HEADER TRANSFERASE 31-JUL-13 4LZO
TITLE CRYSTAL STRUCTURE OF HUMAN PRS1 A87T MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPRIBP, PHOSPHORIBOSYL PYROPHOSPHATE SYNTHASE I, PRS-I;
COMPND 5 EC: 2.7.6.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PRPS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PRS1, PRPP SYNTHESIS ENZYME, ATP R5P, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CHEN,M.TENG,X.LI
REVDAT 3 20-MAR-24 4LZO 1 REMARK SEQADV
REVDAT 2 25-MAR-15 4LZO 1 JRNL
REVDAT 1 04-FEB-15 4LZO 0
JRNL AUTH P.CHEN,Z.LIU,X.WANG,J.PENG,Q.SUN,J.LI,M.WANG,L.NIU,Z.ZHANG,
JRNL AUTH 2 G.CAI,M.TENG,X.LI
JRNL TITL CRYSTAL AND EM STRUCTURES OF HUMAN PHOSPHORIBOSYL
JRNL TITL 2 PYROPHOSPHATE SYNTHASE I (PRS1) PROVIDE NOVEL INSIGHTS INTO
JRNL TITL 3 THE DISEASE-ASSOCIATED MUTATIONS
JRNL REF PLOS ONE V. 10 20304 2015
JRNL REFN ESSN 1932-6203
JRNL PMID 25781187
JRNL DOI 10.1371/JOURNAL.PONE.0120304
REMARK 2
REMARK 2 RESOLUTION. 3.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 9535
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) : 0.266
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 482
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) : 3.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 687
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4684
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.83000
REMARK 3 B22 (A**2) : 1.83000
REMARK 3 B33 (A**2) : -2.75000
REMARK 3 B12 (A**2) : 0.92000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.738
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.603
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.074
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.795
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.740
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4774 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6459 ; 1.141 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 608 ; 5.350 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 199 ;38.148 ;24.523
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 857 ;17.552 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;14.483 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 765 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3478 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3039 ; 0.370 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4920 ; 0.685 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1735 ; 0.664 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1539 ; 1.209 ; 4.500
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 : 1.40
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 4LZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10020
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.310
REMARK 200 RESOLUTION RANGE LOW (A) : 34.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.1, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 85.20100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.19082
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 20.71467
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 85.20100
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 49.19082
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 20.71467
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 85.20100
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 49.19082
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 20.71467
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 98.38164
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 41.42933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 98.38164
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 41.42933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 98.38164
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 41.42933
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -431.0 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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 1
REMARK 465 PRO A 2
REMARK 465 ARG A 196
REMARK 465 LYS A 197
REMARK 465 LYS A 198
REMARK 465 ALA A 199
REMARK 465 ASN A 200
REMARK 465 GLU A 201
REMARK 465 VAL A 202
REMARK 465 SER A 314
REMARK 465 HIS A 315
REMARK 465 VAL A 316
REMARK 465 PRO A 317
REMARK 465 LEU A 318
REMARK 465 LEU A 319
REMARK 465 GLU A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ARG B 196
REMARK 465 LYS B 197
REMARK 465 LYS B 198
REMARK 465 ALA B 199
REMARK 465 ASN B 200
REMARK 465 GLU B 201
REMARK 465 VAL B 202
REMARK 465 LEU B 318
REMARK 465 LEU B 319
REMARK 465 GLU B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS B 326
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 11 N - CA - C ANGL. DEV. = -29.6 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 8 -168.03 -104.84
REMARK 500 SER A 11 -158.45 -139.47
REMARK 500 GLN A 38 -0.87 71.04
REMARK 500 ARG A 84 144.47 -173.71
REMARK 500 LYS A 102 -0.22 71.62
REMARK 500 ASP A 128 62.87 34.90
REMARK 500 ILE A 134 63.22 -64.68
REMARK 500 GLN A 135 -24.40 -140.08
REMARK 500 ALA A 232 -37.47 -39.91
REMARK 500 SER B 10 -140.84 60.00
REMARK 500 HIS B 12 80.05 -69.34
REMARK 500 GLN B 38 14.60 86.45
REMARK 500 GLU B 46 127.62 -174.78
REMARK 500 SER B 47 119.66 -37.69
REMARK 500 ARG B 49 106.34 -55.25
REMARK 500 GLN B 97 61.43 -109.77
REMARK 500 LYS B 102 14.20 52.31
REMARK 500 ASP B 128 73.04 44.16
REMARK 500 ASN B 164 29.81 -147.35
REMARK 500 ASP B 224 -78.54 -109.03
REMARK 500 ASN B 273 45.80 -94.01
REMARK 500 TYR B 311 -1.89 -55.28
REMARK 500 SER B 314 31.95 -143.64
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 SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LYG RELATED DB: PDB
REMARK 900 RELATED ID: 4LZP RELATED DB: PDB
REMARK 900 RELATED ID: 4M0P RELATED DB: PDB
REMARK 900 RELATED ID: 4M0U RELATED DB: PDB
DBREF 4LZO A 1 318 UNP P60891 PRPS1_HUMAN 1 318
DBREF 4LZO B 1 318 UNP P60891 PRPS1_HUMAN 1 318
SEQADV 4LZO THR A 87 UNP P60891 ALA 87 ENGINEERED MUTATION
SEQADV 4LZO LEU A 319 UNP P60891 EXPRESSION TAG
SEQADV 4LZO GLU A 320 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS A 321 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS A 322 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS A 323 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS A 324 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS A 325 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS A 326 UNP P60891 EXPRESSION TAG
SEQADV 4LZO THR B 87 UNP P60891 ALA 87 ENGINEERED MUTATION
SEQADV 4LZO LEU B 319 UNP P60891 EXPRESSION TAG
SEQADV 4LZO GLU B 320 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS B 321 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS B 322 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS B 323 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS B 324 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS B 325 UNP P60891 EXPRESSION TAG
SEQADV 4LZO HIS B 326 UNP P60891 EXPRESSION TAG
SEQRES 1 A 326 MET PRO ASN ILE LYS ILE PHE SER GLY SER SER HIS GLN
SEQRES 2 A 326 ASP LEU SER GLN LYS ILE ALA ASP ARG LEU GLY LEU GLU
SEQRES 3 A 326 LEU GLY LYS VAL VAL THR LYS LYS PHE SER ASN GLN GLU
SEQRES 4 A 326 THR CYS VAL GLU ILE GLY GLU SER VAL ARG GLY GLU ASP
SEQRES 5 A 326 VAL TYR ILE VAL GLN SER GLY CYS GLY GLU ILE ASN ASP
SEQRES 6 A 326 ASN LEU MET GLU LEU LEU ILE MET ILE ASN ALA CYS LYS
SEQRES 7 A 326 ILE ALA SER ALA SER ARG VAL THR THR VAL ILE PRO CYS
SEQRES 8 A 326 PHE PRO TYR ALA ARG GLN ASP LYS LYS ASP LYS SER ARG
SEQRES 9 A 326 ALA PRO ILE SER ALA LYS LEU VAL ALA ASN MET LEU SER
SEQRES 10 A 326 VAL ALA GLY ALA ASP HIS ILE ILE THR MET ASP LEU HIS
SEQRES 11 A 326 ALA SER GLN ILE GLN GLY PHE PHE ASP ILE PRO VAL ASP
SEQRES 12 A 326 ASN LEU TYR ALA GLU PRO ALA VAL LEU LYS TRP ILE ARG
SEQRES 13 A 326 GLU ASN ILE SER GLU TRP ARG ASN CYS THR ILE VAL SER
SEQRES 14 A 326 PRO ASP ALA GLY GLY ALA LYS ARG VAL THR SER ILE ALA
SEQRES 15 A 326 ASP ARG LEU ASN VAL ASP PHE ALA LEU ILE HIS LYS GLU
SEQRES 16 A 326 ARG LYS LYS ALA ASN GLU VAL ASP ARG MET VAL LEU VAL
SEQRES 17 A 326 GLY ASP VAL LYS ASP ARG VAL ALA ILE LEU VAL ASP ASP
SEQRES 18 A 326 MET ALA ASP THR CYS GLY THR ILE CYS HIS ALA ALA ASP
SEQRES 19 A 326 LYS LEU LEU SER ALA GLY ALA THR ARG VAL TYR ALA ILE
SEQRES 20 A 326 LEU THR HIS GLY ILE PHE SER GLY PRO ALA ILE SER ARG
SEQRES 21 A 326 ILE ASN ASN ALA CYS PHE GLU ALA VAL VAL VAL THR ASN
SEQRES 22 A 326 THR ILE PRO GLN GLU ASP LYS MET LYS HIS CYS SER LYS
SEQRES 23 A 326 ILE GLN VAL ILE ASP ILE SER MET ILE LEU ALA GLU ALA
SEQRES 24 A 326 ILE ARG ARG THR HIS ASN GLY GLU SER VAL SER TYR LEU
SEQRES 25 A 326 PHE SER HIS VAL PRO LEU LEU GLU HIS HIS HIS HIS HIS
SEQRES 26 A 326 HIS
SEQRES 1 B 326 MET PRO ASN ILE LYS ILE PHE SER GLY SER SER HIS GLN
SEQRES 2 B 326 ASP LEU SER GLN LYS ILE ALA ASP ARG LEU GLY LEU GLU
SEQRES 3 B 326 LEU GLY LYS VAL VAL THR LYS LYS PHE SER ASN GLN GLU
SEQRES 4 B 326 THR CYS VAL GLU ILE GLY GLU SER VAL ARG GLY GLU ASP
SEQRES 5 B 326 VAL TYR ILE VAL GLN SER GLY CYS GLY GLU ILE ASN ASP
SEQRES 6 B 326 ASN LEU MET GLU LEU LEU ILE MET ILE ASN ALA CYS LYS
SEQRES 7 B 326 ILE ALA SER ALA SER ARG VAL THR THR VAL ILE PRO CYS
SEQRES 8 B 326 PHE PRO TYR ALA ARG GLN ASP LYS LYS ASP LYS SER ARG
SEQRES 9 B 326 ALA PRO ILE SER ALA LYS LEU VAL ALA ASN MET LEU SER
SEQRES 10 B 326 VAL ALA GLY ALA ASP HIS ILE ILE THR MET ASP LEU HIS
SEQRES 11 B 326 ALA SER GLN ILE GLN GLY PHE PHE ASP ILE PRO VAL ASP
SEQRES 12 B 326 ASN LEU TYR ALA GLU PRO ALA VAL LEU LYS TRP ILE ARG
SEQRES 13 B 326 GLU ASN ILE SER GLU TRP ARG ASN CYS THR ILE VAL SER
SEQRES 14 B 326 PRO ASP ALA GLY GLY ALA LYS ARG VAL THR SER ILE ALA
SEQRES 15 B 326 ASP ARG LEU ASN VAL ASP PHE ALA LEU ILE HIS LYS GLU
SEQRES 16 B 326 ARG LYS LYS ALA ASN GLU VAL ASP ARG MET VAL LEU VAL
SEQRES 17 B 326 GLY ASP VAL LYS ASP ARG VAL ALA ILE LEU VAL ASP ASP
SEQRES 18 B 326 MET ALA ASP THR CYS GLY THR ILE CYS HIS ALA ALA ASP
SEQRES 19 B 326 LYS LEU LEU SER ALA GLY ALA THR ARG VAL TYR ALA ILE
SEQRES 20 B 326 LEU THR HIS GLY ILE PHE SER GLY PRO ALA ILE SER ARG
SEQRES 21 B 326 ILE ASN ASN ALA CYS PHE GLU ALA VAL VAL VAL THR ASN
SEQRES 22 B 326 THR ILE PRO GLN GLU ASP LYS MET LYS HIS CYS SER LYS
SEQRES 23 B 326 ILE GLN VAL ILE ASP ILE SER MET ILE LEU ALA GLU ALA
SEQRES 24 B 326 ILE ARG ARG THR HIS ASN GLY GLU SER VAL SER TYR LEU
SEQRES 25 B 326 PHE SER HIS VAL PRO LEU LEU GLU HIS HIS HIS HIS HIS
SEQRES 26 B 326 HIS
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HET SO4 B 401 5
HET SO4 B 402 5
HET SO4 B 403 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 6(O4 S 2-)
HELIX 1 1 HIS A 12 LEU A 23 1 12
HELIX 2 2 GLU A 62 ALA A 80 1 19
HELIX 3 3 ILE A 107 GLY A 120 1 14
HELIX 4 4 ALA A 147 ILE A 159 1 13
HELIX 5 5 GLU A 161 ASN A 164 5 4
HELIX 6 6 ASP A 171 GLY A 173 5 3
HELIX 7 7 GLY A 174 LEU A 185 1 12
HELIX 8 8 CYS A 226 ALA A 239 1 14
HELIX 9 9 PRO A 256 ASN A 263 1 8
HELIX 10 10 GLN A 277 HIS A 283 1 7
HELIX 11 11 ILE A 292 GLY A 306 1 15
HELIX 12 12 VAL A 309 PHE A 313 5 5
HELIX 13 13 GLN B 13 LEU B 23 1 11
HELIX 14 14 GLU B 62 ALA B 80 1 19
HELIX 15 15 ILE B 107 GLY B 120 1 14
HELIX 16 16 ALA B 131 PHE B 138 5 8
HELIX 17 17 ALA B 147 ILE B 159 1 13
HELIX 18 18 SER B 160 ARG B 163 5 4
HELIX 19 19 GLY B 174 ASN B 186 1 13
HELIX 20 20 CYS B 226 ALA B 239 1 14
HELIX 21 21 PRO B 256 ALA B 264 1 9
HELIX 22 22 GLN B 277 CYS B 284 1 8
HELIX 23 23 ILE B 292 GLY B 306 1 15
HELIX 24 24 SER B 308 PHE B 313 5 6
SHEET 1 A 5 ILE A 4 PHE A 7 0
SHEET 2 A 5 ASP A 52 VAL A 56 1 O TYR A 54 N PHE A 7
SHEET 3 A 5 ARG A 84 VAL A 88 1 O VAL A 88 N ILE A 55
SHEET 4 A 5 HIS A 123 MET A 127 1 O ILE A 125 N THR A 87
SHEET 5 A 5 VAL A 142 LEU A 145 1 O LEU A 145 N THR A 126
SHEET 1 B 2 LYS A 33 LYS A 34 0
SHEET 2 B 2 THR A 40 CYS A 41 -1 O CYS A 41 N LYS A 33
SHEET 1 C 7 MET A 205 VAL A 208 0
SHEET 2 C 7 ASP A 188 LYS A 194 -1 N LEU A 191 O VAL A 208
SHEET 3 C 7 THR A 166 SER A 169 1 N SER A 169 O ALA A 190
SHEET 4 C 7 ALA A 216 ALA A 223 1 O ILE A 217 N THR A 166
SHEET 5 C 7 VAL A 244 GLY A 251 1 O ILE A 247 N LEU A 218
SHEET 6 C 7 VAL A 269 THR A 272 1 O VAL A 270 N LEU A 248
SHEET 7 C 7 ILE A 287 ILE A 290 1 O GLN A 288 N VAL A 269
SHEET 1 D 5 ILE B 4 SER B 8 0
SHEET 2 D 5 ASP B 52 VAL B 56 1 O TYR B 54 N PHE B 7
SHEET 3 D 5 ARG B 84 ILE B 89 1 O VAL B 88 N ILE B 55
SHEET 4 D 5 HIS B 123 MET B 127 1 O ILE B 125 N ILE B 89
SHEET 5 D 5 VAL B 142 LEU B 145 1 O LEU B 145 N THR B 126
SHEET 1 E 2 LYS B 33 LYS B 34 0
SHEET 2 E 2 THR B 40 CYS B 41 -1 O CYS B 41 N LYS B 33
SHEET 1 F 7 MET B 205 VAL B 208 0
SHEET 2 F 7 ASP B 188 LYS B 194 -1 N HIS B 193 O VAL B 206
SHEET 3 F 7 CYS B 165 SER B 169 1 N SER B 169 O ILE B 192
SHEET 4 F 7 VAL B 215 ALA B 223 1 O ILE B 217 N THR B 166
SHEET 5 F 7 VAL B 244 GLY B 251 1 O TYR B 245 N LEU B 218
SHEET 6 F 7 PHE B 266 THR B 272 1 O GLU B 267 N VAL B 244
SHEET 7 F 7 ILE B 287 ILE B 290 1 O GLN B 288 N VAL B 269
SITE 1 AC1 6 SER A 47 ARG A 49 SER A 308 VAL A 309
SITE 2 AC1 6 SER A 310 ARG B 104
SITE 1 AC2 5 ALA A 223 ASP A 224 THR A 225 CYS A 226
SITE 2 AC2 5 THR A 228
SITE 1 AC3 7 SER A 132 GLN A 135 ASN A 144 TYR A 146
SITE 2 AC3 7 LYS B 100 ASP B 101 LYS B 102
SITE 1 AC4 6 ARG A 104 SER B 47 ARG B 49 SER B 308
SITE 2 AC4 6 VAL B 309 SER B 310
SITE 1 AC5 6 ALA B 223 ASP B 224 THR B 225 CYS B 226
SITE 2 AC5 6 GLY B 227 THR B 228
SITE 1 AC6 8 LYS A 99 LYS A 100 ASP A 101 LYS A 102
SITE 2 AC6 8 SER B 132 GLN B 135 ASN B 144 TYR B 146
CRYST1 170.402 170.402 62.144 90.00 90.00 120.00 H 3 18
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 0.005868 0.003388 0.000000 0.00000
SCALE2 0.000000 0.006776 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016092 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
