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HEADER HYDROLASE 23-OCT-14 4RNC
TITLE CRYSTAL STRUCTURE OF AN ESTERASE RHEST1 FROM RHODOCOCCUS SP. ECU1013
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 STRAIN: ECU1013 ISOLATED FROM SOIL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DOU,X.D.KONG,J.H.XU,J.ZHOU
REVDAT 1 28-OCT-15 4RNC 0
JRNL AUTH Z.J.LUAN,F.L LI,S.DOU,Q.CHEN,X.D.KONG,J.ZHOU,H.L.YU,J.H.XU
JRNL TITL SUBSTRATE CHANNEL EVOLUTION OF AN ESTERASE FOR THE SYNTHESIS
JRNL TITL 2 OF CILASTATIN
JRNL REF CATALYSIS SCIENCE AND V. 5 2622 2015
JRNL REF 2 TECHNOLOGY
JRNL REFN ISSN 2044-4753
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 52476
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2674
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3591
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 211
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6063
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 597
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.65000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : 0.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.279
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6195 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5811 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8430 ; 1.692 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13317 ; 0.861 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 828 ; 6.412 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;32.032 ;23.253
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 900 ;14.712 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;19.767 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 948 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7224 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1407 ; 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): 3321 ; 2.777 ; 3.243
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3320 ; 2.777 ; 3.241
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4146 ; 3.727 ; 4.848
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): 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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4RNC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-14.
REMARK 100 THE RCSB ID CODE IS RCSB087559.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52476
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.59400
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: SAD
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3 M NA/K PHOSPHATE, 0.1M TRIS PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 106.46300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.69150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.46300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.69150
REMARK 290 SMTRY3 4 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: 3140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 -21.11221
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 74.50968
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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER 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 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 LEU A 282
REMARK 465 GLU A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER 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 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 LYS B 276
REMARK 465 LEU B 277
REMARK 465 ALA B 278
REMARK 465 GLY B 279
REMARK 465 ALA B 280
REMARK 465 ALA B 281
REMARK 465 LEU B 282
REMARK 465 GLU B 283
REMARK 465 HIS B 284
REMARK 465 HIS B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER 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 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 LEU C -7
REMARK 465 VAL C -6
REMARK 465 PRO C -5
REMARK 465 ARG C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
REMARK 465 LYS C 276
REMARK 465 LEU C 277
REMARK 465 ALA C 278
REMARK 465 GLY C 279
REMARK 465 ALA C 280
REMARK 465 ALA C 281
REMARK 465 LEU C 282
REMARK 465 GLU C 283
REMARK 465 HIS C 284
REMARK 465 HIS C 285
REMARK 465 HIS C 286
REMARK 465 HIS C 287
REMARK 465 HIS C 288
REMARK 465 HIS C 289
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 OG SER B 101 P PO4 B 301 1.68
REMARK 500 OG SER A 101 P PO4 A 301 1.71
REMARK 500 OG SER C 101 P PO4 C 301 1.85
REMARK 500 O HOH A 435 O HOH A 620 2.05
REMARK 500 O HOH C 403 O HOH C 498 2.07
REMARK 500 NH1 ARG A 211 O HOH A 507 2.10
REMARK 500 O HOH C 403 O HOH C 520 2.13
REMARK 500 O GLU B 89 O HOH B 519 2.14
REMARK 500 OD1 ASN A 21 O HOH A 461 2.15
REMARK 500 OH TYR B 187 O HOH B 482 2.15
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 196 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 196 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 211 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 74 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 196 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 196 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 211 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 211 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 192 NE - CZ - NH1 ANGL. DEV. = 3.1 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 GLN A 35 -156.40 -122.08
REMARK 500 SER A 101 -115.22 52.02
REMARK 500 LYS A 242 41.36 -102.23
REMARK 500 ASN A 252 -142.02 -92.44
REMARK 500 ASP A 259 78.84 -151.34
REMARK 500 GLN B 35 -160.11 -122.71
REMARK 500 SER B 101 -108.64 49.26
REMARK 500 PRO B 173 -73.81 -41.57
REMARK 500 LYS B 242 50.55 -102.44
REMARK 500 ASN B 252 -136.81 -93.82
REMARK 500 LEU B 274 44.14 -66.06
REMARK 500 GLN C 35 -160.60 -115.95
REMARK 500 SER C 101 -111.54 52.62
REMARK 500 ARG C 145 41.13 -107.61
REMARK 500 PRO C 149 -72.78 -55.91
REMARK 500 LYS C 242 47.59 -109.02
REMARK 500 ASN C 252 -138.68 -95.89
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 C 143 MET C 144 -148.93
REMARK 500 ARG C 145 SER C 146 141.38
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 532 DISTANCE = 5.99 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PO4 A 301
REMARK 610 PO4 B 301
REMARK 610 PO4 C 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 301
DBREF 4RNC A -20 289 PDB 4RNC 4RNC -20 289
DBREF 4RNC B -20 289 PDB 4RNC 4RNC -20 289
DBREF 4RNC C -20 289 PDB 4RNC 4RNC -20 289
SEQRES 1 A 310 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 310 LEU VAL PRO ARG GLY SER HIS MET MET SER ILE ARG GLU
SEQRES 3 A 310 ALA VAL SER VAL ASP GLY THR SER ILE VAL TYR ARG VAL
SEQRES 4 A 310 THR GLY ASN SER ALA GLY THR PRO LEU VAL LEU LEU HIS
SEQRES 5 A 310 GLY TRP ALA GLN SER SER GLN CYS TRP GLY GLU GLN VAL
SEQRES 6 A 310 LEU ALA ASP LEU ALA ALA ASP TYR ARG LEU ILE ALA VAL
SEQRES 7 A 310 ASP LEU ARG GLY HIS GLY TYR SER ASP ALA PRO GLU SER
SEQRES 8 A 310 GLY TYR ASP ASP SER ALA ASN TRP ALA GLY ASP VAL ALA
SEQRES 9 A 310 ALA VAL LEU ALA ALA GLU GLY VAL THR GLU ASN ALA ILE
SEQRES 10 A 310 LEU LEU GLY TRP SER TYR GLY GLY LEU VAL ILE CYS ASP
SEQRES 11 A 310 TYR LEU ALA ALA HIS GLY THR GLY ALA VAL ALA GLY ALA
SEQRES 12 A 310 VAL LEU VAL GLY ALA ILE THR SER ILE GLY ARG GLY GLU
SEQRES 13 A 310 LYS GLY GLY LYS VAL GLY SER ALA MET ARG SER ALA VAL
SEQRES 14 A 310 PRO GLY ALA MET SER GLU ASP PRO ARG GLU ALA ILE ARG
SEQRES 15 A 310 ALA LEU GLY ALA PHE GLY ASN ALA LEU THR GLY PRO PRO
SEQRES 16 A 310 GLU GLY LYS GLY ALA ALA SER GLN ALA LEU PHE GLY TYR
SEQRES 17 A 310 SER LEU SER THR ARG PRO ARG VAL ARG ALA ALA LEU PHE
SEQRES 18 A 310 ASN ARG ALA VAL GLY HIS ASP GLU LEU LEU ARG ASN LEU
SEQRES 19 A 310 ASP ILE PRO VAL LEU VAL LEU HIS GLY THR ASP ASP SER
SEQRES 20 A 310 VAL VAL ASP VAL SER ALA GLY LYS HIS ALA GLU GLU LEU
SEQRES 21 A 310 ILE PRO LYS SER GLN ALA SER TYR TRP VAL GLY CYS ASN
SEQRES 22 A 310 HIS GLY PRO PHE VAL GLU ASP PRO THR ARG PHE VAL SER
SEQRES 23 A 310 GLU VAL ARG THR PHE ILE SER SER LEU GLY LYS LEU ALA
SEQRES 24 A 310 GLY ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 310 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 310 LEU VAL PRO ARG GLY SER HIS MET MET SER ILE ARG GLU
SEQRES 3 B 310 ALA VAL SER VAL ASP GLY THR SER ILE VAL TYR ARG VAL
SEQRES 4 B 310 THR GLY ASN SER ALA GLY THR PRO LEU VAL LEU LEU HIS
SEQRES 5 B 310 GLY TRP ALA GLN SER SER GLN CYS TRP GLY GLU GLN VAL
SEQRES 6 B 310 LEU ALA ASP LEU ALA ALA ASP TYR ARG LEU ILE ALA VAL
SEQRES 7 B 310 ASP LEU ARG GLY HIS GLY TYR SER ASP ALA PRO GLU SER
SEQRES 8 B 310 GLY TYR ASP ASP SER ALA ASN TRP ALA GLY ASP VAL ALA
SEQRES 9 B 310 ALA VAL LEU ALA ALA GLU GLY VAL THR GLU ASN ALA ILE
SEQRES 10 B 310 LEU LEU GLY TRP SER TYR GLY GLY LEU VAL ILE CYS ASP
SEQRES 11 B 310 TYR LEU ALA ALA HIS GLY THR GLY ALA VAL ALA GLY ALA
SEQRES 12 B 310 VAL LEU VAL GLY ALA ILE THR SER ILE GLY ARG GLY GLU
SEQRES 13 B 310 LYS GLY GLY LYS VAL GLY SER ALA MET ARG SER ALA VAL
SEQRES 14 B 310 PRO GLY ALA MET SER GLU ASP PRO ARG GLU ALA ILE ARG
SEQRES 15 B 310 ALA LEU GLY ALA PHE GLY ASN ALA LEU THR GLY PRO PRO
SEQRES 16 B 310 GLU GLY LYS GLY ALA ALA SER GLN ALA LEU PHE GLY TYR
SEQRES 17 B 310 SER LEU SER THR ARG PRO ARG VAL ARG ALA ALA LEU PHE
SEQRES 18 B 310 ASN ARG ALA VAL GLY HIS ASP GLU LEU LEU ARG ASN LEU
SEQRES 19 B 310 ASP ILE PRO VAL LEU VAL LEU HIS GLY THR ASP ASP SER
SEQRES 20 B 310 VAL VAL ASP VAL SER ALA GLY LYS HIS ALA GLU GLU LEU
SEQRES 21 B 310 ILE PRO LYS SER GLN ALA SER TYR TRP VAL GLY CYS ASN
SEQRES 22 B 310 HIS GLY PRO PHE VAL GLU ASP PRO THR ARG PHE VAL SER
SEQRES 23 B 310 GLU VAL ARG THR PHE ILE SER SER LEU GLY LYS LEU ALA
SEQRES 24 B 310 GLY ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 310 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 310 LEU VAL PRO ARG GLY SER HIS MET MET SER ILE ARG GLU
SEQRES 3 C 310 ALA VAL SER VAL ASP GLY THR SER ILE VAL TYR ARG VAL
SEQRES 4 C 310 THR GLY ASN SER ALA GLY THR PRO LEU VAL LEU LEU HIS
SEQRES 5 C 310 GLY TRP ALA GLN SER SER GLN CYS TRP GLY GLU GLN VAL
SEQRES 6 C 310 LEU ALA ASP LEU ALA ALA ASP TYR ARG LEU ILE ALA VAL
SEQRES 7 C 310 ASP LEU ARG GLY HIS GLY TYR SER ASP ALA PRO GLU SER
SEQRES 8 C 310 GLY TYR ASP ASP SER ALA ASN TRP ALA GLY ASP VAL ALA
SEQRES 9 C 310 ALA VAL LEU ALA ALA GLU GLY VAL THR GLU ASN ALA ILE
SEQRES 10 C 310 LEU LEU GLY TRP SER TYR GLY GLY LEU VAL ILE CYS ASP
SEQRES 11 C 310 TYR LEU ALA ALA HIS GLY THR GLY ALA VAL ALA GLY ALA
SEQRES 12 C 310 VAL LEU VAL GLY ALA ILE THR SER ILE GLY ARG GLY GLU
SEQRES 13 C 310 LYS GLY GLY LYS VAL GLY SER ALA MET ARG SER ALA VAL
SEQRES 14 C 310 PRO GLY ALA MET SER GLU ASP PRO ARG GLU ALA ILE ARG
SEQRES 15 C 310 ALA LEU GLY ALA PHE GLY ASN ALA LEU THR GLY PRO PRO
SEQRES 16 C 310 GLU GLY LYS GLY ALA ALA SER GLN ALA LEU PHE GLY TYR
SEQRES 17 C 310 SER LEU SER THR ARG PRO ARG VAL ARG ALA ALA LEU PHE
SEQRES 18 C 310 ASN ARG ALA VAL GLY HIS ASP GLU LEU LEU ARG ASN LEU
SEQRES 19 C 310 ASP ILE PRO VAL LEU VAL LEU HIS GLY THR ASP ASP SER
SEQRES 20 C 310 VAL VAL ASP VAL SER ALA GLY LYS HIS ALA GLU GLU LEU
SEQRES 21 C 310 ILE PRO LYS SER GLN ALA SER TYR TRP VAL GLY CYS ASN
SEQRES 22 C 310 HIS GLY PRO PHE VAL GLU ASP PRO THR ARG PHE VAL SER
SEQRES 23 C 310 GLU VAL ARG THR PHE ILE SER SER LEU GLY LYS LEU ALA
SEQRES 24 C 310 GLY ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET PO4 A 301 4
HET PO4 B 301 4
HET PO4 C 301 4
HETNAM PO4 PHOSPHATE ION
FORMUL 4 PO4 3(O4 P 3-)
FORMUL 7 HOH *597(H2 O)
HELIX 1 1 GLY A 41 ALA A 50 1 10
HELIX 2 2 ASP A 74 GLU A 89 1 16
HELIX 3 3 TYR A 102 GLY A 115 1 14
HELIX 4 4 GLU A 135 LYS A 139 5 5
HELIX 5 5 GLY A 141 VAL A 148 1 8
HELIX 6 6 PRO A 149 SER A 153 5 5
HELIX 7 7 ASP A 155 ALA A 165 1 11
HELIX 8 8 LYS A 177 SER A 190 1 14
HELIX 9 9 ARG A 192 LEU A 199 1 8
HELIX 10 10 HIS A 206 LEU A 213 1 8
HELIX 11 11 ASP A 229 ILE A 240 1 12
HELIX 12 12 GLY A 254 ASP A 259 1 6
HELIX 13 13 ASP A 259 SER A 273 1 15
HELIX 14 14 LYS A 276 ALA A 281 1 6
HELIX 15 15 SER B 36 TRP B 40 5 5
HELIX 16 16 GLY B 41 TYR B 52 1 12
HELIX 17 17 ASP B 74 GLU B 89 1 16
HELIX 18 18 TYR B 102 GLY B 115 1 14
HELIX 19 19 GLU B 135 LYS B 139 5 5
HELIX 20 20 GLY B 141 ALA B 147 1 7
HELIX 21 21 PRO B 149 SER B 153 5 5
HELIX 22 22 ASP B 155 GLY B 172 1 18
HELIX 23 23 LYS B 177 THR B 191 1 15
HELIX 24 24 ARG B 192 ASN B 201 1 10
HELIX 25 25 HIS B 206 ARG B 211 1 6
HELIX 26 26 ASP B 229 ILE B 240 1 12
HELIX 27 27 GLY B 254 ASP B 259 1 6
HELIX 28 28 ASP B 259 LEU B 274 1 16
HELIX 29 29 GLY C 41 TYR C 52 1 12
HELIX 30 30 ASP C 74 GLU C 89 1 16
HELIX 31 31 TYR C 102 GLY C 115 1 14
HELIX 32 32 GLU C 135 LYS C 139 5 5
HELIX 33 33 ALA C 143 VAL C 148 1 6
HELIX 34 34 PRO C 149 SER C 153 5 5
HELIX 35 35 ASP C 155 GLY C 172 1 18
HELIX 36 36 LYS C 177 SER C 190 1 14
HELIX 37 37 ARG C 192 LEU C 199 1 8
HELIX 38 38 HIS C 206 ARG C 211 1 6
HELIX 39 39 ASP C 229 ILE C 240 1 12
HELIX 40 40 GLY C 254 ASP C 259 1 6
HELIX 41 41 ASP C 259 LEU C 274 1 16
SHEET 1 A 8 ILE A 3 VAL A 7 0
SHEET 2 A 8 SER A 13 GLY A 20 -1 O ILE A 14 N ALA A 6
SHEET 3 A 8 TYR A 52 VAL A 57 -1 O ALA A 56 N ARG A 17
SHEET 4 A 8 THR A 25 LEU A 30 1 N LEU A 29 O ILE A 55
SHEET 5 A 8 ALA A 95 TRP A 100 1 O LEU A 98 N LEU A 30
SHEET 6 A 8 VAL A 119 VAL A 125 1 O VAL A 125 N GLY A 99
SHEET 7 A 8 VAL A 217 GLY A 222 1 O LEU A 218 N LEU A 124
SHEET 8 A 8 SER A 243 TRP A 248 1 O GLN A 244 N VAL A 219
SHEET 1 B 8 ILE B 3 VAL B 7 0
SHEET 2 B 8 SER B 13 THR B 19 -1 O ILE B 14 N ALA B 6
SHEET 3 B 8 ARG B 53 VAL B 57 -1 O ALA B 56 N ARG B 17
SHEET 4 B 8 PRO B 26 LEU B 30 1 N LEU B 29 O ILE B 55
SHEET 5 B 8 ALA B 95 TRP B 100 1 O ILE B 96 N VAL B 28
SHEET 6 B 8 VAL B 119 VAL B 125 1 O VAL B 125 N GLY B 99
SHEET 7 B 8 VAL B 217 GLY B 222 1 O LEU B 218 N LEU B 124
SHEET 8 B 8 SER B 243 TRP B 248 1 O GLN B 244 N VAL B 219
SHEET 1 C 8 ILE C 3 VAL C 7 0
SHEET 2 C 8 SER C 13 THR C 19 -1 O ILE C 14 N ALA C 6
SHEET 3 C 8 ARG C 53 VAL C 57 -1 O ALA C 56 N ARG C 17
SHEET 4 C 8 PRO C 26 LEU C 30 1 N LEU C 27 O ILE C 55
SHEET 5 C 8 ALA C 95 TRP C 100 1 O LEU C 98 N VAL C 28
SHEET 6 C 8 VAL C 119 VAL C 125 1 O VAL C 125 N GLY C 99
SHEET 7 C 8 VAL C 217 GLY C 222 1 O LEU C 218 N LEU C 124
SHEET 8 C 8 SER C 243 TRP C 248 1 O SER C 246 N VAL C 219
CISPEP 1 VAL A 148 PRO A 149 0 12.67
CISPEP 2 VAL B 148 PRO B 149 0 7.83
CISPEP 3 PRO B 173 PRO B 174 0 -15.49
SITE 1 AC1 6 TRP A 33 SER A 101 TYR A 102 ILE A 128
SITE 2 AC1 6 MET A 144 VAL A 227
SITE 1 AC2 6 TRP B 33 SER B 101 TYR B 102 ILE B 128
SITE 2 AC2 6 MET B 144 VAL B 227
SITE 1 AC3 5 GLY C 32 TRP C 33 SER C 101 TYR C 102
SITE 2 AC3 5 VAL C 227
CRYST1 212.926 45.383 77.443 90.00 105.82 90.00 C 1 2 1 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 0.004696 0.000000 0.001330 0.00000
SCALE2 0.000000 0.022035 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013421 0.00000
TER 2046 ALA A 281
TER 4056 GLY B 275
TER 6066 GLY C 275
MASTER 489 0 3 41 24 0 6 6 6672 3 12 72
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