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HEADER HYDROLASE 07-NOV-12 4HVT
TITLE STRUCTURE OF A POST-PROLINE CLEAVING ENZYME FROM RICKETTSIA TYPHI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POST-PROLINE CLEAVING ENZYME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL TRUNCATION (UNP RESIDUES 19-720);
COMPND 5 SYNONYM: RITYA.17583.B;
COMPND 6 EC: 3.4.21.26;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RICKETTSIA TYPHI;
SOURCE 3 ORGANISM_TAXID: 257363;
SOURCE 4 STRAIN: ATCC VR-144 / WILMINGTON;
SOURCE 5 GENE: PPCE, RT0165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: RITYA.17583.B.B2
KEYWDS SSGCID, POST-PROLINE CLEAVING ENZYME, STRUCTURAL GENOMICS, SEATTLE
KEYWDS 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, POST-PROLINE
KEYWDS 3 CLEAVAGE PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 28-NOV-12 4HVT 0
JRNL AUTH SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 2 (SSGCID),J.ABENDROTH,B.SANKARAN,D.FOX III,T.E.EDWARDS,
JRNL AUTH 3 B.L.STAKER
JRNL TITL STRUCTURE OF A POST-PROLINE CLEAVING ENZYME FROM RICKETTSIA
JRNL TITL 2 TYPHI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 81804
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4322
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5994
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 331
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5510
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 746
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.79000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.54000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.886
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5739 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5324 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7804 ; 1.683 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12259 ; 0.850 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 712 ; 6.687 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 264 ;34.673 ;24.583
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 945 ;12.879 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;11.997 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 852 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6514 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1357 ; 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): 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 20 A 710
REMARK 3 RESIDUE RANGE : A 801 A 808
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7250 61.6720 16.0530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0536 T22: 0.0092
REMARK 3 T33: 0.0850 T12: 0.0113
REMARK 3 T13: -0.0666 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.4637 L22: 0.5290
REMARK 3 L33: 0.5823 L12: 0.0058
REMARK 3 L13: 0.2563 L23: -0.0524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0773 S12: -0.0259 S13: 0.0877
REMARK 3 S21: -0.0150 S22: 0.0270 S23: 0.0072
REMARK 3 S31: -0.0651 S32: -0.0668 S33: 0.0504
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: WITH TLS ADDED
REMARK 4
REMARK 4 4HVT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB075982.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-12; 17-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.5; 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : ALS; ROTATING ANODE
REMARK 200 BEAMLINE : 5.0.1; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774; 1.5418
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL, CYLINDRICALLY
REMARK 200 BENT, SI(220); RIGAKU VARIMAX
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R; RIGAKU SATURN
REMARK 200 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86126
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD, MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER_EP, PHASER_MR
REMARK 200 STARTING MODEL: AN INITIAL MODEL WAS OBTAINED FROM IODIDE SAD
REMARK 200 PHASING USING CRYSTAL 2 (P21). THE INITIAL MODEL WAS THEN USED AS
REMARK 200 SEARCH MODEL FOR C2 HIGH RESOLUTION DATA SET, CRYSTAL 1.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MICROLYIC MCSG1 SCREEN B10: 24% PEG
REMARK 280 4000, 20% GLYCEROL, 160MM MAGNESIUM CHLORIDE, 80MM TRIS:HCL PH
REMARK 280 8.5; RITYA17583BB2.PS01616 AT 26.6MG/ML, CRYO: EG; SG C2; FOR
REMARK 280 PHASING CRYSTAL 2 WAS USED SG P21, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K. MICROLYIC MCSG1 SCREEN C5: 20% PEG 3350, 200MM
REMARK 280 MAGNESIUM ACETATE; RITYA17583BB2.PS01616 AT 26.6MG/ML, FOR
REMARK 280 PHASING A CRYSTAL WAS SOAKED IN RESERVOIR + 20% EG WITH 2.5M
REMARK 280 SODIUM IODIDE (FINAL 500MM NAI) FOR 1 MINUTE, THIS SAMPLE IS FROM
REMARK 280 A DIFFERET SPACE GROUP (P21) THAN CRYSTAL 1, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 99.79500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.64000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 99.79500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.64000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A1386 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 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 MET A 9
REMARK 465 ALA A 10
REMARK 465 MET A 11
REMARK 465 GLU A 12
REMARK 465 ASP A 13
REMARK 465 ASN A 14
REMARK 465 ASN A 15
REMARK 465 LYS A 16
REMARK 465 GLN A 17
REMARK 465 ILE A 18
REMARK 465 PHE A 19
REMARK 465 ASN A 711
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 ASN A 20 CG OD1 ND2
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 VAL A 33 CG1 CG2
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 GLU A 37 CG CD OE1 OE2
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 LYS A 45 CG CD CE NZ
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 GLN A 54 CG CD OE1 NE2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 ASN A 111 CG OD1 ND2
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 ILE A 125 CG1 CG2 CD1
REMARK 470 LYS A 127 CG CD CE NZ
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 LYS A 170 CG CD CE NZ
REMARK 470 LYS A 206 CG CD CE NZ
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 SER A 314 OG
REMARK 470 ASN A 381 CG OD1 ND2
REMARK 470 LYS A 391 CG CD CE NZ
REMARK 470 LYS A 433 CG CD CE NZ
REMARK 470 LYS A 500 CG CD CE NZ
REMARK 470 GLU A 525 CG CD OE1 OE2
REMARK 470 LEU A 634 CG CD1 CD2
REMARK 470 LYS A 637 CG CD CE NZ
REMARK 470 LYS A 678 CG CD CE NZ
REMARK 470 LYS A 689 CG CD CE NZ
REMARK 470 LYS A 707 CG CD CE NZ
REMARK 470 LYS A 709 CG CD CE NZ
REMARK 470 ILE A 710 CG1 CG2 CD1
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 A 226 OE1 GLU A 228 2.06
REMARK 500 O HOH A 1286 O HOH A 1573 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 606 CB SER A 606 OG -0.099
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 71 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU A 481 CB - CG - CD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 LEU A 593 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ASP A 687 CB - CG - OD1 ANGL. DEV. = 6.8 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 GLU A 31 -166.63 -114.61
REMARK 500 VAL A 33 -83.58 -130.93
REMARK 500 ASP A 265 30.02 -142.19
REMARK 500 PHE A 266 -45.43 90.22
REMARK 500 LYS A 299 -133.20 50.72
REMARK 500 LYS A 313 -117.81 52.74
REMARK 500 ASN A 353 -69.45 -107.76
REMARK 500 PRO A 393 44.83 -86.46
REMARK 500 TYR A 485 -75.31 -125.77
REMARK 500 TRP A 504 -61.46 -95.74
REMARK 500 SER A 566 -122.24 65.29
REMARK 500 VAL A 590 58.79 32.56
REMARK 500 LEU A 593 -25.75 -155.52
REMARK 500 HIS A 653 139.10 87.67
REMARK 500 ASP A 679 13.07 -146.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 808
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-RITYA.17583.B RELATED DB: TARGETTRACK
DBREF 4HVT A 10 711 UNP Q68XJ3 Q68XJ3_RICTY 19 720
SEQADV 4HVT MET A 1 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT ALA A 2 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT HIS A 3 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT HIS A 4 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT HIS A 5 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT HIS A 6 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT HIS A 7 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT HIS A 8 UNP Q68XJ3 EXPRESSION TAG
SEQADV 4HVT MET A 9 UNP Q68XJ3 EXPRESSION TAG
SEQRES 1 A 711 MET ALA HIS HIS HIS HIS HIS HIS MET ALA MET GLU ASP
SEQRES 2 A 711 ASN ASN LYS GLN ILE PHE ASN PRO LYS GLU THR LYS PHE
SEQRES 3 A 711 LEU GLU GLU ALA GLU GLY VAL GLU ALA LEU GLU TRP ALA
SEQRES 4 A 711 LYS GLU ARG THR SER LYS THR GLU LYS ALA LEU GLN ALA
SEQRES 5 A 711 MET GLN GLU TYR LYS GLN ILE LYS LYS GLU ILE GLU THR
SEQRES 6 A 711 ILE PHE TYR ASP GLN ARG LYS THR PRO TYR GLY VAL ILE
SEQRES 7 A 711 ARG LYS GLY TYR VAL TYR ASN PHE TRP MET ASP ASP LYS
SEQRES 8 A 711 ASN PRO GLN GLY LEU TRP ARG ARG THR LEU VAL ASP ASN
SEQRES 9 A 711 TYR SER LYS ASP LYS PRO ASN TRP GLU VAL LEU ILE ASP
SEQRES 10 A 711 PHE ASP LYS LEU SER LYS LYS ILE GLY LYS LYS VAL ALA
SEQRES 11 A 711 TYR ARG GLY VAL SER ASN CYS PHE GLN ASN PRO ASN ARG
SEQRES 12 A 711 TYR LEU ILE SER MET SER PHE GLY GLY LYS ASP GLU MET
SEQRES 13 A 711 PHE PHE ARG GLU TRP ASP LEU GLU LYS LYS ASP PHE VAL
SEQRES 14 A 711 LYS ASN GLY PHE GLU PRO ILE THR ASN SER GLY LYS LEU
SEQRES 15 A 711 LEU GLU GLY LYS PHE THR TYR PRO THR TRP ILE ASN LYS
SEQRES 16 A 711 ASP THR ILE ILE PHE ASN LEU VAL LEU HIS LYS ASN GLU
SEQRES 17 A 711 ILE THR SER SER LEU TYR PRO ASN SER LEU TYR ILE TRP
SEQRES 18 A 711 LYS ARG GLY GLU SER ILE GLU LYS ALA LYS LYS LEU PHE
SEQRES 19 A 711 GLU VAL PRO LYS GLU TYR ILE TYR VAL SER ALA GLY LYS
SEQRES 20 A 711 LEU LEU SER ASP THR ILE SER SER SER LEU ILE PHE ILE
SEQRES 21 A 711 SER ALA ASN LYS ASP PHE TYR ASN TYR ASP ASN TYR ILE
SEQRES 22 A 711 LEU ASP THR LYS TYR LYS ASN LEU LYS LEU GLN LYS ILE
SEQRES 23 A 711 ASN MET PRO SER ASP ALA THR LEU GLN GLY SER PHE LYS
SEQRES 24 A 711 GLU TYR VAL PHE TRP LEU LEU ARG SER ASP TRP LYS PHE
SEQRES 25 A 711 LYS SER HIS ASN ILE LYS ALA GLY SER LEU VAL ALA LEU
SEQRES 26 A 711 HIS PHE THR ASP LEU LEU LYS THR GLU SER ASP LYS THR
SEQRES 27 A 711 SER LEU LYS ILE LEU PHE THR PRO THR ALA ASN GLU VAL
SEQRES 28 A 711 PHE ASN PHE ILE SER THR THR LYS ASP ARG VAL PHE LEU
SEQRES 29 A 711 ALA THR TYR ASP ASN VAL VAL ALA LYS VAL VAL THR PHE
SEQRES 30 A 711 THR LEU GLU ASN GLU GLN TRP THR LYS PRO VAL VAL LEU
SEQRES 31 A 711 LYS LEU PRO TYR GLN ASN ALA ILE PHE GLY MET SER SER
SEQRES 32 A 711 TYR GLU GLU GLU GLU GLU ALA LEU ILE THR ILE GLU ASN
SEQRES 33 A 711 SER ILE VAL PRO PRO THR ILE TYR LEU TRP VAL LYS THR
SEQRES 34 A 711 HIS GLU LEU LYS ILE ILE ARG LYS ALA LEU TYR SER PHE
SEQRES 35 A 711 ASP SER GLU ASN TYR VAL LEU GLU GLN LYS GLU ALA THR
SEQRES 36 A 711 SER PHE ASP GLY VAL LYS ILE PRO TYR PHE LEU VAL TYR
SEQRES 37 A 711 LYS LYS GLY ILE LYS PHE ASP GLY LYS ASN PRO THR LEU
SEQRES 38 A 711 LEU GLU ALA TYR GLY GLY PHE GLN VAL ILE ASN ALA PRO
SEQRES 39 A 711 TYR PHE SER ARG ILE LYS ASN GLU VAL TRP VAL LYS ASN
SEQRES 40 A 711 ALA GLY VAL SER VAL LEU ALA ASN ILE ARG GLY GLY GLY
SEQRES 41 A 711 GLU PHE GLY PRO GLU TRP HIS LYS SER ALA GLN GLY ILE
SEQRES 42 A 711 LYS ARG GLN THR ALA PHE ASN ASP PHE PHE ALA VAL SER
SEQRES 43 A 711 GLU GLU LEU ILE LYS GLN ASN ILE THR SER PRO GLU TYR
SEQRES 44 A 711 LEU GLY ILE LYS GLY GLY SER ASN GLY GLY LEU LEU VAL
SEQRES 45 A 711 SER VAL ALA MET THR GLN ARG PRO GLU LEU PHE GLY ALA
SEQRES 46 A 711 VAL ALA CYS GLU VAL PRO ILE LEU ASP MET ILE ARG TYR
SEQRES 47 A 711 LYS GLU PHE GLY ALA GLY HIS SER TRP VAL THR GLU TYR
SEQRES 48 A 711 GLY ASP PRO GLU ILE PRO ASN ASP LEU LEU HIS ILE LYS
SEQRES 49 A 711 LYS TYR ALA PRO LEU GLU ASN LEU SER LEU THR GLN LYS
SEQRES 50 A 711 TYR PRO THR VAL LEU ILE THR ASP SER VAL LEU ASP GLN
SEQRES 51 A 711 ARG VAL HIS PRO TRP HIS GLY ARG ILE PHE GLU TYR VAL
SEQRES 52 A 711 LEU ALA GLN ASN PRO ASN THR LYS THR TYR PHE LEU GLU
SEQRES 53 A 711 SER LYS ASP SER GLY HIS GLY SER GLY SER ASP LEU LYS
SEQRES 54 A 711 GLU SER ALA ASN TYR PHE ILE ASN LEU TYR THR PHE PHE
SEQRES 55 A 711 ALA ASN ALA LEU LYS LEU LYS ILE ASN
HET EDO A 801 4
HET EDO A 802 4
HET EDO A 803 4
HET EDO A 804 4
HET EDO A 805 4
HET EDO A 806 4
HET CL A 807 1
HET CL A 808 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 6(C2 H6 O2)
FORMUL 8 CL 2(CL 1-)
FORMUL 10 HOH *746(H2 O)
HELIX 1 1 ASN A 20 LYS A 25 1 6
HELIX 2 2 PHE A 26 GLU A 29 5 4
HELIX 3 3 VAL A 33 ALA A 52 1 20
HELIX 4 4 GLU A 55 TYR A 68 1 14
HELIX 5 5 VAL A 102 SER A 106 1 5
HELIX 6 6 PHE A 118 GLY A 126 1 9
HELIX 7 7 SER A 226 ALA A 230 5 5
HELIX 8 8 THR A 328 LYS A 332 5 5
HELIX 9 9 THR A 333 LYS A 337 5 5
HELIX 10 10 ASP A 443 GLU A 445 5 3
HELIX 11 11 SER A 497 TRP A 504 1 8
HELIX 12 12 VAL A 505 ALA A 508 5 4
HELIX 13 13 GLY A 523 SER A 529 1 7
HELIX 14 14 ALA A 530 LYS A 534 5 5
HELIX 15 15 ARG A 535 GLN A 552 1 18
HELIX 16 16 SER A 556 GLU A 558 5 3
HELIX 17 17 ASN A 567 ARG A 579 1 13
HELIX 18 18 PRO A 580 PHE A 583 5 4
HELIX 19 19 ARG A 597 PHE A 601 5 5
HELIX 20 20 ALA A 603 SER A 606 5 4
HELIX 21 21 TRP A 607 GLY A 612 1 6
HELIX 22 22 ILE A 616 ALA A 627 1 12
HELIX 23 23 PRO A 628 ASN A 631 5 4
HELIX 24 24 PRO A 654 ALA A 665 1 12
HELIX 25 25 ASP A 687 LYS A 707 1 21
SHEET 1 A 4 VAL A 77 ARG A 79 0
SHEET 2 A 4 TYR A 82 TRP A 87 -1 O TYR A 84 N VAL A 77
SHEET 3 A 4 LEU A 96 LEU A 101 -1 O THR A 100 N VAL A 83
SHEET 4 A 4 GLU A 113 ASP A 117 -1 O LEU A 115 N TRP A 97
SHEET 1 B 4 VAL A 129 ASN A 136 0
SHEET 2 B 4 ARG A 143 PHE A 150 -1 O SER A 149 N ALA A 130
SHEET 3 B 4 GLU A 155 ASP A 162 -1 O ARG A 159 N ILE A 146
SHEET 4 B 4 ASP A 167 PHE A 168 -1 O ASP A 167 N ASP A 162
SHEET 1 C 4 VAL A 129 ASN A 136 0
SHEET 2 C 4 ARG A 143 PHE A 150 -1 O SER A 149 N ALA A 130
SHEET 3 C 4 GLU A 155 ASP A 162 -1 O ARG A 159 N ILE A 146
SHEET 4 C 4 GLY A 185 LYS A 186 -1 O GLY A 185 N MET A 156
SHEET 1 D 4 PRO A 190 ASN A 194 0
SHEET 2 D 4 THR A 197 PHE A 200 -1 O THR A 197 N ILE A 193
SHEET 3 D 4 SER A 217 LYS A 222 -1 O TRP A 221 N ILE A 198
SHEET 4 D 4 LYS A 231 GLU A 235 -1 O LEU A 233 N LEU A 218
SHEET 1 E 4 TYR A 242 LYS A 247 0
SHEET 2 E 4 LEU A 257 ASN A 263 -1 O PHE A 259 N GLY A 246
SHEET 3 E 4 TYR A 269 ASP A 275 -1 O LEU A 274 N ILE A 258
SHEET 4 E 4 LYS A 282 LYS A 285 -1 O GLN A 284 N ILE A 273
SHEET 1 F 4 THR A 293 PHE A 298 0
SHEET 2 F 4 TYR A 301 LEU A 305 -1 O PHE A 303 N GLN A 295
SHEET 3 F 4 LEU A 322 HIS A 326 -1 O VAL A 323 N TRP A 304
SHEET 4 F 4 LYS A 341 PHE A 344 -1 O LYS A 341 N ALA A 324
SHEET 1 G 2 TRP A 310 PHE A 312 0
SHEET 2 G 2 HIS A 315 ILE A 317 -1 O ILE A 317 N TRP A 310
SHEET 1 H 4 GLU A 350 THR A 357 0
SHEET 2 H 4 VAL A 362 ASP A 368 -1 O PHE A 363 N SER A 356
SHEET 3 H 4 VAL A 371 PHE A 377 -1 O LYS A 373 N THR A 366
SHEET 4 H 4 VAL A 388 LEU A 390 -1 O LEU A 390 N VAL A 374
SHEET 1 I 2 LEU A 379 GLU A 380 0
SHEET 2 I 2 GLN A 383 TRP A 384 -1 O GLN A 383 N GLU A 380
SHEET 1 J 4 ILE A 398 SER A 402 0
SHEET 2 J 4 ALA A 410 GLU A 415 -1 O THR A 413 N GLY A 400
SHEET 3 J 4 THR A 422 TRP A 426 -1 O TYR A 424 N ILE A 412
SHEET 4 J 4 LEU A 432 ARG A 436 -1 O LYS A 433 N LEU A 425
SHEET 1 K 8 TYR A 447 THR A 455 0
SHEET 2 K 8 LYS A 461 LYS A 469 -1 O TYR A 464 N LYS A 452
SHEET 3 K 8 VAL A 510 ALA A 514 -1 O LEU A 513 N PHE A 465
SHEET 4 K 8 THR A 480 GLU A 483 1 N LEU A 481 O VAL A 512
SHEET 5 K 8 LEU A 560 GLY A 565 1 O GLY A 561 N THR A 480
SHEET 6 K 8 ALA A 585 GLU A 589 1 O GLU A 589 N GLY A 564
SHEET 7 K 8 THR A 640 SER A 646 1 O LEU A 642 N VAL A 586
SHEET 8 K 8 THR A 672 SER A 677 1 O TYR A 673 N ILE A 643
SITE 1 AC1 10 ASN A 171 GLY A 172 PHE A 173 TRP A 221
SITE 2 AC1 10 LYS A 222 ARG A 223 GLY A 224 GLU A 225
SITE 3 AC1 10 LYS A 386 HOH A1114
SITE 1 AC2 6 THR A 73 ASN A 85 PHE A 86 TRP A 87
SITE 2 AC2 6 MET A 88 HOH A1376
SITE 1 AC3 6 ASN A 349 GLU A 453 LYS A 461 PHE A 522
SITE 2 AC3 6 HOH A1026 HOH A1640
SITE 1 AC4 7 LEU A 213 PHE A 601 GLY A 602 HIS A 653
SITE 2 AC4 7 HOH A1117 HOH A1371 HOH A1586
SITE 1 AC5 4 LEU A 432 ILE A 434 HOH A 937 HOH A1013
SITE 1 AC6 2 TYR A 75 GLU A 415
SITE 1 AC7 4 ARG A 79 TYR A 84 TRP A 97 HOH A1645
SITE 1 AC8 2 ARG A 143 ARG A 223
CRYST1 199.590 73.280 55.460 90.00 98.52 90.00 C 1 2 1 4
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 0.005010 0.000000 0.000751 0.00000
SCALE2 0.000000 0.013646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018232 0.00000
TER 5564 ILE A 710
MASTER 458 0 8 25 44 0 13 6 6282 1 24 55
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