HEADER HYDROLASE 05-MAR-01 1I6T
TITLE STRUCTURE OF INORGANIC PYROPHOSPHATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INORGANIC PYROPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS HYDROLASE, INORGANIC PYROPHOSPHATASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.R.SAMYGINA,A.N.POPOV,V.S.LAMZIN,S.M.AVAEVA
REVDAT 6 09-AUG-23 1I6T 1 REMARK LINK
REVDAT 5 04-OCT-17 1I6T 1 REMARK
REVDAT 4 13-JUL-11 1I6T 1 VERSN
REVDAT 3 24-FEB-09 1I6T 1 VERSN
REVDAT 2 01-APR-03 1I6T 1 JRNL
REVDAT 1 05-DEC-01 1I6T 0
JRNL AUTH V.R.SAMYGINA,A.N.POPOV,E.V.RODINA,N.N.VOROBYEVA,V.S.LAMZIN,
JRNL AUTH 2 K.M.POLYAKOV,S.A.KURILOVA,T.I.NAZAROVA,S.M.AVAEVA
JRNL TITL THE STRUCTURES OF ESCHERICHIA COLI INORGANIC PYROPHOSPHATASE
JRNL TITL 2 COMPLEXED WITH CA(2+) OR CAPP(I) AT ATOMIC RESOLUTION AND
JRNL TITL 3 THEIR MECHANISTIC IMPLICATIONS.
JRNL REF J.MOL.BIOL. V. 314 633 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11846572
JRNL DOI 10.1006/JMBI.2001.5149
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.129
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.129
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 259
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 49270
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.121
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.121
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 220
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 4163
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 254
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1577.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1247.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 2
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 1487
REMARK 3 NUMBER OF RESTRAINTS : 1830
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.090
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.090
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.020
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.060
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.090
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I6T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.906
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 640235
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : 0.02600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.44100
REMARK 200 R SYM FOR SHELL (I) : 53.5000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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 1IGP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, PH 5.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 54.67800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 31.56836
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 25.19400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 54.67800
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 31.56836
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 25.19400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 54.67800
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 31.56836
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 25.19400
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 54.67800
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 31.56836
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 25.19400
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 54.67800
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 31.56836
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 25.19400
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 54.67800
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 31.56836
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 25.19400
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 63.13672
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 50.38800
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 63.13672
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 50.38800
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 63.13672
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 50.38800
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 63.13672
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 50.38800
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 63.13672
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 50.38800
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 63.13672
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 50.38800
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATION:-Y, X-Y, Z AND -X+Y,
REMARK 300 -X, Z AND Y, X, -Z AND X-Y, -Y, -Z AND -X, -X+Y, -Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -622.0 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 -0.500000 -0.866025 0.000000 164.03400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 94.70507
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 189.41015
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 75.58200
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 189.41015
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 75.58200
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 164.03400
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 94.70507
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 75.58200
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 573 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 593 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 638 LIES ON A SPECIAL POSITION.
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 ASN A 4 C VAL A 5 N 0.169
REMARK 500 CYS A 53 CB CYS A 53 SG -0.127
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 VAL A 5 C - N - CA ANGL. DEV. = -20.5 DEGREES
REMARK 500 LEU A 11 CA - CB - CG ANGL. DEV. = 23.9 DEGREES
REMARK 500 ASP A 33 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 MET A 45 CA - CB - CG ANGL. DEV. = 22.5 DEGREES
REMARK 500 TYR A 57 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 GLN A 80 CG - CD - OE1 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 HIS A 110 CG - ND1 - CE1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 118 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASN A 124 CB - CG - OD1 ANGL. DEV. = 13.9 DEGREES
REMARK 500 LYS A 146 CA - C - N ANGL. DEV. = 14.6 DEGREES
REMARK 500 LYS A 146 O - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = 3.9 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 10 76.50 -160.27
REMARK 500 ASP A 97 -162.40 -122.37
REMARK 500 ASP A 102 82.78 -156.70
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 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 24 O
REMARK 620 2 HOH A 420 O 83.7
REMARK 620 3 HOH A 439 O 99.3 98.8
REMARK 620 4 HOH A 471 O 99.2 99.8 155.0
REMARK 620 5 HOH A 471 O 111.9 164.5 79.4 78.2
REMARK 620 6 HOH A 573 O 166.0 82.3 82.9 83.2 82.2
REMARK 620 7 HOH A 573 O 166.0 82.3 82.9 83.2 82.2 0.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 65 OD1
REMARK 620 2 ASP A 70 OD1 138.7
REMARK 620 3 ASP A 70 OD2 161.4 47.9
REMARK 620 4 ASP A 102 OD1 84.3 114.6 78.2
REMARK 620 5 ASP A 102 OD2 92.4 128.4 81.7 51.5
REMARK 620 6 POP A 411 O2 103.2 96.0 91.9 123.7 72.3
REMARK 620 7 HOH A 436 O 79.4 71.7 115.9 159.3 141.4 73.0
REMARK 620 8 HOH A 437 O 78.5 71.6 91.1 76.3 127.7 159.9 87.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 70 OD1
REMARK 620 2 POP A 411 O1 94.7
REMARK 620 3 HOH A 418 O 88.0 105.5
REMARK 620 4 HOH A 426 O 87.7 168.8 85.5
REMARK 620 5 HOH A 435 O 167.2 88.7 79.2 91.4
REMARK 620 6 HOH A 436 O 85.1 82.9 169.6 86.4 107.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 97 OD2
REMARK 620 2 ASP A 102 OD2 97.1
REMARK 620 3 POP A 411 O2 157.9 72.3
REMARK 620 4 POP A 411 O5 98.1 146.6 82.6
REMARK 620 5 HOH A 481 O 76.0 75.9 82.5 79.2
REMARK 620 6 HOH A 524 O 78.9 132.6 122.7 79.7 144.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 142 O
REMARK 620 2 GLU A 145 O 91.8
REMARK 620 3 LYS A 148 O 94.8 87.8
REMARK 620 4 HOH A 450 O 87.5 174.7 87.1
REMARK 620 5 HOH A 462 O 99.9 86.2 164.3 99.0
REMARK 620 6 HOH A 549 O 178.6 87.8 83.8 92.7 81.5
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 CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 411
DBREF 1I6T A 1 175 UNP P0A7A9 IPYR_ECOLI 1 175
SEQADV 1I6T THR A 85 UNP P0A7A9 ILE 85 SEE REMARK 999
SEQRES 1 A 175 SER LEU LEU ASN VAL PRO ALA GLY LYS ASP LEU PRO GLU
SEQRES 2 A 175 ASP ILE TYR VAL VAL ILE GLU ILE PRO ALA ASN ALA ASP
SEQRES 3 A 175 PRO ILE LYS TYR GLU ILE ASP LYS GLU SER GLY ALA LEU
SEQRES 4 A 175 PHE VAL ASP ARG PHE MET SER THR ALA MET PHE TYR PRO
SEQRES 5 A 175 CYS ASN TYR GLY TYR ILE ASN HIS THR LEU SER LEU ASP
SEQRES 6 A 175 GLY ASP PRO VAL ASP VAL LEU VAL PRO THR PRO TYR PRO
SEQRES 7 A 175 LEU GLN PRO GLY SER VAL THR ARG CYS ARG PRO VAL GLY
SEQRES 8 A 175 VAL LEU LYS MET THR ASP GLU ALA GLY GLU ASP ALA LYS
SEQRES 9 A 175 LEU VAL ALA VAL PRO HIS SER LYS LEU SER LYS GLU TYR
SEQRES 10 A 175 ASP HIS ILE LYS ASP VAL ASN ASP LEU PRO GLU LEU LEU
SEQRES 11 A 175 LYS ALA GLN ILE ALA HIS PHE PHE GLU HIS TYR LYS ASP
SEQRES 12 A 175 LEU GLU LYS GLY LYS TRP VAL LYS VAL GLU GLY TRP GLU
SEQRES 13 A 175 ASN ALA GLU ALA ALA LYS ALA GLU ILE VAL ALA SER PHE
SEQRES 14 A 175 GLU ARG ALA LYS ASN LYS
HET CA A 301 1
HET CA A 302 1
HET CA A 303 1
HET CA A 304 1
HET NA A 305 1
HET CL A 310 1
HET CL A 311 1
HET CL A 312 1
HET POP A 411 9
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM POP PYROPHOSPHATE 2-
FORMUL 2 CA 4(CA 2+)
FORMUL 6 NA NA 1+
FORMUL 7 CL 3(CL 1-)
FORMUL 10 POP H2 O7 P2 2-
FORMUL 11 HOH *254(H2 O)
HELIX 1 1 SER A 1 VAL A 5 5 5
HELIX 2 2 ASP A 122 LEU A 126 5 5
HELIX 3 3 PRO A 127 TYR A 141 1 15
HELIX 4 4 ASN A 157 ASN A 174 1 18
SHEET 1 A 2 ILE A 28 ILE A 32 0
SHEET 2 A 2 LEU A 39 PHE A 44 -1 N PHE A 40 O GLU A 31
SHEET 1 B10 VAL A 150 GLU A 156 0
SHEET 2 B10 VAL A 84 ASP A 97 -1 O VAL A 92 N GLU A 156
SHEET 3 B10 ILE A 15 ILE A 21 -1 O ILE A 15 N CYS A 87
SHEET 4 B10 ASN A 54 TYR A 57 -1 O TYR A 55 N GLU A 20
SHEET 5 B10 ASP A 70 VAL A 73 -1 O VAL A 71 N GLY A 56
SHEET 6 B10 LYS A 104 PRO A 109 1 O LEU A 105 N LEU A 72
SHEET 7 B10 VAL A 84 ASP A 97 -1 O ARG A 88 N VAL A 108
SHEET 8 B10 GLY A 100 GLU A 101 -1 O GLY A 100 N ASP A 97
SHEET 9 B10 VAL A 84 ASP A 97 -1 N ASP A 97 O GLY A 100
SHEET 10 B10 VAL A 150 GLU A 156 -1 N LYS A 151 O THR A 96
LINK O ASN A 24 CA CA A 304 1555 1555 2.30
LINK OD1 ASP A 65 CA CA A 301 1555 1555 2.30
LINK OD1 ASP A 70 CA CA A 301 1555 1555 2.92
LINK OD2 ASP A 70 CA CA A 301 1555 1555 2.36
LINK OD1 ASP A 70 CA CA A 302 1555 1555 2.34
LINK OD2 ASP A 97 CA CA A 303 1555 1555 2.19
LINK OD1 ASP A 102 CA CA A 301 1555 1555 2.50
LINK OD2 ASP A 102 CA CA A 301 1555 1555 2.48
LINK OD2 ASP A 102 CA CA A 303 1555 1555 2.44
LINK O LYS A 142 NA NA A 305 1555 1555 2.43
LINK O GLU A 145 NA NA A 305 1555 1555 2.18
LINK O LYS A 148 NA NA A 305 1555 1555 2.28
LINK CA CA A 301 O2 APOP A 411 1555 1555 2.42
LINK CA CA A 301 O HOH A 436 1555 1555 2.45
LINK CA CA A 301 O AHOH A 437 1555 1555 2.41
LINK CA CA A 302 O1 APOP A 411 1555 1555 2.38
LINK CA CA A 302 O HOH A 418 1555 1555 2.31
LINK CA CA A 302 O HOH A 426 1555 1555 2.37
LINK CA CA A 302 O HOH A 435 1555 1555 2.31
LINK CA CA A 302 O HOH A 436 1555 1555 2.34
LINK CA CA A 303 O2 APOP A 411 1555 1555 2.46
LINK CA CA A 303 O5 APOP A 411 1555 1555 2.35
LINK CA CA A 303 O AHOH A 481 1555 1555 2.61
LINK CA CA A 303 O HOH A 524 1555 1555 2.49
LINK CA CA A 304 O HOH A 420 1555 1555 2.39
LINK CA CA A 304 O HOH A 439 1555 1555 2.44
LINK CA CA A 304 O HOH A 471 1555 1555 2.43
LINK CA CA A 304 O HOH A 471 1555 4556 2.49
LINK CA CA A 304 O HOH A 573 1555 1555 2.42
LINK CA CA A 304 O HOH A 573 1555 4556 2.42
LINK NA NA A 305 O HOH A 450 1555 1555 2.42
LINK NA NA A 305 O HOH A 462 1555 1555 2.53
LINK NA NA A 305 O HOH A 549 1555 1555 2.83
CISPEP 1 LEU A 11 PRO A 12 0 -3.02
SITE 1 AC1 6 ASP A 65 ASP A 70 ASP A 102 POP A 411
SITE 2 AC1 6 HOH A 436 HOH A 437
SITE 1 AC2 7 ASP A 70 POP A 411 HOH A 412 HOH A 418
SITE 2 AC2 7 HOH A 426 HOH A 435 HOH A 436
SITE 1 AC3 5 ASP A 97 ASP A 102 POP A 411 HOH A 481
SITE 2 AC3 5 HOH A 524
SITE 1 AC4 5 ASN A 24 HOH A 420 HOH A 439 HOH A 471
SITE 2 AC4 5 HOH A 573
SITE 1 AC5 6 LYS A 142 GLU A 145 LYS A 148 HOH A 450
SITE 2 AC5 6 HOH A 462 HOH A 549
SITE 1 AC6 3 ARG A 88 HIS A 110 SER A 111
SITE 1 AC7 5 PRO A 6 ALA A 7 HIS A 60 HOH A 605
SITE 2 AC7 5 HOH A 648
SITE 1 AC8 7 ALA A 23 CYS A 53 ASN A 54 PRO A 74
SITE 2 AC8 7 THR A 75 HOH A 415 HOH A 452
SITE 1 AC9 19 LYS A 29 ARG A 43 TYR A 55 ASP A 65
SITE 2 AC9 19 ASP A 70 ASP A 97 ASP A 102 LYS A 104
SITE 3 AC9 19 TYR A 141 LYS A 142 CA A 301 CA A 302
SITE 4 AC9 19 CA A 303 HOH A 412 HOH A 436 HOH A 477
SITE 5 AC9 19 HOH A 481 HOH A 502 HOH A 518
CRYST1 109.356 109.356 75.582 90.00 90.00 120.00 H 3 2 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 0.009144 0.005280 0.000000 0.00000
SCALE2 0.000000 0.010559 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013231 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
