HEADER TRANSFERASE 11-MAY-05 1ZN9
TITLE HUMAN ADENINE PHOSPHORIBOSYLTRANSFERASE IN APO AND AMP COMPLEXED FORMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENINE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: APRT;
COMPND 5 EC: 2.4.2.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: APRT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET29A
KEYWDS GLYCOSYLTRANSFERASE, PURINE SALVAGE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.IULEK,M.SILVA,C.H.T.P.TOMICH,O.H.THIEMANN
REVDAT 5 14-FEB-24 1ZN9 1 REMARK
REVDAT 4 13-JUL-11 1ZN9 1 VERSN
REVDAT 3 24-FEB-09 1ZN9 1 VERSN
REVDAT 2 29-APR-08 1ZN9 1 JRNL
REVDAT 1 25-APR-06 1ZN9 0
JRNL AUTH C.H.SILVA,M.SILVA,J.IULEK,O.H.THIEMANN
JRNL TITL STRUCTURAL COMPLEXES OF HUMAN ADENINE
JRNL TITL 2 PHOSPHORIBOSYLTRANSFERASE REVEAL NOVEL FEATURES OF THE APRT
JRNL TITL 3 CATALYTIC MECHANISM
JRNL REF J.BIOMOL.STRUCT.DYN. V. 25 589 2008
JRNL REFN ISSN 0739-1102
JRNL PMID 18399692
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 19146
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1032
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1217
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.1750
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2733
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -0.09000
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): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.512
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2890 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2794 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3925 ; 1.793 ; 2.017
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6495 ; 0.965 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 356 ; 6.526 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;35.104 ;23.689
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 514 ;16.617 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;20.205 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 462 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3143 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 562 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 555 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2734 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1309 ; 0.169 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1793 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 217 ; 0.196 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.003 ; 0.200
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): 15 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 100 ; 0.300 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.277 ; 0.200
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): 1977 ; 1.007 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 732 ; 0.233 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2903 ; 1.455 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1178 ; 2.338 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1022 ; 3.404 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 180
REMARK 3 RESIDUE RANGE : B 2 B 180
REMARK 3 RESIDUE RANGE : B 1031 B 1031
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9150 7.0600 51.1720
REMARK 3 T TENSOR
REMARK 3 T11: -0.1849 T22: -0.1351
REMARK 3 T33: -0.2042 T12: -0.0119
REMARK 3 T13: -0.0068 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.8255 L22: 0.8456
REMARK 3 L33: 0.7721 L12: -0.1874
REMARK 3 L13: -0.1885 L23: -0.0208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0322 S12: -0.0412 S13: 0.0201
REMARK 3 S21: 0.0820 S22: -0.0008 S23: -0.0241
REMARK 3 S31: -0.0100 S32: 0.0689 S33: 0.0330
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 1ZN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000032920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20179
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 28.520
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) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.0 % (V/V) GLYCEROL, 25.5 % (W/V)
REMARK 280 POLYETHYLENE GLYCOL 4000, 0.17 MOL/L SODIUM ACETATE AND 0.085
REMARK 280 MOL/L TRIS-HCL PH 8.5 , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.75550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.05250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.62600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.05250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.75550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.62600
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: DIMERIC
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 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 MET B 1
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 LYS A 107 CE NZ
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 TYR B 105 CG CD1 CD2 CE1 CE2 CZ OH
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 OE2 GLU A 5 O HOH A 333 2.16
REMARK 500 O3' AMP B 1031 O HOH B 1084 2.17
REMARK 500 OE1 GLU B 111 O HOH B 1120 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 57 O HOH B 1121 1545 2.11
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 89 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LEU B 110 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP B 128 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 MET B 136 CG - SD - CE ANGL. DEV. = -9.9 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 ASP A 3 -95.36 175.60
REMARK 500 GLU A 104 -113.48 47.93
REMARK 500 ALA A 131 -103.35 -107.93
REMARK 500 ASP B 3 -88.33 -13.70
REMARK 500 GLU B 104 94.24 -64.99
REMARK 500 TYR B 105 111.73 66.37
REMARK 500 ALA B 131 -106.64 -105.84
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 AMP B 1031
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ORE RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN ADENINE PHOSPHORIBOSYLTRANSFERASE
REMARK 900 RELATED ID: 1ZN7 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH PRPP, ADE AND R5P
REMARK 900 RELATED ID: 1ZN8 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH AMP, IN SPACE GROUP P1 AT 1.76 A
REMARK 900 RESOLUTION
DBREF 1ZN9 A 1 180 UNP P07741 APT_HUMAN 1 179
DBREF 1ZN9 B 1 180 UNP P07741 APT_HUMAN 1 179
SEQRES 1 A 180 MET ALA ASP SER GLU LEU GLN LEU VAL GLU GLN ARG ILE
SEQRES 2 A 180 ARG SER PHE PRO ASP PHE PRO THR PRO GLY VAL VAL PHE
SEQRES 3 A 180 ARG ASP ILE SER PRO VAL LEU LYS ASP PRO ALA SER PHE
SEQRES 4 A 180 ARG ALA ALA ILE GLY LEU LEU ALA ARG HIS LEU LYS ALA
SEQRES 5 A 180 THR HIS GLY GLY ARG ILE ASP TYR ILE ALA GLY LEU ASP
SEQRES 6 A 180 SER ARG GLY PHE LEU PHE GLY PRO SER LEU ALA GLN GLU
SEQRES 7 A 180 LEU GLY LEU GLY CYS VAL LEU ILE ARG LYS ARG GLY LYS
SEQRES 8 A 180 LEU PRO GLY PRO THR LEU TRP ALA SER TYR SER LEU GLU
SEQRES 9 A 180 TYR GLY LYS ALA GLU LEU GLU ILE GLN LYS ASP ALA LEU
SEQRES 10 A 180 GLU PRO GLY GLN ARG VAL VAL VAL VAL ASP ASP LEU LEU
SEQRES 11 A 180 ALA THR GLY GLY THR MET ASN ALA ALA CYS GLU LEU LEU
SEQRES 12 A 180 GLY ARG LEU GLN ALA GLU VAL LEU GLU CYS VAL SER LEU
SEQRES 13 A 180 VAL GLU LEU THR SER LEU LYS GLY ARG GLU LYS LEU ALA
SEQRES 14 A 180 PRO VAL PRO PHE PHE SER LEU LEU GLN TYR GLU
SEQRES 1 B 180 MET ALA ASP SER GLU LEU GLN LEU VAL GLU GLN ARG ILE
SEQRES 2 B 180 ARG SER PHE PRO ASP PHE PRO THR PRO GLY VAL VAL PHE
SEQRES 3 B 180 ARG ASP ILE SER PRO VAL LEU LYS ASP PRO ALA SER PHE
SEQRES 4 B 180 ARG ALA ALA ILE GLY LEU LEU ALA ARG HIS LEU LYS ALA
SEQRES 5 B 180 THR HIS GLY GLY ARG ILE ASP TYR ILE ALA GLY LEU ASP
SEQRES 6 B 180 SER ARG GLY PHE LEU PHE GLY PRO SER LEU ALA GLN GLU
SEQRES 7 B 180 LEU GLY LEU GLY CYS VAL LEU ILE ARG LYS ARG GLY LYS
SEQRES 8 B 180 LEU PRO GLY PRO THR LEU TRP ALA SER TYR SER LEU GLU
SEQRES 9 B 180 TYR GLY LYS ALA GLU LEU GLU ILE GLN LYS ASP ALA LEU
SEQRES 10 B 180 GLU PRO GLY GLN ARG VAL VAL VAL VAL ASP ASP LEU LEU
SEQRES 11 B 180 ALA THR GLY GLY THR MET ASN ALA ALA CYS GLU LEU LEU
SEQRES 12 B 180 GLY ARG LEU GLN ALA GLU VAL LEU GLU CYS VAL SER LEU
SEQRES 13 B 180 VAL GLU LEU THR SER LEU LYS GLY ARG GLU LYS LEU ALA
SEQRES 14 B 180 PRO VAL PRO PHE PHE SER LEU LEU GLN TYR GLU
HET AMP B1031 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 3 AMP C10 H14 N5 O7 P
FORMUL 4 HOH *273(H2 O)
HELIX 1 1 SER A 4 ARG A 12 1 9
HELIX 2 2 ILE A 29 ASP A 35 1 7
HELIX 3 3 ASP A 35 GLY A 55 1 21
HELIX 4 4 SER A 66 LEU A 70 5 5
HELIX 5 5 PHE A 71 GLY A 80 1 10
HELIX 6 6 GLY A 133 LEU A 146 1 14
HELIX 7 7 LYS A 163 ALA A 169 1 7
HELIX 8 8 ALA B 2 GLN B 11 1 10
HELIX 9 9 ILE B 29 ASP B 35 1 7
HELIX 10 10 ASP B 35 GLY B 55 1 21
HELIX 11 11 SER B 66 LEU B 70 5 5
HELIX 12 12 PHE B 71 GLY B 80 1 10
HELIX 13 13 GLY B 133 LEU B 146 1 14
HELIX 14 14 LYS B 163 ALA B 169 1 7
SHEET 1 A 2 ARG A 14 PRO A 17 0
SHEET 2 A 2 VAL A 25 ASP A 28 -1 O ASP A 28 N ARG A 14
SHEET 1 B 7 THR A 96 LEU A 103 0
SHEET 2 B 7 GLY A 106 GLN A 113 -1 O ALA A 108 N TYR A 101
SHEET 3 B 7 GLY A 82 LYS A 88 -1 N ARG A 87 O GLU A 111
SHEET 4 B 7 TYR A 60 LEU A 64 1 N ILE A 61 O VAL A 84
SHEET 5 B 7 ARG A 122 LEU A 130 1 O VAL A 124 N ALA A 62
SHEET 6 B 7 GLU A 149 LEU A 159 1 O VAL A 154 N VAL A 125
SHEET 7 B 7 PHE A 173 TYR A 179 1 O TYR A 179 N GLU A 158
SHEET 1 C 2 ARG B 14 PRO B 17 0
SHEET 2 C 2 VAL B 25 ASP B 28 -1 O ASP B 28 N ARG B 14
SHEET 1 D 7 THR B 96 SER B 102 0
SHEET 2 D 7 LYS B 107 GLN B 113 -1 O ALA B 108 N TYR B 101
SHEET 3 D 7 GLY B 82 LYS B 88 -1 N ARG B 87 O GLU B 111
SHEET 4 D 7 TYR B 60 LEU B 64 1 N ILE B 61 O VAL B 84
SHEET 5 D 7 ARG B 122 VAL B 126 1 O VAL B 126 N ALA B 62
SHEET 6 D 7 GLU B 149 LEU B 159 1 O VAL B 154 N VAL B 125
SHEET 7 D 7 LEU B 129 LEU B 130 1 N LEU B 130 O LEU B 159
SHEET 1 E 7 THR B 96 SER B 102 0
SHEET 2 E 7 LYS B 107 GLN B 113 -1 O ALA B 108 N TYR B 101
SHEET 3 E 7 GLY B 82 LYS B 88 -1 N ARG B 87 O GLU B 111
SHEET 4 E 7 TYR B 60 LEU B 64 1 N ILE B 61 O VAL B 84
SHEET 5 E 7 ARG B 122 VAL B 126 1 O VAL B 126 N ALA B 62
SHEET 6 E 7 GLU B 149 LEU B 159 1 O VAL B 154 N VAL B 125
SHEET 7 E 7 PHE B 173 TYR B 179 1 O LEU B 177 N LEU B 156
CISPEP 1 PHE A 19 PRO A 20 0 -0.36
CISPEP 2 ASP A 65 SER A 66 0 0.25
CISPEP 3 ALA A 169 PRO A 170 0 6.62
CISPEP 4 PHE B 19 PRO B 20 0 4.98
CISPEP 5 ASP B 65 SER B 66 0 -7.63
CISPEP 6 ALA B 169 PRO B 170 0 4.19
SITE 1 AC1 18 VAL B 25 PHE B 26 ARG B 27 ARG B 67
SITE 2 AC1 18 ASP B 127 ASP B 128 LEU B 129 ALA B 131
SITE 3 AC1 18 THR B 132 GLY B 133 GLY B 134 THR B 135
SITE 4 AC1 18 LEU B 159 HOH B1036 HOH B1084 HOH B1106
SITE 5 AC1 18 HOH B1116 HOH B1136
CRYST1 47.511 49.252 140.105 90.00 90.00 90.00 P 21 21 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 0.021048 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007138 0.00000
(ATOM LINES ARE NOT SHOWN.)
END