B 209 5 2
HELIX 28 AD1 ASN B 210 VAL B 214 5 5
HELIX 29 AD2 PRO B 234 ASN B 239 1 6
HELIX 30 AD3 ASN B 249 GLY B 256 1 8
HELIX 31 AD4 GLY B 256 ALA B 262 1 7
HELIX 32 AD5 TRP B 268 ALA B 272 5 5
HELIX 33 AD6 SER B 273 GLN B 278 1 6
HELIX 34 AD7 LEU B 293 ALA B 307 1 15
HELIX 35 AD8 ALA B 322 PHE B 326 5 5
HELIX 36 AD9 ILE B 330 LYS B 346 1 17
HELIX 37 AE1 ASP C 16 ALA C 25 1 10
HELIX 38 AE2 THR C 36 ASN C 45 1 10
HELIX 39 AE3 GLU C 48 ASP C 61 1 14
HELIX 40 AE4 GLY C 111 MET C 115 5 5
HELIX 41 AE5 TYR C 121 ASN C 133 1 13
HELIX 42 AE6 PRO C 159 ASN C 175 1 17
HELIX 43 AE7 ASN C 175 SER C 180 1 6
HELIX 44 AE8 SER C 192 GLN C 207 1 16
HELIX 45 AE9 ASP C 208 GLY C 209 5 2
HELIX 46 AF1 ASN C 210 VAL C 214 5 5
HELIX 47 AF2 PRO C 234 ASN C 239 1 6
HELIX 48 AF3 ASN C 249 GLY C 256 1 8
HELIX 49 AF4 GLY C 256 ALA C 262 1 7
HELIX 50 AF5 TRP C 268 ALA C 272 5 5
HELIX 51 AF6 SER C 273 GLN C 278 1 6
HELIX 52 AF7 LEU C 293 ALA C 307 1 15
HELIX 53 AF8 ALA C 322 PHE C 326 5 5
HELIX 54 AF9 ILE C 330 LYS C 346 1 17
HELIX 55 AG1 ASP D 16 ALA D 24 1 9
HELIX 56 AG2 THR D 36 ASN D 45 1 10
HELIX 57 AG3 GLU D 48 ASP D 61 1 14
HELIX 58 AG4 GLY D 111 MET D 115 5 5
HELIX 59 AG5 TYR D 121 ASN D 133 1 13
HELIX 60 AG6 PRO D 159 ASN D 175 1 17
HELIX 61 AG7 ASN D 175 SER D 180 1 6
HELIX 62 AG8 SER D 192 GLN D 207 1 16
HELIX 63 AG9 ASP D 208 GLY D 209 5 2
HELIX 64 AH1 ASN D 210 VAL D 214 5 5
HELIX 65 AH2 PRO D 234 ASN D 239 1 6
HELIX 66 AH3 ASN D 249 GLY D 256 1 8
HELIX 67 AH4 GLY D 256 ALA D 262 1 7
HELIX 68 AH5 TRP D 268 ALA D 272 5 5
HELIX 69 AH6 SER D 273 GLN D 278 1 6
HELIX 70 AH7 LEU D 293 ALA D 307 1 15
HELIX 71 AH8 ALA D 322 PHE D 326 5 5
HELIX 72 AH9 ILE D 330 LYS D 346 1 17
SHEET 1 AA116 LEU A 74 SER A 83 0
SHEET 2 AA116 ASN A 88 PRO A 97 -1 O PHE A 94 N SER A 77
SHEET 3 AA116 ALA A 137 VAL A 141 -1 O VAL A 138 N ILE A 95
SHEET 4 AA116 VAL A 103 ILE A 109 1 N VAL A 106 O ALA A 137
SHEET 5 AA116 ILE A 181 GLU A 191 1 O ALA A 189 N ILE A 109
SHEET 6 AA116 LEU A 217 LEU A 220 1 O LEU A 220 N GLY A 190
SHEET 7 AA116 THR A 283 ASN A 288 1 O VAL A 284 N LEU A 217
SHEET 8 AA116 ALA A 311 VAL A 316 1 O ARG A 312 N ILE A 285
SHEET 9 AA116 ALA B 311 MET B 317 -1 O GLN B 315 N GLN A 315
SHEET 10 AA116 THR B 283 ASN B 288 1 N VAL B 287 O ARG B 314
SHEET 11 AA116 GLY B 216 LEU B 220 1 N LEU B 217 O VAL B 284
SHEET 12 AA116 ILE B 181 GLU B 191 1 N GLY B 190 O LEU B 220
SHEET 13 AA116 VAL B 103 ILE B 109 1 N ILE B 109 O ALA B 189
SHEET 14 AA116 ALA B 137 VAL B 141 1 O ALA B 137 N VAL B 106
SHEET 15 AA116 ASN B 88 PRO B 97 -1 N ILE B 95 O VAL B 138
SHEET 16 AA116 LEU B 74 SER B 83 -1 N SER B 77 O PHE B 94
SHEET 1 AA216 LEU C 74 SER C 83 0
SHEET 2 AA216 ASN C 88 PRO C 97 -1 O PHE C 94 N SER C 77
SHEET 3 AA216 ALA C 137 VAL C 141 -1 O VAL C 138 N ILE C 95
SHEET 4 AA216 VAL C 103 ILE C 109 1 N VAL C 106 O ALA C 137
SHEET 5 AA216 ILE C 181 GLU C 191 1 O ALA C 189 N ILE C 109
SHEET 6 AA216 GLY C 216 LEU C 220 1 O LEU C 220 N GLY C 190
SHEET 7 AA216 THR C 283 ASN C 288 1 O VAL C 284 N ALA C 219
SHEET 8 AA216 ALA C 311 VAL C 316 1 O ARG C 314 N VAL C 287
SHEET 9 AA216 ALA D 311 VAL D 316 -1 O GLN D 315 N GLN C 315
SHEET 10 AA216 THR D 283 ASN D 288 1 N ILE D 285 O ARG D 312
SHEET 11 AA216 GLY D 216 LEU D 220 1 N LEU D 217 O VAL D 284
SHEET 12 AA216 ILE D 181 GLU D 191 1 N GLY D 190 O LEU D 220
SHEET 13 AA216 VAL D 103 ILE D 109 1 N ILE D 109 O ALA D 189
SHEET 14 AA216 ALA D 137 VAL D 141 1 O ALA D 137 N VAL D 106
SHEET 15 AA216 ASN D 88 PRO D 97 -1 N ILE D 95 O VAL D 138
SHEET 16 AA216 LEU D 74 SER D 83 -1 N SER D 77 O PHE D 94
LINK OG SER A 192 P01 ZK8 A 402 1555 1555 1.63
LINK OG SER B 192 P01 ZK8 B 402 1555 1555 1.63
LINK OG SER C 192 P01 ZK8 C 404 1555 1555 1.66
LINK OG SER D 192 P01 ZK8 D 402 1555 1555 1.63
CISPEP 1 SER A 84 PRO A 85 0 -4.62
CISPEP 2 PHE A 158 PRO A 159 0 -20.30
CISPEP 3 TRP A 228 PRO A 229 0 -6.30
CISPEP 4 SER B 84 PRO B 85 0 -13.42
CISPEP 5 PHE B 158 PRO B 159 0 -20.08
CISPEP 6 TRP B 228 PRO B 229 0 -6.85
CISPEP 7 SER C 84 PRO C 85 0 -12.60
CISPEP 8 PHE C 158 PRO C 159 0 -19.47
CISPEP 9 TRP C 228 PRO C 229 0 -6.42
CISPEP 10 SER D 84 PRO D 85 0 -13.31
CISPEP 11 PHE D 158 PRO D 159 0 -20.51
CISPEP 12 TRP D 228 PRO D 229 0 -7.02
CRYST1 56.755 189.390 75.954 90.00 111.93 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017620 0.000000 0.007092 0.00000
SCALE2 0.000000 0.005280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014192 0.00000
TER 2548 GLY A 347
TER 5078 GLY B 347
TER 7643 GLY C 347
TER 10182 GLY D 347
MASTER 491 0 10 72 32 0 0 610427 4 131 116
END |