HEADER TRANSFERASE 28-DEC-01 1GS5
TITLE N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS
TITLE 2 SUBSTRATE N-ACETYLGLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLGLUTAMATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NAG KINASE, AGK, N-ACETYL-L-GLUTAMATE 5-PHOSPHOTRANSFERASE;
COMPND 5 EC: 2.7.2.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 469008;
SOURCE 4 STRAIN: BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-15B;
SOURCE 9 OTHER_DETAILS: NOVAGEN
KEYWDS CARBAMATE KINASE, AMINO ACID KINASE, ARGININE BIOSYNTHESIS,
KEYWDS 2 PHOSPHORYL GROUP TRANSFER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RAMON-MAIQUES,A.MARINA,F.GIL-ORTIZ,I.FITA,V.RUBIO
REVDAT 4 13-DEC-23 1GS5 1 REMARK LINK
REVDAT 3 05-FEB-14 1GS5 1 HEADER SOURCE KEYWDS REMARK
REVDAT 3 2 1 VERSN FORMUL SITE
REVDAT 2 24-FEB-09 1GS5 1 VERSN
REVDAT 1 16-MAY-02 1GS5 0
JRNL AUTH S.RAMON-MAIQUES,A.MARINA,F.GIL-ORTIZ,I.FITA,V.RUBIO
JRNL TITL STRUCTURE OF ACETYLGLUTAMATE KINASE, A KEY ENZYME FOR
JRNL TITL 2 ARGININE BIOSYNTHESIS AND A PROTOTYPE FOR THE AMINO ACID
JRNL TITL 3 KINASE ENZYME FAMILY, DURING CATALYSIS
JRNL REF STRUCTURE V. 10 329 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12005432
JRNL DOI 10.1016/S0969-2126(02)00721-9
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 35599
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1883
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1903
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.600
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NONE
REMARK 4
REMARK 4 1GS5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1290009174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37460
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 53.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GSJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-32% PEG MONOMETHYLETHER 2000, 0.1
REMARK 280 -0.3M AMMONIUM SULFATE, 5% ETHYLENE GLYCOL, 0.1M SODIUM ACETATE
REMARK 280 PH 4.6, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 53.70900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.70900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.78200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.16600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.78200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.16600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.70900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.78200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 36.16600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.70900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.78200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 36.16600
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 59.56400
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 53.70900
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 OD1 ASP A 212 N GLY A 213 1.24
REMARK 500 O HOH A 2189 O HOH A 2191 1.51
REMARK 500 OE1 GLU A 138 O HOH A 2118 1.81
REMARK 500 O HOH A 2179 O HOH A 2180 1.92
REMARK 500 O ILE A 75 O HOH A 2064 1.96
REMARK 500 O HOH A 2162 O HOH A 2163 2.00
REMARK 500 OE1 GLU A 138 O HOH A 2117 2.08
REMARK 500 O HOH A 2061 O HOH A 2062 2.16
REMARK 500 O HOH A 2018 O HOH A 2062 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 MET A 1 CG MET A 1 SD 0.160
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 22 CD - NE - CZ ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 HIS A 95 CE1 - NE2 - CD2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 PHE A 103 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 192 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 GLU A 202 CG - CD - OE1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 VAL A 218 O - C - N ANGL. DEV. = -9.8 DEGREES
REMARK 500 ASP A 233 O - C - N ANGL. DEV. = 11.0 DEGREES
REMARK 500 ILE A 234 O - C - N ANGL. DEV. = -10.0 DEGREES
REMARK 500 GLU A 241 OE1 - CD - OE2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 MET A 250 CG - SD - CE ANGL. DEV. = 10.5 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 ASN A 56 38.28 70.36
REMARK 500 ASP A 212 -129.56 53.62
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 MG A1261 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A1260 O2G
REMARK 620 2 ANP A1260 O2A 94.0
REMARK 620 3 ANP A1260 O1B 80.5 89.0
REMARK 620 4 HOH A2135 O 166.7 97.3 106.4
REMARK 620 5 HOH A2195 O 82.5 175.0 86.9 86.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NLG A 1259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 1260
DBREF 1GS5 A 1 258 UNP P11445 ARGB_ECOLI 1 258
SEQRES 1 A 258 MET MET ASN PRO LEU ILE ILE LYS LEU GLY GLY VAL LEU
SEQRES 2 A 258 LEU ASP SER GLU GLU ALA LEU GLU ARG LEU PHE SER ALA
SEQRES 3 A 258 LEU VAL ASN TYR ARG GLU SER HIS GLN ARG PRO LEU VAL
SEQRES 4 A 258 ILE VAL HIS GLY GLY GLY CYS VAL VAL ASP GLU LEU MET
SEQRES 5 A 258 LYS GLY LEU ASN LEU PRO VAL LYS LYS LYS ASN GLY LEU
SEQRES 6 A 258 ARG VAL THR PRO ALA ASP GLN ILE ASP ILE ILE THR GLY
SEQRES 7 A 258 ALA LEU ALA GLY THR ALA ASN LYS THR LEU LEU ALA TRP
SEQRES 8 A 258 ALA LYS LYS HIS GLN ILE ALA ALA VAL GLY LEU PHE LEU
SEQRES 9 A 258 GLY ASP GLY ASP SER VAL LYS VAL THR GLN LEU ASP GLU
SEQRES 10 A 258 GLU LEU GLY HIS VAL GLY LEU ALA GLN PRO GLY SER PRO
SEQRES 11 A 258 LYS LEU ILE ASN SER LEU LEU GLU ASN GLY TYR LEU PRO
SEQRES 12 A 258 VAL VAL SER SER ILE GLY VAL THR ASP GLU GLY GLN LEU
SEQRES 13 A 258 MET ASN VAL ASN ALA ASP GLN ALA ALA THR ALA LEU ALA
SEQRES 14 A 258 ALA THR LEU GLY ALA ASP LEU ILE LEU LEU SER ASP VAL
SEQRES 15 A 258 SER GLY ILE LEU ASP GLY LYS GLY GLN ARG ILE ALA GLU
SEQRES 16 A 258 MET THR ALA ALA LYS ALA GLU GLN LEU ILE GLU GLN GLY
SEQRES 17 A 258 ILE ILE THR ASP GLY MET ILE VAL LYS VAL ASN ALA ALA
SEQRES 18 A 258 LEU ASP ALA ALA ARG THR LEU GLY ARG PRO VAL ASP ILE
SEQRES 19 A 258 ALA SER TRP ARG HIS ALA GLU GLN LEU PRO ALA LEU PHE
SEQRES 20 A 258 ASN GLY MET PRO MET GLY THR ARG ILE LEU ALA
HET NLG A1259 13
HET ANP A1260 31
HET MG A1261 1
HETNAM NLG N-ACETYL-L-GLUTAMATE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 2 NLG C7 H11 N O5
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 MG MG 2+
FORMUL 5 HOH *198(H2 O)
HELIX 1 1 GLY A 11 ASP A 15 5 5
HELIX 2 2 SER A 16 GLU A 32 1 17
HELIX 3 3 GLY A 44 ASN A 56 1 13
HELIX 4 4 PRO A 69 GLY A 82 1 14
HELIX 5 5 GLY A 82 HIS A 95 1 14
HELIX 6 6 GLY A 105 ASP A 108 5 4
HELIX 7 7 ASP A 116 LEU A 119 5 4
HELIX 8 8 PRO A 130 ASN A 139 1 10
HELIX 9 9 ASN A 160 GLY A 173 1 14
HELIX 10 10 THR A 197 GLN A 207 1 11
HELIX 11 11 ASP A 212 GLY A 229 1 18
HELIX 12 12 HIS A 239 GLU A 241 5 3
HELIX 13 13 GLN A 242 ASN A 248 1 7
SHEET 1 AA 8 ALA A 99 LEU A 102 0
SHEET 2 AA 8 LEU A 142 VAL A 145 1 O LEU A 142 N VAL A 100
SHEET 3 AA 8 LEU A 38 HIS A 42 1 O ILE A 40 N VAL A 145
SHEET 4 AA 8 LEU A 5 LEU A 9 1 O LEU A 5 N VAL A 39
SHEET 5 AA 8 ASP A 175 SER A 180 1 O ASP A 175 N ILE A 6
SHEET 6 AA 8 VAL A 232 SER A 236 1 O ASP A 233 N LEU A 178
SHEET 7 AA 8 THR A 254 ILE A 256 -1 O THR A 254 N ILE A 234
SHEET 8 AA 8 GLU A 195 MET A 196 1 N MET A 196 O ARG A 255
SHEET 1 AB 2 LYS A 61 LYS A 62 0
SHEET 2 AB 2 LEU A 65 ARG A 66 -1 O LEU A 65 N LYS A 62
SHEET 1 AC 2 VAL A 110 GLN A 114 0
SHEET 2 AC 2 GLY A 123 PRO A 127 -1 O LEU A 124 N THR A 113
SHEET 1 AD 2 ILE A 148 VAL A 150 0
SHEET 2 AD 2 LEU A 156 ASN A 158 -1 O MET A 157 N GLY A 149
LINK O2G ANP A1260 MG MG A1261 1555 1555 2.77
LINK O2A ANP A1260 MG MG A1261 1555 1555 2.13
LINK O1B ANP A1260 MG MG A1261 1555 1555 2.18
LINK MG MG A1261 O HOH A2135 1555 1555 2.65
LINK MG MG A1261 O HOH A2195 1555 1555 2.51
SITE 1 AC1 3 ANP A1260 HOH A2135 HOH A2195
SITE 1 AC2 14 GLY A 43 GLY A 44 GLY A 45 LEU A 65
SITE 2 AC2 14 ARG A 66 LEU A 80 ASN A 158 VAL A 159
SITE 3 AC2 14 ASN A 160 ALA A 161 ANP A1260 HOH A2194
SITE 4 AC2 14 HOH A2195 HOH A2196
SITE 1 AC3 18 LYS A 8 GLY A 10 GLY A 11 GLY A 43
SITE 2 AC3 18 GLY A 44 GLY A 45 SER A 180 VAL A 182
SITE 3 AC3 18 LEU A 186 ILE A 209 ILE A 210 THR A 211
SITE 4 AC3 18 MET A 214 LYS A 217 NLG A1259 MG A1261
SITE 5 AC3 18 HOH A2197 HOH A2198
CRYST1 59.564 72.332 107.418 90.00 90.00 90.00 C 2 2 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 0.016789 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009309 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
