HEADER RIBOSOME 17-JUN-04 1TQM
TITLE CRYSTAL STRUCTURE OF A. FULGIDUS RIO2 SERINE PROTEIN KINASE BOUND TO
TITLE 2 AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RIO2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 224325;
SOURCE 4 STRAIN: DSM 4304;
SOURCE 5 GENE: RIO2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST14
KEYWDS SERINE KINASE, AMPPNP, ANP, RIBOSOME
EXPDTA X-RAY DIFFRACTION
AUTHOR N.LARONDE-LEBLANC,A.WLODAWER
REVDAT 4 23-AUG-23 1TQM 1 REMARK
REVDAT 3 13-JUL-11 1TQM 1 VERSN
REVDAT 2 24-FEB-09 1TQM 1 VERSN
REVDAT 1 28-SEP-04 1TQM 0
JRNL AUTH N.LARONDE-LEBLANC,A.WLODAWER
JRNL TITL CRYSTAL STRUCTURE OF A. FULGIDUS RIO2 DEFINES A NEW FAMILY
JRNL TITL 2 OF SERINE PROTEIN KINASES
JRNL REF STRUCTURE V. 12 1585 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15341724
JRNL DOI 10.1016/J.STR.2004.06.016
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 20313
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1106
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) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1347
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2185
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.353
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2260 ; 0.028 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2053 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3053 ; 2.067 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4747 ; 1.023 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ;10.287 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 331 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2486 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 487 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 503 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2318 ; 0.255 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1295 ; 0.092 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.230 ; 0.200
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): 16 ; 0.205 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 53 ; 0.270 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.282 ; 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): 1330 ; 1.466 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2136 ; 2.637 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 930 ; 4.032 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 917 ; 6.552 ; 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 : BABINET MODEL WITH 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 1TQM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.83
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99998
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20313
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.12500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: PDB ENTRY 1TQI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 900, SODIUM PHOSPHATE, SODIUM
REMARK 280 CITRATE, PH 3.83, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 58.08250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.12950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.08250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.12950
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 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 A 332 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 451 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 GLY A 125
REMARK 465 HIS A 126
REMARK 465 THR A 127
REMARK 465 SER A 128
REMARK 465 PHE A 129
REMARK 465 LYS A 130
REMARK 465 LYS A 135
REMARK 465 ARG A 136
REMARK 465 ASP A 137
REMARK 465 TYR A 138
REMARK 465 GLY A 139
REMARK 465 ASP A 140
REMARK 465 LEU A 141
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 GLU A 5 CG CD OE1 OE2
REMARK 470 LYS A 12 CD CE NZ
REMARK 470 ARG A 63 CD NE CZ NH1 NH2
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 131 CG CD CE NZ
REMARK 470 LYS A 133 CG CD CE NZ
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 MET A 98 SD MET A 98 CE -0.437
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 19 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 196 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 248 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 248 NE - CZ - NH2 ANGL. DEV. = -3.2 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 218 33.25 -154.08
REMARK 500 ASP A 235 72.31 79.39
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 GLY A 243 GLU A 244 132.14
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 ANP A 283
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TQI RELATED DB: PDB
REMARK 900 RELATED ID: 1TQP RELATED DB: PDB
DBREF 1TQM A 1 282 UNP O30245 O30245_ARCFU 1 282
SEQRES 1 A 282 MET ASN ILE ALA GLU LEU TYR GLY LYS MET GLY LYS HIS
SEQRES 2 A 282 SER TRP ARG ILE MET ASP ALA ILE PHE LYS ASN LEU TRP
SEQRES 3 A 282 ASP TYR GLU TYR VAL PRO LEU GLN LEU ILE SER SER HIS
SEQRES 4 A 282 ALA ARG ILE GLY GLU GLU LYS ALA ARG ASN ILE LEU LYS
SEQRES 5 A 282 TYR LEU SER ASP LEU ARG VAL VAL GLN ASN ARG GLN LYS
SEQRES 6 A 282 ASP TYR GLU GLY SER THR PHE THR PHE ILE GLY LEU SER
SEQRES 7 A 282 LEU TYR SER LEU HIS ARG LEU VAL ARG SER GLY LYS VAL
SEQRES 8 A 282 ASP ALA ILE GLY LYS LEU MET GLY GLU GLY LYS GLU SER
SEQRES 9 A 282 ALA VAL PHE ASN CYS TYR SER GLU LYS PHE GLY GLU CYS
SEQRES 10 A 282 VAL VAL LYS PHE HIS LYS VAL GLY HIS THR SER PHE LYS
SEQRES 11 A 282 LYS VAL LYS GLU LYS ARG ASP TYR GLY ASP LEU HIS PHE
SEQRES 12 A 282 SER VAL LEU ALA ILE ARG SER ALA ARG ASN GLU PHE ARG
SEQRES 13 A 282 ALA LEU GLN LYS LEU GLN GLY LEU ALA VAL PRO LYS VAL
SEQRES 14 A 282 TYR ALA TRP GLU GLY ASN ALA VAL LEU MET GLU LEU ILE
SEQRES 15 A 282 ASP ALA LYS GLU LEU TYR ARG VAL ARG VAL GLU ASN PRO
SEQRES 16 A 282 ASP GLU VAL LEU ASP MET ILE LEU GLU GLU VAL ALA LYS
SEQRES 17 A 282 PHE TYR HIS ARG GLY ILE VAL HIS GLY ASP LEU SER GLN
SEQRES 18 A 282 TYR ASN VAL LEU VAL SER GLU GLU GLY ILE TRP ILE ILE
SEQRES 19 A 282 ASP PHE PRO GLN SER VAL GLU VAL GLY GLU GLU GLY TRP
SEQRES 20 A 282 ARG GLU ILE LEU GLU ARG ASP VAL ARG ASN ILE ILE THR
SEQRES 21 A 282 TYR PHE SER ARG THR TYR ARG THR GLU LYS ASP ILE ASN
SEQRES 22 A 282 SER ALA ILE ASP ARG ILE LEU GLN GLU
HET ANP A 283 31
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 2 ANP C10 H17 N6 O12 P3
FORMUL 3 HOH *197(H2 O)
HELIX 1 1 ASN A 2 LYS A 9 1 8
HELIX 2 2 GLY A 11 LYS A 23 1 13
HELIX 3 3 LEU A 33 ARG A 41 1 9
HELIX 4 4 GLY A 43 LEU A 57 1 15
HELIX 5 5 THR A 73 SER A 88 1 16
HELIX 6 6 HIS A 142 LEU A 161 1 20
HELIX 7 7 TYR A 188 VAL A 190 5 3
HELIX 8 8 ASN A 194 ARG A 212 1 19
HELIX 9 9 GLY A 246 ARG A 267 1 22
HELIX 10 10 ASP A 271 GLU A 282 1 12
SHEET 1 A 3 VAL A 31 PRO A 32 0
SHEET 2 A 3 GLY A 69 PHE A 72 -1 O SER A 70 N VAL A 31
SHEET 3 A 3 VAL A 60 ARG A 63 -1 N GLN A 61 O THR A 71
SHEET 1 B 5 ALA A 93 GLU A 100 0
SHEET 2 B 5 SER A 104 SER A 111 -1 O VAL A 106 N MET A 98
SHEET 3 B 5 GLY A 115 HIS A 122 -1 O PHE A 121 N ALA A 105
SHEET 4 B 5 ALA A 176 GLU A 180 -1 O MET A 179 N VAL A 118
SHEET 5 B 5 VAL A 169 GLU A 173 -1 N TYR A 170 O LEU A 178
SHEET 1 C 3 LYS A 185 GLU A 186 0
SHEET 2 C 3 VAL A 224 SER A 227 -1 O VAL A 226 N LYS A 185
SHEET 3 C 3 GLY A 230 ILE A 233 -1 O TRP A 232 N LEU A 225
SHEET 1 D 2 ILE A 214 VAL A 215 0
SHEET 2 D 2 VAL A 240 GLU A 241 -1 O VAL A 240 N VAL A 215
SITE 1 AC1 22 MET A 98 GLU A 103 SER A 104 LYS A 120
SITE 2 AC1 22 MET A 179 GLU A 180 ILE A 182 GLU A 186
SITE 3 AC1 22 TYR A 222 ASN A 223 ILE A 234 ASP A 235
SITE 4 AC1 22 HOH A 284 HOH A 313 HOH A 340 HOH A 368
SITE 5 AC1 22 HOH A 375 HOH A 398 HOH A 405 HOH A 423
SITE 6 AC1 22 HOH A 443 HOH A 461
CRYST1 116.165 44.259 62.097 90.00 94.38 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 0.008608 0.000000 0.000660 0.00000
SCALE2 0.000000 0.022594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
