HEADER HYDROLASE 31-OCT-01 1KA1
TITLE THE PAPASE HAL2P COMPLEXED WITH CALCIUM AND MAGNESIUM IONS AND
TITLE 2 REACTION SUBSTRATE: PAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOTOLERANCE PROTEIN HAL2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HAL2P, 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE, PHOSPHOADENYLATE
COMPND 5 3'-NUCLEOTIDASE, 3'-PHOSPHOADENYLYLSULFATE 3'-PHOSPHATASE;
COMPND 6 EC: 3.1.3.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: HAL2;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: RS1051;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: MULTI-COPY PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PRS-421-HAL2
KEYWDS NUCLEOTIDASE, SALT TOLERANCE, INOSITOL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PATEL,A.ALBERT,T.L.BLUNDELL
REVDAT 4 16-AUG-23 1KA1 1 REMARK LINK
REVDAT 3 24-FEB-09 1KA1 1 VERSN
REVDAT 2 05-APR-05 1KA1 1 JRNL REMARK
REVDAT 1 07-NOV-01 1KA1 0
JRNL AUTH S.PATEL,M.MARTINEZ-RIPOLL,T.L.BLUNDELL,A.ALBERT
JRNL TITL STRUCTURAL ENZYMOLOGY OF LI(+)-SENSITIVE/MG(2+)-DEPENDENT
JRNL TITL 2 PHOSPHATASES.
JRNL REF J.MOL.BIOL. V. 320 1087 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12126627
JRNL DOI 10.1016/S0022-2836(02)00564-8
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 3 NUMBER OF REFLECTIONS : 73179
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) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3654
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4201
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 227
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2718
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 446
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.072
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2797 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2504 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3789 ; 1.723 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5838 ; 1.253 ; 2.995
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 353 ; 6.181 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 494 ;15.123 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 430 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3124 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 547 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 596 ; 0.269 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2337 ; 0.225 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 6 ; 0.383 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 313 ; 0.267 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.296 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.087 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.259 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 53 ; 0.274 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.254 ; 0.500
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): 1748 ; 2.399 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2807 ; 3.214 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1049 ; 4.396 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 982 ; 6.143 ; 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): 2797 ; 2.631 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 2 ; 6.221 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2747 ; 5.360 ; 2.000
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 1KA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014747.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8700
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73179
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1QGX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG5000 MME, 0.1 M SODIUM ACETATE,
REMARK 280 5 MM BETA-MERCAPTOETHANOL, 0.1 M MES. (CRYSTALS WERE SOAKED IN
REMARK 280 MOTHER LIQUOR CONTAINING 0.5 M CALCIUM CHLORIDE FOR 5 HOURS.) ,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 22.48400
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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 ASN A 356
REMARK 465 ALA A 357
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 32 CB CG CD CE NZ
REMARK 470 ASP A 33 CB CG OD1 OD2
REMARK 470 LYS A 189 CG CD CE NZ
REMARK 470 LYS A 229 CD CE NZ
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 O HOH A 768 O HOH A 1031 1.70
REMARK 500 OH TYR A 183 O HOH A 1035 1.87
REMARK 500 O HOH A 779 O HOH A 1029 1.92
REMARK 500 O HOH A 797 O HOH A 1048 1.97
REMARK 500 O HOH A 986 O HOH A 989 2.00
REMARK 500 O HOH A 997 O HOH A 1035 2.02
REMARK 500 N LEU A 3 O HOH A 1026 2.05
REMARK 500 O HOH A 667 O HOH A 918 2.06
REMARK 500 O HOH A 755 O HOH A 989 2.07
REMARK 500 CE LYS A 329 O HOH A 854 2.09
REMARK 500 O HOH A 759 O HOH A 821 2.11
REMARK 500 O HOH A 657 O HOH A 1019 2.11
REMARK 500 O HOH A 916 O HOH A 1002 2.13
REMARK 500 NZ LYS A 258 O HOH A 910 2.14
REMARK 500 O HOH A 777 O HOH A 1032 2.14
REMARK 500 O HOH A 982 O HOH A 1023 2.16
REMARK 500 CG ARG A 5 O HOH A 933 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 O HOH A 744 O HOH A 1031 2555 2.02
REMARK 500 O HOH A 926 O HOH A 1033 2544 2.03
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 LYS A 16 CE LYS A 16 NZ 0.177
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 5 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 104 CB - CG - OD2 ANGL. DEV. = 6.8 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 LYS A 32 43.74 -85.06
REMARK 500 GLU A 154 -142.12 -113.45
REMARK 500 PHE A 194 41.72 -154.99
REMARK 500 ASP A 213 -82.93 -92.24
REMARK 500 SER A 264 171.31 84.89
REMARK 500 HIS A 295 -13.34 -141.48
REMARK 500 MET A 313 -54.05 -128.06
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 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 72 OE1
REMARK 620 2 ASP A 142 OD1 89.5
REMARK 620 3 ASP A 142 OD2 87.9 46.9
REMARK 620 4 ILE A 144 O 163.9 79.3 92.6
REMARK 620 5 A3P A 601 O1P 94.2 110.6 64.0 100.5
REMARK 620 6 HOH A 603 O 86.5 86.5 133.1 81.4 162.9
REMARK 620 7 HOH A 613 O 94.9 169.3 142.9 94.4 78.9 84.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 142 OD2
REMARK 620 2 ASP A 145 OD1 86.7
REMARK 620 3 ASP A 294 OD1 95.6 90.7
REMARK 620 4 A3P A 601 O1P 82.5 108.6 160.3
REMARK 620 5 A3P A 601 O3' 132.1 72.4 126.3 65.3
REMARK 620 6 HOH A 639 O 100.5 170.5 82.5 78.6 106.3
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A3P A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QGX RELATED DB: PDB
REMARK 900 1QGX IS COMPLEXED WITH TWO MAGNESIUM IONS AND A LITHIUM ION AND
REMARK 900 REACTION PRODUCTS AMP AND INORGANIC PHOSPHATE
REMARK 900 RELATED ID: 1K9Y RELATED DB: PDB
REMARK 900 THE PAPASE HAL2P COMPLEXED WITH MAGNESIUM IONS AND REACTION
REMARK 900 PRODUCTS: AMP AND INORGANIC PHOSPHATE
REMARK 900 RELATED ID: 1K9Z RELATED DB: PDB
REMARK 900 THE PAPASE HAL2P COMPLEXED WITH ZINC IONS
REMARK 900 RELATED ID: 1KA0 RELATED DB: PDB
REMARK 900 THE PAPASE HAL2P COMPLEXED WITH A SODIUM ION AND THE REACTION
REMARK 900 PRODUCT AMP
DBREF 1KA1 A 1 357 UNP P32179 HAL2_YEAST 1 357
SEQRES 1 A 357 MET ALA LEU GLU ARG GLU LEU LEU VAL ALA THR GLN ALA
SEQRES 2 A 357 VAL ARG LYS ALA SER LEU LEU THR LYS ARG ILE GLN SER
SEQRES 3 A 357 GLU VAL ILE SER HIS LYS ASP SER THR THR ILE THR LYS
SEQRES 4 A 357 ASN ASP ASN SER PRO VAL THR THR GLY ASP TYR ALA ALA
SEQRES 5 A 357 GLN THR ILE ILE ILE ASN ALA ILE LYS SER ASN PHE PRO
SEQRES 6 A 357 ASP ASP LYS VAL VAL GLY GLU GLU SER SER SER GLY LEU
SEQRES 7 A 357 SER ASP ALA PHE VAL SER GLY ILE LEU ASN GLU ILE LYS
SEQRES 8 A 357 ALA ASN ASP GLU VAL TYR ASN LYS ASN TYR LYS LYS ASP
SEQRES 9 A 357 ASP PHE LEU PHE THR ASN ASP GLN PHE PRO LEU LYS SER
SEQRES 10 A 357 LEU GLU ASP VAL ARG GLN ILE ILE ASP PHE GLY ASN TYR
SEQRES 11 A 357 GLU GLY GLY ARG LYS GLY ARG PHE TRP CYS LEU ASP PRO
SEQRES 12 A 357 ILE ASP GLY THR LYS GLY PHE LEU ARG GLY GLU GLN PHE
SEQRES 13 A 357 ALA VAL CYS LEU ALA LEU ILE VAL ASP GLY VAL VAL GLN
SEQRES 14 A 357 LEU GLY CYS ILE GLY CYS PRO ASN LEU VAL LEU SER SER
SEQRES 15 A 357 TYR GLY ALA GLN ASP LEU LYS GLY HIS GLU SER PHE GLY
SEQRES 16 A 357 TYR ILE PHE ARG ALA VAL ARG GLY LEU GLY ALA PHE TYR
SEQRES 17 A 357 SER PRO SER SER ASP ALA GLU SER TRP THR LYS ILE HIS
SEQRES 18 A 357 VAL ARG HIS LEU LYS ASP THR LYS ASP MET ILE THR LEU
SEQRES 19 A 357 GLU GLY VAL GLU LYS GLY HIS SER SER HIS ASP GLU GLN
SEQRES 20 A 357 THR ALA ILE LYS ASN LYS LEU ASN ILE SER LYS SER LEU
SEQRES 21 A 357 HIS LEU ASP SER GLN ALA LYS TYR CYS LEU LEU ALA LEU
SEQRES 22 A 357 GLY LEU ALA ASP VAL TYR LEU ARG LEU PRO ILE LYS LEU
SEQRES 23 A 357 SER TYR GLN GLU LYS ILE TRP ASP HIS ALA ALA GLY ASN
SEQRES 24 A 357 VAL ILE VAL HIS GLU ALA GLY GLY ILE HIS THR ASP ALA
SEQRES 25 A 357 MET GLU ASP VAL PRO LEU ASP PHE GLY ASN GLY ARG THR
SEQRES 26 A 357 LEU ALA THR LYS GLY VAL ILE ALA SER SER GLY PRO ARG
SEQRES 27 A 357 GLU LEU HIS ASP LEU VAL VAL SER THR SER CYS ASP VAL
SEQRES 28 A 357 ILE GLN SER ARG ASN ALA
HET CA A 401 1
HET MG A 501 1
HET A3P A 601 27
HET BME A 602 4
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM A3P ADENOSINE-3'-5'-DIPHOSPHATE
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 2 CA CA 2+
FORMUL 3 MG MG 2+
FORMUL 4 A3P C10 H15 N5 O10 P2
FORMUL 5 BME C2 H6 O S
FORMUL 6 HOH *446(H2 O)
HELIX 1 1 LEU A 3 HIS A 31 1 29
HELIX 2 2 THR A 47 PHE A 64 1 18
HELIX 3 3 SER A 79 TYR A 101 1 23
HELIX 4 4 SER A 117 PHE A 127 1 11
HELIX 5 5 GLY A 146 ARG A 152 1 7
HELIX 6 6 VAL A 179 GLY A 184 5 6
HELIX 7 7 ASP A 227 ASP A 230 5 4
HELIX 8 8 SER A 243 LEU A 254 1 12
HELIX 9 9 GLN A 265 GLY A 274 1 10
HELIX 10 10 LYS A 291 ASP A 294 5 4
HELIX 11 11 HIS A 295 ALA A 305 1 11
HELIX 12 12 PRO A 337 SER A 354 1 18
SHEET 1 A 2 THR A 36 THR A 38 0
SHEET 2 A 2 PRO A 44 THR A 46 -1 O VAL A 45 N ILE A 37
SHEET 1 B 7 VAL A 69 GLY A 71 0
SHEET 2 B 7 ARG A 137 ASP A 145 1 O TRP A 139 N VAL A 70
SHEET 3 B 7 ALA A 157 VAL A 164 -1 O ALA A 157 N ASP A 145
SHEET 4 B 7 VAL A 167 CYS A 175 -1 O GLY A 174 N VAL A 158
SHEET 5 B 7 TYR A 196 VAL A 201 -1 O TYR A 196 N CYS A 175
SHEET 6 B 7 ALA A 206 PRO A 210 -1 O SER A 209 N ILE A 197
SHEET 7 B 7 THR A 218 LYS A 219 -1 O THR A 218 N TYR A 208
SHEET 1 C 5 LYS A 258 HIS A 261 0
SHEET 2 C 5 ILE A 232 GLU A 235 1 N GLU A 235 O LEU A 260
SHEET 3 C 5 VAL A 278 ARG A 281 1 O VAL A 278 N LEU A 234
SHEET 4 C 5 VAL A 331 SER A 334 -1 O ALA A 333 N TYR A 279
SHEET 5 C 5 ILE A 308 THR A 310 -1 N THR A 310 O ILE A 332
LINK SG CYS A 349 S2 BME A 602 1555 1555 1.82
LINK OE1 GLU A 72 CA CA A 401 1555 1555 2.27
LINK OD1 ASP A 142 CA CA A 401 1555 1555 2.30
LINK OD2 ASP A 142 CA CA A 401 1555 1555 2.94
LINK OD2 ASP A 142 MG MG A 501 1555 1555 2.32
LINK O ILE A 144 CA CA A 401 1555 1555 2.34
LINK OD1 ASP A 145 MG MG A 501 1555 1555 2.20
LINK OD1 ASP A 294 MG MG A 501 1555 1555 2.11
LINK CA CA A 401 O1P A3P A 601 1555 1555 2.35
LINK CA CA A 401 O HOH A 603 1555 1555 2.40
LINK CA CA A 401 O HOH A 613 1555 1555 2.37
LINK MG MG A 501 O1P A3P A 601 1555 1555 1.98
LINK MG MG A 501 O3' A3P A 601 1555 1555 2.26
LINK MG MG A 501 O HOH A 639 1555 1555 2.66
CISPEP 1 GLY A 336 PRO A 337 0 5.83
SITE 1 AC1 6 GLU A 72 ASP A 142 ILE A 144 A3P A 601
SITE 2 AC1 6 HOH A 603 HOH A 613
SITE 1 AC2 5 ASP A 142 ASP A 145 ASP A 294 A3P A 601
SITE 2 AC2 5 HOH A 639
SITE 1 AC3 27 GLU A 72 ASP A 142 ILE A 144 ASP A 145
SITE 2 AC3 27 GLY A 146 THR A 147 GLY A 240 HIS A 241
SITE 3 AC3 27 ASP A 263 SER A 264 LYS A 267 ARG A 281
SITE 4 AC3 27 TYR A 288 ASP A 294 CA A 401 MG A 501
SITE 5 AC3 27 HOH A 606 HOH A 613 HOH A 627 HOH A 632
SITE 6 AC3 27 HOH A 639 HOH A 640 HOH A 675 HOH A 797
SITE 7 AC3 27 HOH A 815 HOH A 998 HOH A1027
SITE 1 AC4 6 MET A 313 GLU A 314 CYS A 349 GLN A 353
SITE 2 AC4 6 HOH A 807 HOH A1005
CRYST1 54.875 44.968 72.110 90.00 110.72 90.00 P 1 21 1 2
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 0.018223 0.000000 0.006895 0.00000
SCALE2 0.000000 0.022238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014827 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
