HEADER ISOMERASE 19-JUL-00 1E58
TITLE E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.4.2.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: PGM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS PHOSPHOHISTIDINE, GLYCOLYSIS AND GLUCONEOGENESIS,
KEYWDS 2 PHOSPHOGLYCERATE MUTASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.BOND,W.N.HUNTER
REVDAT 2 24-FEB-09 1E58 1 VERSN
REVDAT 1 20-MAR-01 1E58 0
JRNL AUTH C.S.BOND,M.F.WHITE,W.N.HUNTER
JRNL TITL HIGH RESOLUTION STRUCTURE OF THE
JRNL TITL 2 PHOSPHOHISTIDINE-ACTIVATED FORM OF ESCHERICHIA
JRNL TITL 3 COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE.
JRNL REF J.BIOL.CHEM. V. 276 3247 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11038361
JRNL DOI 10.1074/JBC.M007318200
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1209
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.121
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 65026
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1195
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 62531
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2065
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 425
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2434.16
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1977.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 17
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 22606
REMARK 3 NUMBER OF RESTRAINTS : 27457
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.0314
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.079
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.085
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.076
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.042
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.080
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 (1995)53-56
REMARK 3 PHOSPHOHISTIDINE MODELLED AT 0.28 OCCUPANCY COUPLED TO A 0.72
REMARK 3 OCCUPANCY HISTIDINE WITH THREE WATER MOLECULES
REMARK 4
REMARK 4 1E58 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUL-00.
REMARK 100 THE PDBE ID CODE IS EBI-5176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 8.5
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) : 0.89
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67122
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.25
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.4
REMARK 200 DATA REDUNDANCY : 2
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.047
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 211
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 63
REMARK 200 DATA REDUNDANCY IN SHELL : 2
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.071
REMARK 200 <I/SIGMA(I)> FOR SHELL : 11
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL (PH 8.0),
REMARK 280 200 MM LI2SO4, 20% PEG 4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 30.78500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.50000
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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 61.57000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CATALYTIC ACTIVITY: 2-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE =
REMARK 400 3-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE.
REMARK 400 PATHWAY: GLYCOLYSIS.
REMARK 400 SIMILARITY: BELONGS TO THE PHOSPHOGLYCERATE MUTASE FAMILY.
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 ALA A 248
REMARK 465 LYS A 249
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 2262 - O HOH A 2272 2.04
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
REMARK 500 O HOH A 2262 O HOH A 2407 4456 2.09
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 20 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 89 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 115 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 115 NH1 - CZ - NH2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = 3.4 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 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 GLU A 88 152.30 -49.99
REMARK 500 THR A 167 -57.26 -126.18
REMARK 500 ALA A 182 -138.81 -149.79
REMARK 500 ASP A 218 -167.60 -79.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A3001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E59 RELATED DB: PDB
REMARK 900 E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE
REMARK 900 COMPLEXED WITH VANADATE
DBREF 1E58 A 1 249 UNP P62707 GPMA_ECOLI 1 249
SEQRES 1 A 249 ALA VAL THR LYS LEU VAL LEU VAL ARG NEP GLY GLU SER
SEQRES 2 A 249 GLN TRP ASN LYS GLU ASN ARG PHE THR GLY TRP TYR ASP
SEQRES 3 A 249 VAL ASP LEU SER GLU LYS GLY VAL SER GLU ALA LYS ALA
SEQRES 4 A 249 ALA GLY LYS LEU LEU LYS GLU GLU GLY TYR SER PHE ASP
SEQRES 5 A 249 PHE ALA TYR THR SER VAL LEU LYS ARG ALA ILE HIS THR
SEQRES 6 A 249 LEU TRP ASN VAL LEU ASP GLU LEU ASP GLN ALA TRP LEU
SEQRES 7 A 249 PRO VAL GLU LYS SER TRP LYS LEU ASN GLU ARG HIS TYR
SEQRES 8 A 249 GLY ALA LEU GLN GLY LEU ASN LYS ALA GLU THR ALA GLU
SEQRES 9 A 249 LYS TYR GLY ASP GLU GLN VAL LYS GLN TRP ARG ARG GLY
SEQRES 10 A 249 PHE ALA VAL THR PRO PRO GLU LEU THR LYS ASP ASP GLU
SEQRES 11 A 249 ARG TYR PRO GLY HIS ASP PRO ARG TYR ALA LYS LEU SER
SEQRES 12 A 249 GLU LYS GLU LEU PRO LEU THR GLU SER LEU ALA LEU THR
SEQRES 13 A 249 ILE ASP ARG VAL ILE PRO TYR TRP ASN GLU THR ILE LEU
SEQRES 14 A 249 PRO ARG MET LYS SER GLY GLU ARG VAL ILE ILE ALA ALA
SEQRES 15 A 249 HIS GLY ASN SER LEU ARG ALA LEU VAL LYS TYR LEU ASP
SEQRES 16 A 249 ASN MET SER GLU GLU GLU ILE LEU GLU LEU ASN ILE PRO
SEQRES 17 A 249 THR GLY VAL PRO LEU VAL TYR GLU PHE ASP GLU ASN PHE
SEQRES 18 A 249 LYS PRO LEU LYS ARG TYR TYR LEU GLY ASN ALA ASP GLU
SEQRES 19 A 249 ILE ALA ALA LYS ALA ALA ALA VAL ALA ASN GLN GLY LYS
SEQRES 20 A 249 ALA LYS
MODRES 1E58 NEP A 10 HIS N1-PHOSPHONOHISTIDINE
HET NEP A 10 19
HET SO4 A1001 5
HET SO4 A1002 5
HET CL A3001 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM NEP N1-PHOSPHONOHISTIDINE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 3 CL CL 1-
FORMUL 4 NEP C6 H10 N3 O5 P
FORMUL 5 HOH *425(H2 O1)
HELIX 1 1 SER A 13 GLU A 18 1 6
HELIX 2 2 SER A 30 GLU A 47 1 18
HELIX 3 3 LEU A 59 ASP A 74 1 16
HELIX 4 4 TRP A 84 ASN A 87 5 4
HELIX 5 5 TYR A 91 GLN A 95 5 5
HELIX 6 6 ASN A 98 GLY A 107 1 10
HELIX 7 7 GLY A 107 GLY A 117 1 11
HELIX 8 8 TYR A 132 ASP A 136 5 5
HELIX 9 9 ASP A 136 ALA A 140 5 5
HELIX 10 10 SER A 152 THR A 167 1 16
HELIX 11 11 THR A 167 SER A 174 1 8
HELIX 12 12 HIS A 183 ASP A 195 1 13
HELIX 13 13 SER A 198 LEU A 205 1 8
HELIX 14 14 ASN A 231 ALA A 239 1 9
SHEET 1 A 6 VAL A 80 LYS A 82 0
SHEET 2 A 6 PHE A 53 THR A 56 1 N ALA A 54 O GLU A 81
SHEET 3 A 6 VAL A 178 ALA A 182 1 N ILE A 179 O PHE A 53
SHEET 4 A 6 THR A 3 ARG A 9 1 N VAL A 6 O VAL A 178
SHEET 5 A 6 LEU A 213 PHE A 217 -1 N PHE A 217 O THR A 3
SHEET 6 A 6 PRO A 223 TYR A 228 -1 N TYR A 227 O VAL A 214
LINK C ARG A 9 N NEP A 10 1555 1555 1.35
LINK C NEP A 10 N GLY A 11 1555 1555 1.33
SITE 1 AC1 15 NEP A 10 ARG A 20 PHE A 21 THR A 22
SITE 2 AC1 15 GLY A 23 ARG A 61 GLU A 88 TYR A 91
SITE 3 AC1 15 HOH A2033 HOH A2211 HOH A2339 HOH A2417
SITE 4 AC1 15 HOH A2418 HOH A2421 HOH A2424
SITE 1 AC2 9 TYR A 91 ARG A 115 ARG A 116 HOH A2367
SITE 2 AC2 9 HOH A2418 HOH A2419 HOH A2420 HOH A2421
SITE 3 AC2 9 HOH A2422
SITE 1 AC3 2 TRP A 67 LYS A 82
CRYST1 61.570 113.000 40.260 90.00 90.00 90.00 P 21 21 2 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 0.016242 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
