HEADER HYDROLASE 22-JAN-11 3QFN
TITLE CRYSTAL STRUCTURE OF STREPTOCOCCAL ASYMMETRIC AP4A HYDROLASE AND
TITLE 2 PHOSPHODIESTERASE SPR1479/SAPH IN COMPLEX WITH INORGANIC PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-262;
COMPND 5 SYNONYM: SAPH;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 171101;
SOURCE 4 STRAIN: R6;
SOURCE 5 GENE: SPR1479;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P28
KEYWDS SANDWICH FOLD, HYDROLASE, FE3+, MN2+, PO4
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.L.JIANG,J.W.ZHANG,W.L.YU,W.CHENG,C.C.ZHANG,C.Z.ZHOU,Y.CHEN
REVDAT 2 01-NOV-23 3QFN 1 REMARK SEQADV LINK
REVDAT 1 24-AUG-11 3QFN 0
JRNL AUTH Y.L.JIANG,J.W.ZHANG,W.L.YU,W.CHENG,C.C.ZHANG,C.FROLET,
JRNL AUTH 2 A.-M.DI-GUILMI,T.VERNET,C.Z.ZHOU,Y.CHEN
JRNL TITL STRUCTURAL AND ENZYMATIC CHARACTERIZATION OF A STREPTOCOCCAL
JRNL TITL 2 ATP/DIADENOSINE POLYPHOSPHATE AND PHOSPHODIESTER HYDROLASE
JRNL TITL 3 SPR1479/SAPH
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 26450
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1430
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) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1697
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.77000
REMARK 3 B22 (A**2) : -1.87000
REMARK 3 B33 (A**2) : -2.91000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.595
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4142 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5620 ; 1.324 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 496 ; 6.108 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 216 ;35.194 ;23.796
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 718 ;15.211 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;20.772 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 618 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3174 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2470 ; 0.646 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3982 ; 1.229 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1672 ; 1.975 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1638 ; 3.281 ; 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 : 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 3QFN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28781
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51700
REMARK 200 R SYM FOR SHELL (I) : 0.51700
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: MOLREP
REMARK 200 STARTING MODEL: 3QFM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ISO-PROPANOL, 0.1M HEPES, PH 7.5,
REMARK 280 0.2M NH4AC, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.44150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.66300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.46750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.66300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.44150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.46750
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 -7
REMARK 465 GLY A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 THR A 254
REMARK 465 HIS A 255
REMARK 465 HIS A 256
REMARK 465 GLN A 257
REMARK 465 GLU A 258
REMARK 465 PHE A 259
REMARK 465 LEU A 260
REMARK 465 ARG A 261
REMARK 465 GLU A 262
REMARK 465 MET B -7
REMARK 465 GLY B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 THR B 254
REMARK 465 HIS B 255
REMARK 465 HIS B 256
REMARK 465 GLN B 257
REMARK 465 GLU B 258
REMARK 465 PHE B 259
REMARK 465 LEU B 260
REMARK 465 ARG B 261
REMARK 465 GLU B 262
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 O2 PO4 B 263 O HOH B 266 2.07
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 39 64.69 61.73
REMARK 500 MET A 42 141.43 81.54
REMARK 500 ARG A 47 -104.48 -132.06
REMARK 500 HIS A 129 -110.04 -129.74
REMARK 500 HIS A 164 -38.85 75.05
REMARK 500 HIS A 166 35.46 72.83
REMARK 500 ARG A 171 -157.46 -141.37
REMARK 500 ASP B 39 67.73 60.71
REMARK 500 MET B 42 146.22 79.70
REMARK 500 ARG B 47 -104.26 -139.87
REMARK 500 HIS B 129 -117.08 -133.64
REMARK 500 LYS B 133 98.71 -165.42
REMARK 500 HIS B 164 -46.32 75.08
REMARK 500 ARG B 171 -156.96 -142.14
REMARK 500 GLN B 187 59.93 -152.65
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 FE A 265 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 11 OD2
REMARK 620 2 HIS A 13 NE2 115.6
REMARK 620 3 ASP A 39 OD2 87.7 102.3
REMARK 620 4 HIS A 166 NE2 82.7 94.3 163.2
REMARK 620 5 PO4 A 263 O2 153.0 90.8 92.4 90.0
REMARK 620 6 HOH A 266 O 82.1 161.5 71.5 93.4 72.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 264 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 39 OD2
REMARK 620 2 ASN A 66 OD1 104.3
REMARK 620 3 HIS A 128 NE2 88.7 89.6
REMARK 620 4 HIS A 164 ND1 155.1 100.4 88.4
REMARK 620 5 PO4 A 263 O1 90.7 95.0 175.3 90.2
REMARK 620 6 HOH A 266 O 67.0 164.0 103.2 89.7 72.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 265 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 11 OD2
REMARK 620 2 HIS B 13 NE2 114.2
REMARK 620 3 ASP B 39 OD2 83.3 103.6
REMARK 620 4 HIS B 166 NE2 95.8 91.0 164.4
REMARK 620 5 PO4 B 263 O2 152.4 93.4 90.5 83.2
REMARK 620 6 HOH B 266 O 90.1 155.7 77.0 87.5 62.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 264 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 39 OD2
REMARK 620 2 ASN B 66 OD1 101.3
REMARK 620 3 HIS B 128 NE2 91.5 91.2
REMARK 620 4 HIS B 164 ND1 157.6 101.0 86.6
REMARK 620 5 PO4 B 263 O1 92.1 89.6 176.0 89.4
REMARK 620 6 HOH B 266 O 74.0 157.4 110.8 85.8 68.7
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 PO4 A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QFM RELATED DB: PDB
REMARK 900 RELATED ID: 3QFO RELATED DB: PDB
DBREF 3QFN A 1 262 UNP Q8DNX4 Q8DNX4_STRR6 1 262
DBREF 3QFN B 1 262 UNP Q8DNX4 Q8DNX4_STRR6 1 262
SEQADV 3QFN MET A -7 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN GLY A -6 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS A -5 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS A -4 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS A -3 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS A -2 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS A -1 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS A 0 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN MET B -7 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN GLY B -6 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS B -5 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS B -4 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS B -3 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS B -2 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS B -1 UNP Q8DNX4 EXPRESSION TAG
SEQADV 3QFN HIS B 0 UNP Q8DNX4 EXPRESSION TAG
SEQRES 1 A 270 MET GLY HIS HIS HIS HIS HIS HIS MET ASP MET THR LYS
SEQRES 2 A 270 ILE ALA LEU LEU SER ASP ILE HIS GLY ASN THR THR ALA
SEQRES 3 A 270 LEU GLU ALA VAL LEU ALA ASP ALA ARG GLN LEU GLY VAL
SEQRES 4 A 270 ASP GLU TYR TRP LEU LEU GLY ASP ILE LEU MET PRO GLY
SEQRES 5 A 270 THR GLY ARG ARG ARG ILE LEU ASP LEU LEU ASP GLN LEU
SEQRES 6 A 270 PRO ILE THR ALA ARG VAL LEU GLY ASN TRP GLU ASP SER
SEQRES 7 A 270 LEU TRP HIS GLY VAL ARG LYS GLU LEU ASP SER THR ARG
SEQRES 8 A 270 PRO SER GLN ARG TYR LEU LEU ARG GLN CYS GLN TYR VAL
SEQRES 9 A 270 LEU GLU GLU ILE SER LEU GLU GLU ILE GLU VAL LEU HIS
SEQRES 10 A 270 ASN GLN PRO LEU GLN ILE HIS ARG GLN PHE GLY ASP LEU
SEQRES 11 A 270 THR VAL GLY ILE SER HIS HIS LEU PRO ASP LYS ASN TRP
SEQRES 12 A 270 GLY ARG GLU LEU ILE HIS THR GLY LYS GLN GLU GLU PHE
SEQRES 13 A 270 ASP ARG LEU VAL THR HIS PRO PRO CYS ASP ILE ALA VAL
SEQRES 14 A 270 TYR GLY HIS ILE HIS GLN GLN LEU LEU ARG TYR GLY THR
SEQRES 15 A 270 GLY GLY GLN LEU ILE VAL ASN PRO GLY SER ILE GLY GLN
SEQRES 16 A 270 PRO PHE PHE LEU ASP ALA GLN LEU ARG LYS ASP LEU ARG
SEQRES 17 A 270 ALA GLN TYR MET ILE LEU GLU PHE ASP ASP LYS GLY LEU
SEQRES 18 A 270 VAL ASP MET ASP PHE ARG ARG VAL ASP TYR ASP VAL ALA
SEQRES 19 A 270 ALA GLU LEU GLN LEU ALA LYS ASP LEU ARG LEU PRO TYR
SEQRES 20 A 270 PHE GLU VAL TYR TYR GLU SER LEU VAL ASN GLY ILE HIS
SEQRES 21 A 270 HIS THR HIS HIS GLN GLU PHE LEU ARG GLU
SEQRES 1 B 270 MET GLY HIS HIS HIS HIS HIS HIS MET ASP MET THR LYS
SEQRES 2 B 270 ILE ALA LEU LEU SER ASP ILE HIS GLY ASN THR THR ALA
SEQRES 3 B 270 LEU GLU ALA VAL LEU ALA ASP ALA ARG GLN LEU GLY VAL
SEQRES 4 B 270 ASP GLU TYR TRP LEU LEU GLY ASP ILE LEU MET PRO GLY
SEQRES 5 B 270 THR GLY ARG ARG ARG ILE LEU ASP LEU LEU ASP GLN LEU
SEQRES 6 B 270 PRO ILE THR ALA ARG VAL LEU GLY ASN TRP GLU ASP SER
SEQRES 7 B 270 LEU TRP HIS GLY VAL ARG LYS GLU LEU ASP SER THR ARG
SEQRES 8 B 270 PRO SER GLN ARG TYR LEU LEU ARG GLN CYS GLN TYR VAL
SEQRES 9 B 270 LEU GLU GLU ILE SER LEU GLU GLU ILE GLU VAL LEU HIS
SEQRES 10 B 270 ASN GLN PRO LEU GLN ILE HIS ARG GLN PHE GLY ASP LEU
SEQRES 11 B 270 THR VAL GLY ILE SER HIS HIS LEU PRO ASP LYS ASN TRP
SEQRES 12 B 270 GLY ARG GLU LEU ILE HIS THR GLY LYS GLN GLU GLU PHE
SEQRES 13 B 270 ASP ARG LEU VAL THR HIS PRO PRO CYS ASP ILE ALA VAL
SEQRES 14 B 270 TYR GLY HIS ILE HIS GLN GLN LEU LEU ARG TYR GLY THR
SEQRES 15 B 270 GLY GLY GLN LEU ILE VAL ASN PRO GLY SER ILE GLY GLN
SEQRES 16 B 270 PRO PHE PHE LEU ASP ALA GLN LEU ARG LYS ASP LEU ARG
SEQRES 17 B 270 ALA GLN TYR MET ILE LEU GLU PHE ASP ASP LYS GLY LEU
SEQRES 18 B 270 VAL ASP MET ASP PHE ARG ARG VAL ASP TYR ASP VAL ALA
SEQRES 19 B 270 ALA GLU LEU GLN LEU ALA LYS ASP LEU ARG LEU PRO TYR
SEQRES 20 B 270 PHE GLU VAL TYR TYR GLU SER LEU VAL ASN GLY ILE HIS
SEQRES 21 B 270 HIS THR HIS HIS GLN GLU PHE LEU ARG GLU
HET PO4 A 263 5
HET MN A 264 1
HET FE A 265 1
HET PO4 B 263 5
HET MN B 264 1
HET FE B 265 1
HETNAM PO4 PHOSPHATE ION
HETNAM MN MANGANESE (II) ION
HETNAM FE FE (III) ION
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 MN 2(MN 2+)
FORMUL 5 FE 2(FE 3+)
FORMUL 9 HOH *211(H2 O)
HELIX 1 1 ASN A 15 LEU A 29 1 15
HELIX 2 2 ARG A 47 GLN A 56 1 10
HELIX 3 3 GLY A 65 ARG A 76 1 12
HELIX 4 4 ARG A 83 GLU A 98 1 16
HELIX 5 5 SER A 101 ASN A 110 1 10
HELIX 6 6 LYS A 144 ARG A 150 1 7
HELIX 7 7 GLN A 194 ASP A 198 5 5
HELIX 8 8 ASP A 224 ARG A 236 1 13
HELIX 9 9 TYR A 239 ASN A 249 1 11
HELIX 10 10 ASN B 15 LEU B 29 1 15
HELIX 11 11 ARG B 47 GLN B 56 1 10
HELIX 12 12 GLY B 65 ARG B 76 1 12
HELIX 13 13 ARG B 83 GLU B 98 1 16
HELIX 14 14 SER B 101 ASN B 110 1 10
HELIX 15 15 LYS B 144 ASP B 149 1 6
HELIX 16 16 ARG B 150 VAL B 152 5 3
HELIX 17 17 ASP B 192 LYS B 197 1 6
HELIX 18 18 ASP B 224 LEU B 235 1 12
HELIX 19 19 TYR B 239 ASN B 249 1 11
SHEET 1 A10 ILE A 59 ARG A 62 0
SHEET 2 A10 GLU A 33 LEU A 36 1 N LEU A 36 O ALA A 61
SHEET 3 A10 THR A 4 LEU A 9 1 N LEU A 9 O TRP A 35
SHEET 4 A10 ALA A 201 ASP A 209 -1 O LEU A 206 N ILE A 6
SHEET 5 A10 GLY A 212 VAL A 221 -1 O ASP A 217 N ILE A 205
SHEET 6 A10 GLY B 212 VAL B 221 -1 O PHE B 218 N MET A 216
SHEET 7 A10 ALA B 201 ASP B 209 -1 N ASP B 209 O GLY B 212
SHEET 8 A10 THR B 4 LEU B 9 -1 N THR B 4 O PHE B 208
SHEET 9 A10 GLU B 33 LEU B 36 1 O TRP B 35 N ALA B 7
SHEET 10 A10 ILE B 59 ARG B 62 1 O ALA B 61 N LEU B 36
SHEET 1 B 5 GLN A 114 PHE A 119 0
SHEET 2 B 5 LEU A 122 SER A 127 -1 O LEU A 122 N PHE A 119
SHEET 3 B 5 ILE A 159 VAL A 161 1 O ILE A 159 N GLY A 125
SHEET 4 B 5 LEU A 178 PRO A 182 1 O LEU A 178 N ALA A 160
SHEET 5 B 5 GLN A 168 TYR A 172 -1 N ARG A 171 O ILE A 179
SHEET 1 C 5 GLN B 114 PHE B 119 0
SHEET 2 C 5 LEU B 122 SER B 127 -1 O VAL B 124 N ARG B 117
SHEET 3 C 5 ILE B 159 VAL B 161 1 O VAL B 161 N GLY B 125
SHEET 4 C 5 LEU B 178 PRO B 182 1 O LEU B 178 N ALA B 160
SHEET 5 C 5 GLN B 168 TYR B 172 -1 N ARG B 171 O ILE B 179
LINK OD2 ASP A 11 FE FE A 265 1555 1555 2.13
LINK NE2 HIS A 13 FE FE A 265 1555 1555 2.25
LINK OD2 ASP A 39 MN MN A 264 1555 1555 2.32
LINK OD2 ASP A 39 FE FE A 265 1555 1555 2.14
LINK OD1 ASN A 66 MN MN A 264 1555 1555 2.12
LINK NE2 HIS A 128 MN MN A 264 1555 1555 2.18
LINK ND1 HIS A 164 MN MN A 264 1555 1555 2.29
LINK NE2 HIS A 166 FE FE A 265 1555 1555 2.25
LINK O1 PO4 A 263 MN MN A 264 1555 1555 2.04
LINK O2 PO4 A 263 FE FE A 265 1555 1555 2.19
LINK MN MN A 264 O HOH A 266 1555 1555 2.10
LINK FE FE A 265 O HOH A 266 1555 1555 2.04
LINK OD2 ASP B 11 FE FE B 265 1555 1555 2.20
LINK NE2 HIS B 13 FE FE B 265 1555 1555 2.21
LINK OD2 ASP B 39 MN MN B 264 1555 1555 2.07
LINK OD2 ASP B 39 FE FE B 265 1555 1555 2.29
LINK OD1 ASN B 66 MN MN B 264 1555 1555 2.19
LINK NE2 HIS B 128 MN MN B 264 1555 1555 2.18
LINK ND1 HIS B 164 MN MN B 264 1555 1555 2.26
LINK NE2 HIS B 166 FE FE B 265 1555 1555 2.31
LINK O1 PO4 B 263 MN MN B 264 1555 1555 2.06
LINK O2 PO4 B 263 FE FE B 265 1555 1555 2.01
LINK MN MN B 264 O HOH B 266 1555 1555 2.36
LINK FE FE B 265 O HOH B 266 1555 1555 2.00
CISPEP 1 MET A 42 PRO A 43 0 2.80
CISPEP 2 HIS A 154 PRO A 155 0 4.37
CISPEP 3 MET B 42 PRO B 43 0 0.31
CISPEP 4 HIS B 154 PRO B 155 0 -0.70
SITE 1 AC1 10 HIS A 13 ASP A 39 ASN A 66 TRP A 67
SITE 2 AC1 10 HIS A 164 HIS A 166 MN A 264 FE A 265
SITE 3 AC1 10 HOH A 266 HOH A 292
SITE 1 AC2 7 ASP A 39 ASN A 66 HIS A 128 HIS A 164
SITE 2 AC2 7 PO4 A 263 FE A 265 HOH A 266
SITE 1 AC3 7 ASP A 11 HIS A 13 ASP A 39 HIS A 166
SITE 2 AC3 7 PO4 A 263 MN A 264 HOH A 266
SITE 1 AC4 10 HIS B 13 ASP B 39 ASN B 66 TRP B 67
SITE 2 AC4 10 HIS B 164 HIS B 166 MN B 264 FE B 265
SITE 3 AC4 10 HOH B 266 HOH B 278
SITE 1 AC5 7 ASP B 39 ASN B 66 HIS B 128 HIS B 164
SITE 2 AC5 7 PO4 B 263 FE B 265 HOH B 266
SITE 1 AC6 7 ASP B 11 HIS B 13 ASP B 39 HIS B 166
SITE 2 AC6 7 PO4 B 263 MN B 264 HOH B 266
CRYST1 58.883 74.935 149.326 90.00 90.00 90.00 P 21 21 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 0.016983 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006697 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
