HEADER LYASE 29-NOV-01 1KHF
TITLE PEPCK COMPLEX WITH PEP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC (GTP);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOENOLPYRUVATE CARBOXYLASE, PEPCK, PEPCK-C;
COMPND 5 EC: 4.1.1.32;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PCK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUCONEOGENESIS, P-LOOP, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.DUNTEN,C.BELUNIS,R.CROWTHER,K.HOLLFELDER,U.KAMMLOTT,W.LEVIN,
AUTHOR 2 H.MICHEL,G.B.RAMSEY,A.SWAIN,D.WEBER,S.J.WERTHEIMER
REVDAT 4 14-FEB-24 1KHF 1 REMARK SEQADV LINK
REVDAT 3 11-OCT-17 1KHF 1 REMARK
REVDAT 2 24-FEB-09 1KHF 1 VERSN
REVDAT 1 27-FEB-02 1KHF 0
JRNL AUTH P.DUNTEN,C.BELUNIS,R.CROWTHER,K.HOLLFELDER,U.KAMMLOTT,
JRNL AUTH 2 W.LEVIN,H.MICHEL,G.B.RAMSEY,A.SWAIN,D.WEBER,S.J.WERTHEIMER
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC PHOSPHOENOLPYRUVATE
JRNL TITL 2 CARBOXYKINASE REVEALS A NEW GTP-BINDING SITE.
JRNL REF J.MOL.BIOL. V. 316 257 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11851336
JRNL DOI 10.1006/JMBI.2001.5364
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 34451
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1724
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4721
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 164
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : 0.67000
REMARK 3 B33 (A**2) : -0.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
REMARK 3 B23 (A**2) : -0.40000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.239
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.202
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.562
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.028 ; 0.021
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.392 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.671 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.621 ; 4.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KHF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000014964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 6.0
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34451
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG1500, MES, DTT, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 GLY A -2
REMARK 465 GLU A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 ASN A 7
REMARK 465 GLY A 8
REMARK 465 LEU A 9
REMARK 465 THR A 465
REMARK 465 ALA A 466
REMARK 465 ALA A 467
REMARK 465 ALA A 468
REMARK 465 GLU A 469
REMARK 465 HIS A 470
REMARK 465 LYS A 471
REMARK 465 GLY A 472
REMARK 465 LYS A 547
REMARK 465 ALA A 548
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 VAL A 95 CB VAL A 95 CG1 0.127
REMARK 500 TYR A 140 CD1 TYR A 140 CE1 0.109
REMARK 500 TRP A 516 CE3 TRP A 516 CZ3 0.112
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 ASP A 84 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 253 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 253 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 318 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 365 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 395 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 520 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 545 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 562 CB - CG - OD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 591 CB - CG - OD2 ANGL. DEV. = 8.8 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 243 -77.63 -85.02
REMARK 500 LEU A 248 -66.07 -101.48
REMARK 500 ASP A 311 -49.07 -140.10
REMARK 500 PHE A 333 75.60 -107.59
REMARK 500 ASN A 344 69.26 -168.39
REMARK 500 PHE A 480 14.82 53.96
REMARK 500 PHE A 530 -132.18 56.62
REMARK 500 ASN A 601 -119.96 52.87
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 701 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 244 NZ
REMARK 620 2 HIS A 264 NE2 84.9
REMARK 620 3 ASP A 311 OD1 91.8 83.7
REMARK 620 4 HOH A 732 O 99.1 176.0 96.0
REMARK 620 5 HOH A 797 O 92.8 96.1 175.4 83.8
REMARK 620 6 HOH A 804 O 176.2 91.5 86.6 84.5 88.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 702 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PEP A 703 O2
REMARK 620 2 PEP A 703 O1P 57.3
REMARK 620 3 HOH A 813 O 122.8 116.3
REMARK 620 4 HOH A 861 O 152.6 115.8 84.5
REMARK 620 N 1 2 3
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 705
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KHB RELATED DB: PDB
REMARK 900 PEPCK COMPLEX WITH NONHYDROLYZABLE GTP ANALOG, NATIVE DATA
REMARK 900 RELATED ID: 1KHE RELATED DB: PDB
REMARK 900 PEPCK COMPLEX WITH NONHYDROLYZABLE GTP ANALOG, MAD DATA
REMARK 900 RELATED ID: 1KHG RELATED DB: PDB
REMARK 900 PEPCK
DBREF 1KHF A 1 622 UNP P35558 PPCKC_HUMAN 1 622
SEQADV 1KHF GLY A -2 UNP P35558 CLONING ARTIFACT
SEQADV 1KHF GLU A -1 UNP P35558 CLONING ARTIFACT
SEQADV 1KHF LEU A 0 UNP P35558 CLONING ARTIFACT
SEQADV 1KHF VAL A 267 UNP P35558 ILE 267 VARIANT
SEQADV 1KHF ASP A 586 UNP P35558 GLU 586 VARIANT
SEQADV 1KHF VAL A 597 UNP P35558 GLU 597 VARIANT
SEQRES 1 A 625 GLY GLU LEU MET PRO PRO GLN LEU GLN ASN GLY LEU ASN
SEQRES 2 A 625 LEU SER ALA LYS VAL VAL GLN GLY SER LEU ASP SER LEU
SEQRES 3 A 625 PRO GLN ALA VAL ARG GLU PHE LEU GLU ASN ASN ALA GLU
SEQRES 4 A 625 LEU CYS GLN PRO ASP HIS ILE HIS ILE CYS ASP GLY SER
SEQRES 5 A 625 GLU GLU GLU ASN GLY ARG LEU LEU GLY GLN MET GLU GLU
SEQRES 6 A 625 GLU GLY ILE LEU ARG ARG LEU LYS LYS TYR ASP ASN CYS
SEQRES 7 A 625 TRP LEU ALA LEU THR ASP PRO ARG ASP VAL ALA ARG ILE
SEQRES 8 A 625 GLU SER LYS THR VAL ILE VAL THR GLN GLU GLN ARG ASP
SEQRES 9 A 625 THR VAL PRO ILE PRO LYS THR GLY LEU SER GLN LEU GLY
SEQRES 10 A 625 ARG TRP MET SER GLU GLU ASP PHE GLU LYS ALA PHE ASN
SEQRES 11 A 625 ALA ARG PHE PRO GLY CYS MET LYS GLY ARG THR MET TYR
SEQRES 12 A 625 VAL ILE PRO PHE SER MET GLY PRO LEU GLY SER PRO LEU
SEQRES 13 A 625 SER LYS ILE GLY ILE GLU LEU THR ASP SER PRO TYR VAL
SEQRES 14 A 625 VAL ALA SER MET ARG ILE MET THR ARG MET GLY THR PRO
SEQRES 15 A 625 VAL LEU GLU ALA LEU GLY ASP GLY GLU PHE VAL LYS CYS
SEQRES 16 A 625 LEU HIS SER VAL GLY CYS PRO LEU PRO LEU GLN LYS PRO
SEQRES 17 A 625 LEU VAL ASN ASN TRP PRO CYS ASN PRO GLU LEU THR LEU
SEQRES 18 A 625 ILE ALA HIS LEU PRO ASP ARG ARG GLU ILE ILE SER PHE
SEQRES 19 A 625 GLY SER GLY TYR GLY GLY ASN SER LEU LEU GLY LYS LYS
SEQRES 20 A 625 CYS PHE ALA LEU ARG MET ALA SER ARG LEU ALA LYS GLU
SEQRES 21 A 625 GLU GLY TRP LEU ALA GLU HIS MET LEU VAL LEU GLY ILE
SEQRES 22 A 625 THR ASN PRO GLU GLY GLU LYS LYS TYR LEU ALA ALA ALA
SEQRES 23 A 625 PHE PRO SER ALA CYS GLY LYS THR ASN LEU ALA MET MET
SEQRES 24 A 625 ASN PRO SER LEU PRO GLY TRP LYS VAL GLU CYS VAL GLY
SEQRES 25 A 625 ASP ASP ILE ALA TRP MET LYS PHE ASP ALA GLN GLY HIS
SEQRES 26 A 625 LEU ARG ALA ILE ASN PRO GLU ASN GLY PHE PHE GLY VAL
SEQRES 27 A 625 ALA PRO GLY THR SER VAL LYS THR ASN PRO ASN ALA ILE
SEQRES 28 A 625 LYS THR ILE GLN LYS ASN THR ILE PHE THR ASN VAL ALA
SEQRES 29 A 625 GLU THR SER ASP GLY GLY VAL TYR TRP GLU GLY ILE ASP
SEQRES 30 A 625 GLU PRO LEU ALA SER GLY VAL THR ILE THR SER TRP LYS
SEQRES 31 A 625 ASN LYS GLU TRP SER SER GLU ASP GLY GLU PRO CYS ALA
SEQRES 32 A 625 HIS PRO ASN SER ARG PHE CYS THR PRO ALA SER GLN CYS
SEQRES 33 A 625 PRO ILE ILE ASP ALA ALA TRP GLU SER PRO GLU GLY VAL
SEQRES 34 A 625 PRO ILE GLU GLY ILE ILE PHE GLY GLY ARG ARG PRO ALA
SEQRES 35 A 625 GLY VAL PRO LEU VAL TYR GLU ALA LEU SER TRP GLN HIS
SEQRES 36 A 625 GLY VAL PHE VAL GLY ALA ALA MET ARG SER GLU ALA THR
SEQRES 37 A 625 ALA ALA ALA GLU HIS LYS GLY LYS ILE ILE MET HIS ASP
SEQRES 38 A 625 PRO PHE ALA MET ARG PRO PHE PHE GLY TYR ASN PHE GLY
SEQRES 39 A 625 LYS TYR LEU ALA HIS TRP LEU SER MET ALA GLN HIS PRO
SEQRES 40 A 625 ALA ALA LYS LEU PRO LYS ILE PHE HIS VAL ASN TRP PHE
SEQRES 41 A 625 ARG LYS ASP LYS GLU GLY LYS PHE LEU TRP PRO GLY PHE
SEQRES 42 A 625 GLY GLU ASN SER ARG VAL LEU GLU TRP MET PHE ASN ARG
SEQRES 43 A 625 ILE ASP GLY LYS ALA SER THR LYS LEU THR PRO ILE GLY
SEQRES 44 A 625 TYR ILE PRO LYS GLU ASP ALA LEU ASN LEU LYS GLY LEU
SEQRES 45 A 625 GLY HIS ILE ASN MET MET GLU LEU PHE SER ILE SER LYS
SEQRES 46 A 625 GLU PHE TRP ASP LYS GLU VAL GLU ASP ILE GLU LYS TYR
SEQRES 47 A 625 LEU VAL ASP GLN VAL ASN ALA ASP LEU PRO CYS GLU ILE
SEQRES 48 A 625 GLU ARG GLU ILE LEU ALA LEU LYS GLN ARG ILE SER GLN
SEQRES 49 A 625 MET
HET MN A 701 1
HET NA A 702 1
HET PEP A 703 10
HET EDO A 704 4
HET EDO A 705 4
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
HETNAM PEP PHOSPHOENOLPYRUVATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MN MN 2+
FORMUL 3 NA NA 1+
FORMUL 4 PEP C3 H5 O6 P
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 7 HOH *164(H2 O)
HELIX 1 1 ASN A 10 ALA A 13 5 4
HELIX 2 2 SER A 19 LEU A 23 5 5
HELIX 3 3 PRO A 24 GLN A 39 1 16
HELIX 4 4 SER A 49 GLU A 63 1 15
HELIX 5 5 ILE A 88 SER A 90 5 3
HELIX 6 6 GLU A 98 VAL A 103 1 6
HELIX 7 7 SER A 118 ALA A 128 1 11
HELIX 8 8 SER A 163 THR A 174 1 12
HELIX 9 9 GLY A 177 GLY A 185 1 9
HELIX 10 10 ASN A 213 THR A 217 5 5
HELIX 11 11 PRO A 223 ARG A 225 5 3
HELIX 12 12 TYR A 235 LEU A 240 1 6
HELIX 13 13 LEU A 248 GLU A 258 1 11
HELIX 14 14 GLY A 289 MET A 295 1 7
HELIX 15 15 ASN A 344 ILE A 351 1 8
HELIX 16 16 SER A 392 GLY A 396 5 5
HELIX 17 17 SER A 411 CYS A 413 5 3
HELIX 18 18 SER A 449 ALA A 459 1 11
HELIX 19 19 PRO A 479 MET A 482 5 4
HELIX 20 20 ASN A 489 MET A 500 1 12
HELIX 21 21 ALA A 501 HIS A 503 5 3
HELIX 22 22 GLY A 529 GLY A 531 5 3
HELIX 23 23 GLU A 532 ASP A 545 1 14
HELIX 24 24 ASN A 573 PHE A 578 1 6
HELIX 25 25 SER A 581 ASN A 601 1 21
HELIX 26 26 ALA A 602 LEU A 604 5 3
HELIX 27 27 PRO A 605 GLN A 621 1 17
SHEET 1 A 9 TRP A 116 MET A 117 0
SHEET 2 A 9 THR A 92 VAL A 95 1 N ILE A 94 O MET A 117
SHEET 3 A 9 LEU A 218 LEU A 222 1 O ILE A 219 N VAL A 93
SHEET 4 A 9 GLU A 227 PHE A 231 -1 O ILE A 229 N ALA A 220
SHEET 5 A 9 VAL A 190 SER A 195 1 N LEU A 193 O SER A 230
SHEET 6 A 9 LYS A 155 THR A 161 1 N LEU A 160 O CYS A 192
SHEET 7 A 9 THR A 138 MET A 146 -1 N MET A 146 O LYS A 155
SHEET 8 A 9 HIS A 42 ILE A 45 1 N HIS A 42 O MET A 139
SHEET 9 A 9 VAL A 15 GLN A 17 1 N GLN A 17 O ILE A 45
SHEET 1 B 8 TRP A 116 MET A 117 0
SHEET 2 B 8 THR A 92 VAL A 95 1 N ILE A 94 O MET A 117
SHEET 3 B 8 LEU A 218 LEU A 222 1 O ILE A 219 N VAL A 93
SHEET 4 B 8 GLU A 227 PHE A 231 -1 O ILE A 229 N ALA A 220
SHEET 5 B 8 VAL A 190 SER A 195 1 N LEU A 193 O SER A 230
SHEET 6 B 8 LYS A 155 THR A 161 1 N LEU A 160 O CYS A 192
SHEET 7 B 8 THR A 138 MET A 146 -1 N MET A 146 O LYS A 155
SHEET 8 B 8 ARG A 175 MET A 176 -1 O ARG A 175 N SER A 145
SHEET 1 C 5 LEU A 66 ARG A 68 0
SHEET 2 C 5 TRP A 76 ALA A 78 -1 O LEU A 77 N ARG A 67
SHEET 3 C 5 ILE A 356 THR A 358 1 O PHE A 357 N TRP A 76
SHEET 4 C 5 ARG A 405 PRO A 409 -1 O ARG A 405 N THR A 358
SHEET 5 C 5 GLY A 331 VAL A 335 -1 N PHE A 332 O THR A 408
SHEET 1 D 7 LYS A 304 GLY A 309 0
SHEET 2 D 7 LEU A 266 THR A 271 -1 N THR A 271 O LYS A 304
SHEET 3 D 7 LYS A 277 ALA A 283 -1 O LYS A 278 N ILE A 270
SHEET 4 D 7 VAL A 426 PHE A 433 1 O GLY A 430 N ALA A 281
SHEET 5 D 7 LEU A 323 ILE A 326 -1 N ALA A 325 O VAL A 426
SHEET 6 D 7 ALA A 313 PHE A 317 -1 N TRP A 314 O ILE A 326
SHEET 7 D 7 LEU A 261 GLU A 263 -1 N GLU A 263 O ALA A 313
SHEET 1 E 6 LYS A 304 GLY A 309 0
SHEET 2 E 6 LEU A 266 THR A 271 -1 N THR A 271 O LYS A 304
SHEET 3 E 6 LYS A 277 ALA A 283 -1 O LYS A 278 N ILE A 270
SHEET 4 E 6 VAL A 426 PHE A 433 1 O GLY A 430 N ALA A 281
SHEET 5 E 6 LYS A 510 VAL A 514 1 O PHE A 512 N PHE A 433
SHEET 6 E 6 VAL A 444 GLU A 446 -1 N TYR A 445 O HIS A 513
SHEET 1 F 4 VAL A 368 TYR A 369 0
SHEET 2 F 4 ALA A 361 THR A 363 -1 N ALA A 361 O TYR A 369
SHEET 3 F 4 ILE A 383 THR A 384 -1 O THR A 384 N GLU A 362
SHEET 4 F 4 GLU A 390 TRP A 391 -1 O TRP A 391 N ILE A 383
SHEET 1 G 2 ARG A 461 GLU A 463 0
SHEET 2 G 2 ILE A 475 HIS A 477 -1 O MET A 476 N SER A 462
SHEET 1 H 2 THR A 550 THR A 553 0
SHEET 2 H 2 GLY A 556 PRO A 559 -1 O ILE A 558 N LYS A 551
LINK NZ LYS A 244 MN MN A 701 1555 1555 2.32
LINK NE2 HIS A 264 MN MN A 701 1555 1555 2.22
LINK OD1 ASP A 311 MN MN A 701 1555 1555 2.19
LINK MN MN A 701 O HOH A 732 1555 1555 2.20
LINK MN MN A 701 O HOH A 797 1555 1555 2.24
LINK MN MN A 701 O HOH A 804 1555 1555 2.25
LINK NA NA A 702 O2 PEP A 703 1555 1555 2.76
LINK NA NA A 702 O1P PEP A 703 1555 1555 2.94
LINK NA NA A 702 O HOH A 813 1555 1555 2.68
LINK NA NA A 702 O HOH A 861 1555 1555 2.96
CISPEP 1 LEU A 200 PRO A 201 0 11.57
SITE 1 AC1 6 LYS A 244 HIS A 264 ASP A 311 HOH A 732
SITE 2 AC1 6 HOH A 797 HOH A 804
SITE 1 AC2 3 PEP A 703 HOH A 813 HOH A 861
SITE 1 AC3 12 ALA A 86 ARG A 87 TYR A 235 GLY A 236
SITE 2 AC3 12 GLY A 237 LYS A 244 ASN A 403 ARG A 405
SITE 3 AC3 12 NA A 702 HOH A 732 HOH A 797 HOH A 819
SITE 1 AC4 5 TRP A 450 PRO A 509 LYS A 510 ILE A 511
SITE 2 AC4 5 HOH A 824
SITE 1 AC5 5 TYR A 72 GLN A 352 VAL A 368 ILE A 373
SITE 2 AC5 5 HOH A 746
CRYST1 45.251 60.679 62.032 88.69 70.00 72.54 P 1 1
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 0.022099 -0.006952 -0.008694 0.00000
SCALE2 0.000000 0.017276 0.001541 0.00000
SCALE3 0.000000 0.000000 0.017223 0.00000
(ATOM LINES ARE NOT SHOWN.)
END