HEADER ISOMERASE 17-SEP-13 4MRQ
TITLE CRYSTAL STRUCTURE OF WILD-TYPE UNPHOSPHORYLATED PMM/PGM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 9-463;
COMPND 5 SYNONYM: PMM / PGM;
COMPND 6 EC: 5.4.2.2, 5.4.2.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: ALGC, PA5322;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LEE,L.BEAMER
REVDAT 3 20-SEP-23 4MRQ 1 REMARK LINK
REVDAT 2 05-NOV-14 4MRQ 1 JRNL
REVDAT 1 08-JAN-14 4MRQ 0
JRNL AUTH Y.LEE,M.T.VILLAR,A.ARTIGUES,L.J.BEAMER
JRNL TITL PROMOTION OF ENZYME FLEXIBILITY BY DEPHOSPHORYLATION AND
JRNL TITL 2 COUPLING TO THE CATALYTIC MECHANISM OF A PHOSPHOHEXOMUTASE.
JRNL REF J.BIOL.CHEM. V. 289 4674 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24403075
JRNL DOI 10.1074/JBC.M113.532226
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 37555
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) : 0.165
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1879
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2518
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3439
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 218
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.17000
REMARK 3 B22 (A**2) : -1.27000
REMARK 3 B33 (A**2) : 2.44000
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): 0.138
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.425
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3649 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4945 ; 1.517 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 476 ; 5.789 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;34.404 ;24.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 585 ;13.671 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;19.180 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 566 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2736 ; 0.008 ; 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): 1841 ; 1.377 ; 2.092
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2305 ; 1.963 ; 3.128
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1808 ; 2.256 ; 2.466
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 366
REMARK 3 ORIGIN FOR THE GROUP (A): 53.2359 53.4760 5.6057
REMARK 3 T TENSOR
REMARK 3 T11: 0.0120 T22: 0.0150
REMARK 3 T33: 0.0167 T12: 0.0001
REMARK 3 T13: 0.0078 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.8732 L22: 0.7413
REMARK 3 L33: 0.3954 L12: -0.2572
REMARK 3 L13: -0.1796 L23: 0.3436
REMARK 3 S TENSOR
REMARK 3 S11: -0.0315 S12: -0.0234 S13: -0.0395
REMARK 3 S21: 0.0582 S22: 0.0373 S23: 0.0014
REMARK 3 S31: 0.0316 S32: 0.0485 S33: -0.0058
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 367 A 463
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0277 53.8118 29.8612
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.0119
REMARK 3 T33: 0.0111 T12: -0.0045
REMARK 3 T13: 0.0046 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.6833 L22: 3.9444
REMARK 3 L33: 1.4776 L12: 0.4364
REMARK 3 L13: -0.0250 L23: -1.6273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0858 S12: -0.0085 S13: -0.0109
REMARK 3 S21: 0.3501 S22: -0.1086 S23: -0.0155
REMARK 3 S31: -0.1990 S32: 0.0363 S33: 0.0228
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4MRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37720
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1K35
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: PH 7.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 35.27050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.17450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.00150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.17450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.27050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.00150
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 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 ARG A 20 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 30 CG CD OE1 OE2
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 LYS A 316 CG CD CE NZ
REMARK 470 GLN A 397 CG CD OE1 NE2
REMARK 470 LYS A 415 CG CD CE NZ
REMARK 470 GLU A 438 CG CD OE1 OE2
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 25 -92.20 -120.64
REMARK 500 SER A 108 -113.89 60.12
REMARK 500 ASN A 128 -119.32 56.60
REMARK 500 ILE A 187 -33.11 -145.07
REMARK 500 ILE A 187 -41.10 -141.23
REMARK 500 PHE A 210 63.42 38.32
REMARK 500 ASN A 212 -145.93 -107.65
REMARK 500 TRP A 336 -149.95 -147.89
REMARK 500 ASP A 341 104.75 -163.17
REMARK 500 VAL A 380 -128.33 -111.66
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 242 OD2
REMARK 620 2 ASP A 244 OD2 100.2
REMARK 620 3 ASP A 246 OD1 105.8 101.8
REMARK 620 4 TLA A 502 O41 116.9 104.6 123.8
REMARK 620 5 TLA A 502 O4 87.2 157.2 96.8 53.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 514
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K35 RELATED DB: PDB
REMARK 900 RELATED ID: 1K2Y RELATED DB: PDB
REMARK 900 RELATED ID: 1P5D RELATED DB: PDB
REMARK 900 RELATED ID: 1P5G RELATED DB: PDB
DBREF 4MRQ A 9 463 UNP P26276 ALGC_PSEAE 9 463
SEQRES 1 A 455 LEU PRO ALA SER ILE PHE ARG ALA TYR ASP ILE ARG GLY
SEQRES 2 A 455 VAL VAL GLY ASP THR LEU THR ALA GLU THR ALA TYR TRP
SEQRES 3 A 455 ILE GLY ARG ALA ILE GLY SER GLU SER LEU ALA ARG GLY
SEQRES 4 A 455 GLU PRO CYS VAL ALA VAL GLY ARG ASP GLY ARG LEU SER
SEQRES 5 A 455 GLY PRO GLU LEU VAL LYS GLN LEU ILE GLN GLY LEU VAL
SEQRES 6 A 455 ASP CYS GLY CYS GLN VAL SER ASP VAL GLY MET VAL PRO
SEQRES 7 A 455 THR PRO VAL LEU TYR TYR ALA ALA ASN VAL LEU GLU GLY
SEQRES 8 A 455 LYS SER GLY VAL MET LEU THR GLY SER HIS ASN PRO PRO
SEQRES 9 A 455 ASP TYR ASN GLY PHE LYS ILE VAL VAL ALA GLY GLU THR
SEQRES 10 A 455 LEU ALA ASN GLU GLN ILE GLN ALA LEU ARG GLU ARG ILE
SEQRES 11 A 455 GLU LYS ASN ASP LEU ALA SER GLY VAL GLY SER VAL GLU
SEQRES 12 A 455 GLN VAL ASP ILE LEU PRO ARG TYR PHE LYS GLN ILE ARG
SEQRES 13 A 455 ASP ASP ILE ALA MET ALA LYS PRO MET LYS VAL VAL VAL
SEQRES 14 A 455 ASP CYS GLY ASN GLY VAL ALA GLY VAL ILE ALA PRO GLN
SEQRES 15 A 455 LEU ILE GLU ALA LEU GLY CYS SER VAL ILE PRO LEU TYR
SEQRES 16 A 455 CYS GLU VAL ASP GLY ASN PHE PRO ASN HIS HIS PRO ASP
SEQRES 17 A 455 PRO GLY LYS PRO GLU ASN LEU LYS ASP LEU ILE ALA LYS
SEQRES 18 A 455 VAL LYS ALA GLU ASN ALA ASP LEU GLY LEU ALA PHE ASP
SEQRES 19 A 455 GLY ASP GLY ASP ARG VAL GLY VAL VAL THR ASN THR GLY
SEQRES 20 A 455 THR ILE ILE TYR PRO ASP ARG LEU LEU MET LEU PHE ALA
SEQRES 21 A 455 LYS ASP VAL VAL SER ARG ASN PRO GLY ALA ASP ILE ILE
SEQRES 22 A 455 PHE ASP VAL LYS CYS THR ARG ARG LEU ILE ALA LEU ILE
SEQRES 23 A 455 SER GLY TYR GLY GLY ARG PRO VAL MET TRP LYS THR GLY
SEQRES 24 A 455 HIS SER LEU ILE LYS LYS LYS MET LYS GLU THR GLY ALA
SEQRES 25 A 455 LEU LEU ALA GLY GLU MET SER GLY HIS VAL PHE PHE LYS
SEQRES 26 A 455 GLU ARG TRP PHE GLY PHE ASP ASP GLY ILE TYR SER ALA
SEQRES 27 A 455 ALA ARG LEU LEU GLU ILE LEU SER GLN ASP GLN ARG ASP
SEQRES 28 A 455 SER GLU HIS VAL PHE SER ALA PHE PRO SER ASP ILE SER
SEQRES 29 A 455 THR PRO GLU ILE ASN ILE THR VAL THR GLU ASP SER LYS
SEQRES 30 A 455 PHE ALA ILE ILE GLU ALA LEU GLN ARG ASP ALA GLN TRP
SEQRES 31 A 455 GLY GLU GLY ASN ILE THR THR LEU ASP GLY VAL ARG VAL
SEQRES 32 A 455 ASP TYR PRO LYS GLY TRP GLY LEU VAL ARG ALA SER ASN
SEQRES 33 A 455 THR THR PRO VAL LEU VAL LEU ARG PHE GLU ALA ASP THR
SEQRES 34 A 455 GLU GLU GLU LEU GLU ARG ILE LYS THR VAL PHE ARG ASN
SEQRES 35 A 455 GLN LEU LYS ALA VAL ASP SER SER LEU PRO VAL PRO PHE
HET ZN A 501 1
HET TLA A 502 10
HET EDO A 503 4
HET PEG A 504 7
HET PEG A 505 7
HET PEG A 506 7
HET PEG A 507 7
HET PEG A 508 7
HET PGE A 509 10
HET PGE A 510 10
HET PGE A 511 10
HET EDO A 512 4
HET EDO A 513 4
HET EDO A 514 4
HETNAM ZN ZINC ION
HETNAM TLA L(+)-TARTARIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ZN ZN 2+
FORMUL 3 TLA C4 H6 O6
FORMUL 4 EDO 4(C2 H6 O2)
FORMUL 5 PEG 5(C4 H10 O3)
FORMUL 10 PGE 3(C6 H14 O4)
FORMUL 16 HOH *218(H2 O)
HELIX 1 1 PRO A 10 PHE A 14 5 5
HELIX 2 2 THR A 28 ARG A 46 1 19
HELIX 3 3 SER A 60 ASP A 74 1 15
HELIX 4 4 PRO A 86 LEU A 97 1 12
HELIX 5 5 ASN A 128 ASN A 141 1 14
HELIX 6 6 ILE A 155 ILE A 167 1 13
HELIX 7 7 GLY A 182 VAL A 186 5 5
HELIX 8 8 ILE A 187 LEU A 195 1 9
HELIX 9 9 LYS A 219 ASN A 222 5 4
HELIX 10 10 LEU A 223 GLU A 233 1 11
HELIX 11 11 TYR A 259 ASN A 275 1 17
HELIX 12 12 THR A 287 TYR A 297 1 11
HELIX 13 13 GLY A 307 GLY A 319 1 13
HELIX 14 14 ASP A 341 SER A 354 1 14
HELIX 15 15 ASP A 359 ALA A 366 1 8
HELIX 16 16 SER A 384 ALA A 396 1 13
HELIX 17 17 THR A 437 ASP A 456 1 20
SHEET 1 A 3 ILE A 19 VAL A 22 0
SHEET 2 A 3 TYR A 114 VAL A 121 -1 O ASN A 115 N GLY A 21
SHEET 3 A 3 GLU A 124 THR A 125 -1 O GLU A 124 N VAL A 121
SHEET 1 B 6 ILE A 19 VAL A 22 0
SHEET 2 B 6 TYR A 114 VAL A 121 -1 O ASN A 115 N GLY A 21
SHEET 3 B 6 SER A 101 LEU A 105 -1 N GLY A 102 O VAL A 120
SHEET 4 B 6 CYS A 50 ARG A 55 1 N GLY A 54 O LEU A 105
SHEET 5 B 6 GLN A 78 MET A 84 1 O SER A 80 N VAL A 53
SHEET 6 B 6 SER A 149 GLN A 152 1 O SER A 149 N VAL A 79
SHEET 1 C 5 CYS A 197 LEU A 202 0
SHEET 2 C 5 MET A 173 ASP A 178 1 N VAL A 175 O SER A 198
SHEET 3 C 5 LEU A 237 PHE A 241 1 O LEU A 239 N ASP A 178
SHEET 4 C 5 VAL A 248 THR A 252 -1 O GLY A 249 N ALA A 240
SHEET 5 C 5 ILE A 257 ILE A 258 -1 O ILE A 258 N VAL A 250
SHEET 1 D 4 ARG A 300 TRP A 304 0
SHEET 2 D 4 ASP A 279 ASP A 283 1 N PHE A 282 O TRP A 304
SHEET 3 D 4 LEU A 322 GLY A 324 1 O LEU A 322 N ILE A 281
SHEET 4 D 4 VAL A 330 PHE A 332 -1 O PHE A 331 N ALA A 323
SHEET 1 E 3 ILE A 371 SER A 372 0
SHEET 2 E 3 VAL A 428 ALA A 435 -1 O ALA A 435 N ILE A 371
SHEET 3 E 3 ILE A 376 THR A 379 -1 N ILE A 376 O LEU A 431
SHEET 1 F 5 ILE A 371 SER A 372 0
SHEET 2 F 5 VAL A 428 ALA A 435 -1 O ALA A 435 N ILE A 371
SHEET 3 F 5 GLY A 416 ALA A 422 -1 N ARG A 421 O VAL A 430
SHEET 4 F 5 VAL A 409 TYR A 413 -1 N TYR A 413 O GLY A 416
SHEET 5 F 5 ASN A 402 THR A 404 -1 N THR A 404 O ARG A 410
LINK OD2 ASP A 242 ZN ZN A 501 1555 1555 1.89
LINK OD2 ASP A 244 ZN ZN A 501 1555 1555 2.06
LINK OD1 ASP A 246 ZN ZN A 501 1555 1555 1.88
LINK ZN ZN A 501 O41 TLA A 502 1555 1555 1.98
LINK ZN ZN A 501 O4 TLA A 502 1555 1555 2.63
SITE 1 AC1 5 LYS A 118 ASP A 242 ASP A 244 ASP A 246
SITE 2 AC1 5 TLA A 502
SITE 1 AC2 11 ARG A 15 SER A 108 HIS A 109 LYS A 118
SITE 2 AC2 11 ASP A 242 ASP A 244 ASP A 246 ARG A 247
SITE 3 AC2 11 HIS A 329 ZN A 501 HOH A 745
SITE 1 AC3 3 THR A 404 THR A 405 LEU A 406
SITE 1 AC4 2 GLU A 375 ARG A 432
SITE 1 AC5 3 GLU A 30 GLN A 67 PGE A 510
SITE 1 AC6 1 ILE A 138
SITE 1 AC7 2 TYR A 92 VAL A 96
SITE 1 AC8 4 ASN A 128 LYS A 305 LEU A 310 HOH A 684
SITE 1 AC9 4 LEU A 266 LYS A 269 SER A 273 HOH A 655
SITE 1 BC1 3 ASP A 74 GLY A 146 PEG A 505
SITE 1 BC2 6 ARG A 288 ALA A 292 ASP A 383 PRO A 414
SITE 2 BC2 6 HOH A 814 HOH A 817
SITE 1 BC3 5 PRO A 301 VAL A 302 MET A 303 HOH A 735
SITE 2 BC3 5 HOH A 781
SITE 1 BC4 4 ARG A 421 SER A 423 ASN A 424 THR A 425
SITE 1 BC5 2 ARG A 335 PHE A 337
CRYST1 70.541 72.003 92.349 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 0.014176 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013888 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010828 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
