HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 13-JAN-03 1NNH
TITLE HYPOTHETICAL PROTEIN FROM PYROCOCCUS FURIOSUS PFU-1801964
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARAGINYL-TRNA SYNTHETASE-RELATED PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PYROCOCCUS FURIOSUS, ASPARAGINYL-TRNA SYNTHETASE, STRUCTURAL
KEYWDS 2 GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, SOUTHEAST COLLABORATORY
KEYWDS 3 FOR STRUCTURAL GENOMICS, SECSG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR W.TEMPEL,Z.-J.LIU,F.D.SCHUBOT,A.SHAH,W.B.ARENDALL III,J.P.ROSE,
AUTHOR 2 D.C.RICHARDSON,J.S.RICHARDSON,B.-C.WANG,SOUTHEAST COLLABORATORY FOR
AUTHOR 3 STRUCTURAL GENOMICS (SECSG)
REVDAT 6 14-FEB-24 1NNH 1 REMARK LINK
REVDAT 5 11-OCT-17 1NNH 1 REMARK
REVDAT 4 13-JUL-11 1NNH 1 VERSN
REVDAT 3 24-FEB-09 1NNH 1 VERSN
REVDAT 2 01-FEB-05 1NNH 1 AUTHOR KEYWDS REMARK
REVDAT 1 03-FEB-04 1NNH 0
JRNL AUTH SOUTHEAST COLLABORATORY FOR STRUCTURAL GENOMICS
JRNL TITL HYPOTHETICAL PROTEIN FROM PYROCOCCUS FURIOSUS PFU-1801964
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 41501
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) : 0.171
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2086
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2900
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE SET COUNT : 175
REMARK 3 BIN FREE R VALUE : 0.2110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2340
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : -0.16000
REMARK 3 B33 (A**2) : 0.33000
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): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2414 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2246 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3266 ; 1.390 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5203 ; 3.657 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 292 ; 5.992 ; 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): 349 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2659 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 513 ; 0.007 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 620 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2302 ; 0.272 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1577 ; 0.136 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; 0.107 ; 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): 23 ; 0.255 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 51 ; 0.272 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.070 ; 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): 1463 ; 0.641 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2365 ; 1.171 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 951 ; 1.942 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 901 ; 3.220 ; 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 1NNH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 6
REMARK 6 THE PROTEIN WAS CLONED, EXPRESSED AND PURIFIED BY THE SECSG
REMARK 6 PYROCOCCUS PROTEIN PRODUCTION GROUP (M.W.W.ADAMS,
REMARK 6 P.S.BRERETON, M.IZUMI, F.E.JENNEY JR., H.-S.LEE, F.L.POOLE
REMARK 6 II, C.SHAH, F.SUGAR) UNDER THE DIRECTION OF M.W.W.ADAMS.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018033.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.00
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) : 1.04
REMARK 200 MONOCHROMATOR : SI 220 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41526
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 550 MME, SODIUM CHLORIDE, BICINE,
REMARK 280 PH 9, MODIFIED MICROBATCH, TEMPERATURE 291K, PH 9.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 34.26450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 34.26450
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.34200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.26450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.67100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.26450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.01300
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.26450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.26450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 75.34200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 34.26450
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 113.01300
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 34.26450
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.67100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN. THE BIOLOGICAL UNIT IS UNKNOWN.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 68.52900
REMARK 350 BIOMT3 2 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 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 2 CB CG OD1 ND2
REMARK 470 GLU A 5 CG CD OE1 OE2
REMARK 470 GLU A 10 CB CG CD OE1 OE2
REMARK 470 ARG A 103 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 GLU A 168 CG CD OE1 OE2
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 GLU A 179 CD OE1 OE2
REMARK 470 GLU A 181 CD OE1 OE2
REMARK 470 LYS A 235 CD CE NZ
REMARK 470 ASN A 239 CG OD1 ND2
REMARK 470 ASP A 241 CG OD1 OD2
REMARK 470 ARG A 244 CD NE CZ NH1 NH2
REMARK 470 GLU A 248 CD OE1 OE2
REMARK 470 LYS A 251 NZ
REMARK 470 LYS A 276 CD CE NZ
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 52 119.14 -170.77
REMARK 500 LYS A 89 -57.77 73.91
REMARK 500 ASN A 188 62.71 65.29
REMARK 500 ARG A 191 -129.10 -154.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2012 O
REMARK 620 2 HOH A2026 O 91.2
REMARK 620 3 HOH A2029 O 88.2 93.1
REMARK 620 4 HOH A2031 O 176.3 86.8 88.8
REMARK 620 5 HOH A2037 O 90.7 174.5 92.1 91.5
REMARK 620 6 HOH A2039 O 89.7 91.0 175.4 93.5 83.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PFU-1801964-001 RELATED DB: TARGETDB
DBREF 1NNH A 1 294 UNP Q8TZN6 Q8TZN6_PYRFU 1 294
SEQRES 1 A 294 MET ASN ALA VAL GLU ILE ILE SER ARG GLU ILE SER PRO
SEQRES 2 A 294 THR LEU ASP ILE GLN THR LYS ILE LEU GLU TYR MET THR
SEQRES 3 A 294 ASP PHE PHE VAL LYS GLU GLY PHE LYS TRP LEU LEU PRO
SEQRES 4 A 294 VAL ILE ILE SER PRO ILE THR ASP PRO LEU TRP PRO ASP
SEQRES 5 A 294 PRO ALA GLY GLU GLY MET GLU PRO ALA GLU VAL GLU ILE
SEQRES 6 A 294 TYR GLY VAL LYS MET ARG LEU THR HIS SER MET ILE LEU
SEQRES 7 A 294 HIS LYS GLN LEU ALA ILE ALA MET GLY LEU LYS LYS ILE
SEQRES 8 A 294 PHE VAL LEU SER PRO ASN ILE ARG LEU GLU SER ARG GLN
SEQRES 9 A 294 LYS ASP ASP GLY ARG HIS ALA TYR GLU PHE THR GLN LEU
SEQRES 10 A 294 ASP PHE GLU VAL GLU ARG ALA LYS MET GLU ASP ILE MET
SEQRES 11 A 294 ARG LEU ILE GLU ARG LEU VAL TYR GLY LEU PHE ARG LYS
SEQRES 12 A 294 ALA GLU GLU TRP THR GLY ARG GLU PHE PRO LYS THR LYS
SEQRES 13 A 294 ARG PHE GLU VAL PHE GLU TYR SER GLU VAL LEU GLU GLU
SEQRES 14 A 294 PHE GLY SER ASP GLU LYS ALA SER GLN GLU MET GLU GLU
SEQRES 15 A 294 PRO PHE TRP ILE ILE ASN ILE PRO ARG GLU PHE TYR ASP
SEQRES 16 A 294 ARG GLU VAL ASP GLY PHE TRP ARG ASN TYR ASP LEU ILE
SEQRES 17 A 294 LEU PRO TYR GLY TYR GLY GLU VAL ALA SER GLY GLY GLU
SEQRES 18 A 294 ARG GLU TRP GLU TYR GLU LYS ILE VAL ALA LYS ILE ARG
SEQRES 19 A 294 LYS ALA GLY LEU ASN GLU ASP SER PHE ARG PRO TYR LEU
SEQRES 20 A 294 GLU ILE ALA LYS ALA GLY LYS LEU LYS PRO SER ALA GLY
SEQRES 21 A 294 ALA GLY ILE GLY VAL GLU ARG LEU VAL ARG PHE ILE VAL
SEQRES 22 A 294 GLY ALA LYS HIS ILE ALA GLU VAL GLN PRO PHE PRO ARG
SEQRES 23 A 294 ILE PRO GLY ILE PRO ALA VAL ILE
HET NA A2001 1
HETNAM NA SODIUM ION
FORMUL 2 NA NA 1+
FORMUL 3 HOH *148(H2 O)
HELIX 1 1 ASN A 2 SER A 8 1 7
HELIX 2 2 ILE A 11 GLU A 32 1 22
HELIX 3 3 MET A 76 MET A 86 1 11
HELIX 4 4 SER A 102 ASP A 106 5 5
HELIX 5 5 LYS A 125 GLY A 149 1 25
HELIX 6 6 TYR A 163 PHE A 170 1 8
HELIX 7 7 SER A 172 MET A 180 1 9
HELIX 8 8 GLU A 225 ALA A 236 1 12
HELIX 9 9 ASN A 239 SER A 242 5 4
HELIX 10 10 PHE A 243 ALA A 252 1 10
HELIX 11 11 VAL A 265 GLY A 274 1 10
HELIX 12 12 HIS A 277 GLN A 282 5 6
SHEET 1 A 8 LYS A 35 TRP A 36 0
SHEET 2 A 8 LYS A 90 ILE A 98 1 O LYS A 90 N LYS A 35
SHEET 3 A 8 GLU A 113 GLU A 122 -1 O GLN A 116 N SER A 95
SHEET 4 A 8 SER A 258 GLY A 264 -1 O ALA A 261 N PHE A 119
SHEET 5 A 8 GLY A 214 GLU A 221 -1 N SER A 218 O GLY A 262
SHEET 6 A 8 ASN A 204 LEU A 209 -1 N LEU A 207 O VAL A 216
SHEET 7 A 8 PHE A 184 ILE A 187 -1 N PHE A 184 O ILE A 208
SHEET 8 A 8 GLU A 159 GLU A 162 1 N GLU A 159 O TRP A 185
SHEET 1 B 3 ILE A 42 SER A 43 0
SHEET 2 B 3 VAL A 68 LEU A 72 -1 O ARG A 71 N SER A 43
SHEET 3 B 3 GLU A 62 ILE A 65 -1 N ILE A 65 O VAL A 68
SHEET 1 C 2 GLU A 197 VAL A 198 0
SHEET 2 C 2 PHE A 201 TRP A 202 -1 O PHE A 201 N VAL A 198
LINK NA NA A2001 O HOH A2012 1555 1555 2.15
LINK NA NA A2001 O HOH A2026 1555 6665 2.08
LINK NA NA A2001 O HOH A2029 1555 6665 2.19
LINK NA NA A2001 O HOH A2031 1555 6665 2.13
LINK NA NA A2001 O HOH A2037 1555 1555 2.08
LINK NA NA A2001 O HOH A2039 1555 1555 2.16
CISPEP 1 TRP A 50 PRO A 51 0 -10.04
SITE 1 AC1 6 HOH A2012 HOH A2026 HOH A2029 HOH A2031
SITE 2 AC1 6 HOH A2037 HOH A2039
CRYST1 68.529 68.529 150.684 90.00 90.00 90.00 I 41 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 0.014592 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014592 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006636 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
