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HEADER HYDROLASE 10-JUL-15 5CH3
TITLE E3 ALPHA-ESTERASE-7 CARBOXYLESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: GREEN BOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 GENE: LCAE7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, OP HYDROLASE, ORGANOPHOSPHATES, STRUCTURAL
KEYWDS 2 DYNAMICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.CORREY,P.MABBITT,C.J.JACKSON
REVDAT 1 15-JUN-16 5CH3 0
JRNL AUTH G.J.CORREY,P.D.CARR,T.MEIRELLES,P.D.MABBITT,N.J.FRASER,
JRNL AUTH 2 M.WEIK,C.J.JACKSON
JRNL TITL MAPPING THE ACCESSIBLE CONFORMATIONAL LANDSCAPE OF AN INSECT
JRNL TITL 2 CARBOXYLESTERASE USING CONFORMATIONAL ENSEMBLE ANALYSIS AND
JRNL TITL 3 KINETIC CRYSTALLOGRAPHY.
JRNL REF STRUCTURE 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27210287
JRNL DOI 10.1016/J.STR.2016.04.009
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 56138
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3001
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) : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4085
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4557
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.13000
REMARK 3 B22 (A**2) : -1.44000
REMARK 3 B33 (A**2) : -2.69000
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): 0.108
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.725
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4693 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4413 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6353 ; 1.841 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10193 ; 1.072 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 569 ; 6.444 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 221 ;35.176 ;24.253
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 827 ;14.541 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.359 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 677 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5291 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1090 ; 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): 2273 ; 2.884 ; 3.130
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2272 ; 2.882 ; 3.129
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2843 ; 3.754 ; 4.682
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2844 ; 3.755 ; 4.683
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2420 ; 3.842 ; 3.555
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2420 ; 3.841 ; 3.555
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3510 ; 5.676 ; 5.152
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5585 ; 6.910 ;25.738
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5516 ; 6.901 ;25.613
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 : 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 5CH3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211570.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-10
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56138
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 45.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 29.00
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 28.30
REMARK 200 R MERGE FOR SHELL (I) : 3.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4FNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 2K MME, 100MM SODIUM ACETATE
REMARK 280 PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
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+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
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 110.85750
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 110.85750
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 24.28700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.23600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.28700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.23600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 110.85750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.28700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.23600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 110.85750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.28700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.23600
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 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 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 1.000000 0.000000 0.000000 0.00000
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 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 792 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 MET A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 PHE A 3
REMARK 465 ASN A 4
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 OE1 GLU A 124 O HOH A 601 2.13
REMARK 500 OH TYR A 457 O HOH A 602 2.14
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 ASP A 93 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 445 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 445 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 461 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 486 NE - CZ - NH1 ANGL. DEV. = 3.4 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 218 -120.50 54.95
REMARK 500 CYS A 372 16.74 58.62
REMARK 500 PHE A 421 -61.40 -127.04
REMARK 500 HIS A 435 38.84 -149.63
REMARK 500 HIS A 471 132.85 -39.27
REMARK 500 THR A 472 -13.03 80.32
REMARK 500 SER A 542 -148.90 -130.99
REMARK 500 HIS A 566 47.89 -143.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CH5 RELATED DB: PDB
DBREF 5CH3 A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5CH3 MET A -6 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 HIS A -5 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 HIS A -4 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 HIS A -3 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 HIS A -2 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 HIS A -1 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 HIS A 0 UNP Q25252 EXPRESSION TAG
SEQADV 5CH3 ALA A 83 UNP Q25252 ASP 83 ENGINEERED MUTATION
SEQADV 5CH3 LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 5CH3 PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 5CH3 THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 5CH3 THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 5CH3 GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 5CH3 GLY A 554 UNP Q25252 ASP 554 ENGINEERED MUTATION
SEQRES 1 A 577 MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER
SEQRES 2 A 577 LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU
SEQRES 3 A 577 ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR
SEQRES 4 A 577 VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL
SEQRES 5 A 577 LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE
SEQRES 6 A 577 GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU
SEQRES 7 A 577 ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY
SEQRES 8 A 577 VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN
SEQRES 9 A 577 VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP
SEQRES 10 A 577 CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO
SEQRES 11 A 577 GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY
SEQRES 12 A 577 GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY
SEQRES 13 A 577 PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN
SEQRES 14 A 577 ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU
SEQRES 15 A 577 ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU
SEQRES 16 A 577 LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN
SEQRES 17 A 577 CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL
SEQRES 18 A 577 PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET
SEQRES 19 A 577 MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY
SEQRES 20 A 577 ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN
SEQRES 21 A 577 THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU
SEQRES 22 A 577 ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU
SEQRES 23 A 577 GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS
SEQRES 24 A 577 LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN
SEQRES 25 A 577 LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR
SEQRES 26 A 577 GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU
SEQRES 27 A 577 MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET
SEQRES 28 A 577 MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER
SEQRES 29 A 577 ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU
SEQRES 30 A 577 THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA
SEQRES 31 A 577 GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS
SEQRES 32 A 577 ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA
SEQRES 33 A 577 ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP
SEQRES 34 A 577 PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS
SEQRES 35 A 577 THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE
SEQRES 36 A 577 ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG
SEQRES 37 A 577 SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU
SEQRES 38 A 577 LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET
SEQRES 39 A 577 PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET
SEQRES 40 A 577 THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO
SEQRES 41 A 577 TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP
SEQRES 42 A 577 ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU
SEQRES 43 A 577 ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU
SEQRES 44 A 577 MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS
SEQRES 45 A 577 HIS ARG ASP LEU PHE
FORMUL 2 HOH *273(H2 O)
HELIX 1 AA1 SER A 6 LEU A 27 1 22
HELIX 2 AA2 VAL A 68 ARG A 72 5 5
HELIX 3 AA3 TYR A 152 LYS A 156 5 5
HELIX 4 AA4 LEU A 167 LEU A 173 1 7
HELIX 5 AA5 SER A 177 ASN A 181 5 5
HELIX 6 AA6 ASN A 185 CYS A 202 1 18
HELIX 7 AA7 ALA A 203 PHE A 205 5 3
HELIX 8 AA8 SER A 218 THR A 230 1 13
HELIX 9 AA9 GLU A 231 ARG A 234 5 4
HELIX 10 AB1 CYS A 249 ASN A 253 5 5
HELIX 11 AB2 HIS A 258 ALA A 267 1 10
HELIX 12 AB3 ASN A 274 ALA A 285 1 12
HELIX 13 AB4 LYS A 286 GLU A 294 1 9
HELIX 14 AB5 GLU A 295 VAL A 297 5 3
HELIX 15 AB6 THR A 299 ASN A 305 1 7
HELIX 16 AB7 HIS A 328 VAL A 333 1 6
HELIX 17 AB8 LYS A 334 ILE A 341 5 8
HELIX 18 AB9 TYR A 350 PHE A 354 5 5
HELIX 19 AC1 PHE A 355 MET A 362 1 8
HELIX 20 AC2 PRO A 363 THR A 371 5 9
HELIX 21 AC3 CYS A 372 VAL A 376 5 5
HELIX 22 AC4 ALA A 387 VAL A 402 1 16
HELIX 23 AC5 THR A 408 PHE A 421 1 14
HELIX 24 AC6 PHE A 421 ASN A 434 1 14
HELIX 25 AC7 PRO A 456 ARG A 461 1 6
HELIX 26 AC8 THR A 472 PHE A 478 5 7
HELIX 27 AC9 SER A 491 GLY A 511 1 21
HELIX 28 AD1 GLU A 552 MET A 562 1 11
HELIX 29 AD2 HIS A 566 PHE A 570 5 5
SHEET 1 AA1 3 THR A 28 ALA A 35 0
SHEET 2 AA1 3 LYS A 41 LEU A 48 -1 O VAL A 42 N ALA A 35
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 41
SHEET 1 AA212 THR A 28 ALA A 35 0
SHEET 2 AA212 LYS A 41 LEU A 48 -1 O VAL A 42 N ALA A 35
SHEET 3 AA212 SER A 54 PRO A 62 -1 O TYR A 55 N ARG A 47
SHEET 4 AA212 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
SHEET 5 AA212 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 AA212 ARG A 127 ILE A 133 1 N TYR A 132 O ILE A 161
SHEET 7 AA212 GLY A 207 GLU A 217 1 O THR A 213 N VAL A 131
SHEET 8 AA212 ARG A 239 MET A 243 1 O MET A 243 N GLY A 216
SHEET 9 AA212 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 AA212 VAL A 441 PHE A 446 1 O PHE A 446 N ASN A 347
SHEET 11 AA212 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 AA212 LEU A 545 ASP A 549 -1 O LYS A 546 N ASN A 540
SHEET 1 AA3 2 GLN A 97 VAL A 98 0
SHEET 2 AA3 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
CRYST1 48.574 100.472 221.715 90.00 90.00 90.00 C 2 2 21 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 0.020587 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004510 0.00000
TER 4576 PHE A 570
MASTER 352 0 0 29 17 0 0 6 4830 1 0 45
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