HEADER ISOMERASE 06-DEC-13 4NWJ
TITLE CRYSTAL STRUCTURE OF PHOSPHOPGLYCERATE MUTASE FROM STAPHYLOCOCCUS
TITLE 2 AUREUS IN 3-PHOSPHOGLYCERIC ACID BOUND FORM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE
COMPND 3 MUTASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: BPG-INDEPENDENT PGAM, PHOSPHOGLYCEROMUTASE, IPGM;
COMPND 6 EC: 5.4.2.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 93061;
SOURCE 4 STRAIN: NCTC8325;
SOURCE 5 GENE: GPMI, SAOUHSC_00798;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS ISOMERASE, GLYCOLYTIC ENZYME, CYTOSOL
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROYCHOWDHURY,M.BOSE,A.KUNDU,A.GUJAR,A.K.DAS
REVDAT 4 08-NOV-23 4NWJ 1 REMARK SEQADV LINK
REVDAT 3 08-APR-15 4NWJ 1 JRNL
REVDAT 2 11-FEB-15 4NWJ 1 JRNL
REVDAT 1 14-JAN-15 4NWJ 0
JRNL AUTH A.ROYCHOWDHURY,A.KUNDU,M.BOSE,A.GUJAR,S.MUKHERJEE,A.K.DAS
JRNL TITL COMPLETE CATALYTIC CYCLE OF COFACTOR-INDEPENDENT
JRNL TITL 2 PHOSPHOGLYCERATE MUTASE INVOLVES A SPRING-LOADED MECHANISM
JRNL REF FEBS J. V. 282 1097 2015
JRNL REFN ISSN 1742-464X
JRNL PMID 25611430
JRNL DOI 10.1111/FEBS.13205
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 34105
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1798
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2028
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3954
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : -1.32000
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): 0.170
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.567
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4063 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3780 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5508 ; 1.963 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8706 ; 1.015 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 507 ; 6.947 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 212 ;40.578 ;25.472
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 684 ;16.564 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;19.149 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 606 ; 0.172 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4710 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 921 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 4NWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX (OSMIC MIRROR)
REMARK 200 OPTICS : VARIMAX (OSMIC MIRROR)
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35948
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 60.684
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : 0.44600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: 4MY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NACL, BIS-TRIS, 25%(W/V) PEG3350,
REMARK 280 PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 36.81850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.57250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.42050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.57250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.81850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.42050
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
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 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 271 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 279 CG CD OE1 OE2
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 811 O HOH A 812 2.16
REMARK 500 O HOH A 776 O HOH A 924 2.16
REMARK 500 N ALA A 2 O HOH A 956 2.18
REMARK 500 O HOH A 868 O HOH A 869 2.19
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 17 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG A 191 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 191 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 206 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 206 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 259 CB - CG - OD1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 259 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 VAL A 334 CG1 - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 350 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 350 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU A 481 CB - CG - CD1 ANGL. DEV. = 13.0 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 108 47.92 39.98
REMARK 500 SER A 109 -149.00 -104.86
REMARK 500 ASP A 151 -97.37 -91.39
REMARK 500 ASP A 209 114.88 -161.53
REMARK 500 ASN A 240 14.74 56.71
REMARK 500 ASN A 293 -168.55 -164.68
REMARK 500 THR A 335 -92.82 -105.93
REMARK 500 LYS A 365 83.04 -150.50
REMARK 500 MET A 368 -129.22 37.96
REMARK 500 THR A 436 -163.31 -161.32
REMARK 500 HIS A 439 172.55 166.16
REMARK 500 ASN A 441 -65.85 177.84
REMARK 500 THR A 466 55.84 -90.09
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 MN A 602 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 12 OD1
REMARK 620 2 ASP A 12 OD2 54.4
REMARK 620 3 SER A 62 OG 111.7 93.3
REMARK 620 4 ASP A 438 OD2 119.7 80.5 108.3
REMARK 620 5 ASP A 438 OD1 78.5 76.4 157.6 50.9
REMARK 620 6 HIS A 439 NE2 105.6 152.6 112.8 97.9 81.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 601 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 397 OD1
REMARK 620 2 HIS A 401 NE2 101.8
REMARK 620 3 HIS A 456 NE2 114.5 97.3
REMARK 620 4 HOH A 701 O 161.2 87.8 79.8
REMARK 620 5 HOH A 702 O 94.0 153.9 94.9 71.7
REMARK 620 6 HOH A 767 O 85.6 88.8 157.1 78.4 71.7
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 MN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG A 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NWX RELATED DB: PDB
DBREF 4NWJ A 1 505 UNP Q2G029 Q2G029_STAA8 1 505
SEQADV 4NWJ HIS A -7 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ HIS A -6 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ HIS A -5 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ HIS A -4 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ HIS A -3 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ HIS A -2 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ GLY A -1 UNP Q2G029 EXPRESSION TAG
SEQADV 4NWJ SER A 0 UNP Q2G029 EXPRESSION TAG
SEQRES 1 A 513 HIS HIS HIS HIS HIS HIS GLY SER MET ALA LYS LYS PRO
SEQRES 2 A 513 THR ALA LEU ILE ILE LEU ASP GLY PHE ALA ASN ARG GLU
SEQRES 3 A 513 SER GLU HIS GLY ASN ALA VAL LYS LEU ALA ASN LYS PRO
SEQRES 4 A 513 ASN PHE ASP ARG TYR TYR ASN LYS TYR PRO THR THR GLN
SEQRES 5 A 513 ILE GLU ALA SER GLY LEU ASP VAL GLY LEU PRO GLU GLY
SEQRES 6 A 513 GLN MET GLY ASN SER GLU VAL GLY HIS MET ASN ILE GLY
SEQRES 7 A 513 ALA GLY ARG ILE VAL TYR GLN SER LEU THR ARG ILE ASN
SEQRES 8 A 513 LYS SER ILE GLU ASP GLY ASP PHE PHE GLU ASN ASP VAL
SEQRES 9 A 513 LEU ASN ASN ALA ILE ALA HIS VAL ASN SER HIS ASP SER
SEQRES 10 A 513 ALA LEU HIS ILE PHE GLY LEU LEU SER ASP GLY GLY VAL
SEQRES 11 A 513 HIS SER HIS TYR LYS HIS LEU PHE ALA LEU LEU GLU LEU
SEQRES 12 A 513 ALA LYS LYS GLN GLY VAL GLU LYS VAL TYR VAL HIS ALA
SEQRES 13 A 513 PHE LEU ASP GLY ARG ASP VAL ASP GLN LYS SER ALA LEU
SEQRES 14 A 513 LYS TYR ILE GLU GLU THR GLU ALA LYS PHE ASN GLU LEU
SEQRES 15 A 513 GLY ILE GLY GLN PHE ALA SER VAL SER GLY ARG TYR TYR
SEQRES 16 A 513 ALA MET ASP ARG ASP LYS ARG TRP GLU ARG GLU GLU LYS
SEQRES 17 A 513 ALA TYR ASN ALA ILE ARG ASN PHE ASP ALA PRO THR TYR
SEQRES 18 A 513 ALA THR ALA LYS GLU GLY VAL GLU ALA SER TYR ASN GLU
SEQRES 19 A 513 GLY LEU THR ASP GLU PHE VAL VAL PRO PHE ILE VAL GLU
SEQRES 20 A 513 ASN GLN ASN ASP GLY VAL ASN ASP GLY ASP ALA VAL ILE
SEQRES 21 A 513 PHE TYR ASN PHE ARG PRO ASP ARG ALA ALA GLN LEU SER
SEQRES 22 A 513 GLU ILE PHE ALA ASN ARG ALA PHE GLU GLY PHE LYS VAL
SEQRES 23 A 513 GLU GLN VAL LYS ASP LEU PHE TYR ALA THR PHE THR LYS
SEQRES 24 A 513 TYR ASN ASP ASN ILE ASP ALA ALA ILE VAL PHE GLU LYS
SEQRES 25 A 513 VAL ASP LEU ASN ASN THR ILE GLY GLU ILE ALA GLN ASN
SEQRES 26 A 513 ASN ASN LEU THR GLN LEU ARG ILE ALA GLU THR GLU LYS
SEQRES 27 A 513 TYR PRO HIS VAL THR TYR PHE MET SER GLY GLY ARG ASN
SEQRES 28 A 513 GLU GLU PHE LYS GLY GLU ARG ARG ARG LEU ILE ASP SER
SEQRES 29 A 513 PRO LYS VAL ALA THR TYR ASP LEU LYS PRO GLU MET SER
SEQRES 30 A 513 ALA TYR GLU VAL LYS ASP ALA LEU LEU GLU GLU LEU ASN
SEQRES 31 A 513 LYS GLY ASP LEU ASP LEU ILE ILE LEU ASN PHE ALA ASN
SEQRES 32 A 513 PRO ASP MET VAL GLY HIS SER GLY MET LEU GLU PRO THR
SEQRES 33 A 513 ILE LYS ALA ILE GLU ALA VAL ASP GLU CYS LEU GLY GLU
SEQRES 34 A 513 VAL VAL ASP LYS ILE LEU ASP MET ASP GLY TYR ALA ILE
SEQRES 35 A 513 ILE THR ALA ASP HIS GLY ASN SER ASP GLN VAL LEU THR
SEQRES 36 A 513 ASP ASP ASP GLN PRO MET THR THR HIS THR THR ASN PRO
SEQRES 37 A 513 VAL PRO VAL ILE VAL THR LYS GLU GLY VAL THR LEU ARG
SEQRES 38 A 513 GLU THR GLY ARG LEU GLY ASP LEU ALA PRO THR LEU LEU
SEQRES 39 A 513 ASP LEU LEU ASN VAL GLU GLN PRO GLU ASP MET THR GLY
SEQRES 40 A 513 GLU SER LEU ILE LYS HIS
HET MN A 601 1
HET MN A 602 1
HET 3PG A 603 22
HETNAM MN MANGANESE (II) ION
HETNAM 3PG 3-PHOSPHOGLYCERIC ACID
FORMUL 2 MN 2(MN 2+)
FORMUL 4 3PG C3 H7 O7 P
FORMUL 5 HOH *296(H2 O)
HELIX 1 1 ASN A 23 ALA A 28 1 6
HELIX 2 2 LYS A 30 TYR A 40 1 11
HELIX 3 3 SER A 48 GLY A 53 5 6
HELIX 4 4 ASN A 61 GLY A 72 1 12
HELIX 5 5 GLN A 77 GLY A 89 1 13
HELIX 6 6 ASP A 90 GLU A 93 5 4
HELIX 7 7 ASN A 94 ASP A 108 1 15
HELIX 8 8 TYR A 126 GLN A 139 1 14
HELIX 9 9 SER A 159 GLY A 175 1 17
HELIX 10 10 ARG A 185 MET A 189 1 5
HELIX 11 11 ARG A 194 ARG A 206 1 13
HELIX 12 12 THR A 215 GLU A 226 1 12
HELIX 13 13 THR A 229 VAL A 233 5 5
HELIX 14 14 ARG A 257 ASN A 270 1 14
HELIX 15 15 THR A 310 ASN A 318 1 9
HELIX 16 16 LYS A 330 THR A 335 1 6
HELIX 17 17 THR A 361 LYS A 365 5 5
HELIX 18 18 SER A 369 GLY A 384 1 16
HELIX 19 19 ALA A 394 HIS A 401 1 8
HELIX 20 20 MET A 404 MET A 429 1 26
HELIX 21 21 ARG A 477 GLY A 479 5 3
HELIX 22 22 ASP A 480 LEU A 489 1 10
SHEET 1 A 7 THR A 42 ILE A 45 0
SHEET 2 A 7 VAL A 461 VAL A 465 -1 O VAL A 461 N ILE A 45
SHEET 3 A 7 TYR A 432 THR A 436 -1 N ILE A 435 O ILE A 464
SHEET 4 A 7 THR A 6 LEU A 11 1 N ILE A 9 O ILE A 434
SHEET 5 A 7 LEU A 388 PHE A 393 1 O LEU A 391 N LEU A 8
SHEET 6 A 7 GLN A 322 GLU A 327 1 N LEU A 323 O ILE A 390
SHEET 7 A 7 GLU A 349 ILE A 354 1 O ARG A 352 N ARG A 324
SHEET 1 B 8 THR A 212 TYR A 213 0
SHEET 2 B 8 PHE A 236 VAL A 238 1 O ILE A 237 N TYR A 213
SHEET 3 B 8 GLN A 178 GLY A 184 -1 N VAL A 182 O PHE A 236
SHEET 4 B 8 VAL A 144 LEU A 150 1 N VAL A 146 O GLN A 178
SHEET 5 B 8 LEU A 111 LEU A 116 1 N LEU A 111 O TYR A 145
SHEET 6 B 8 ALA A 250 PHE A 253 1 O ALA A 250 N HIS A 112
SHEET 7 B 8 PHE A 285 THR A 288 1 O ALA A 287 N VAL A 251
SHEET 8 B 8 ALA A 299 ILE A 300 1 O ALA A 299 N TYR A 286
LINK OD1 ASP A 12 MN MN A 602 1555 1555 1.87
LINK OD2 ASP A 12 MN MN A 602 1555 1555 2.65
LINK OG SER A 62 MN MN A 602 1555 1555 1.82
LINK OD1 ASP A 397 MN MN A 601 1555 1555 2.02
LINK NE2 HIS A 401 MN MN A 601 1555 1555 2.19
LINK OD2 ASP A 438 MN MN A 602 1555 1555 1.94
LINK OD1 ASP A 438 MN MN A 602 1555 1555 2.79
LINK NE2 HIS A 439 MN MN A 602 1555 1555 2.03
LINK NE2 HIS A 456 MN MN A 601 1555 1555 2.22
LINK MN MN A 601 O HOH A 701 1555 1555 2.19
LINK MN MN A 601 O HOH A 702 1555 1555 2.02
LINK MN MN A 601 O HOH A 767 1555 1555 2.25
SITE 1 AC1 6 ASP A 397 HIS A 401 HIS A 456 HOH A 701
SITE 2 AC1 6 HOH A 702 HOH A 767
SITE 1 AC2 4 ASP A 12 SER A 62 ASP A 438 HIS A 439
SITE 1 AC3 8 HIS A 123 ARG A 153 ASP A 154 ARG A 185
SITE 2 AC3 8 ARG A 191 ARG A 257 ARG A 260 HOH A 972
CRYST1 73.637 82.841 89.145 90.00 90.00 90.00 P 21 21 21 4
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 0.013580 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011218 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
