HEADER LYASE 07-APR-06 2GMV
TITLE PEPCK COMPLEX WITH A GTP-COMPETITIVE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOENOLPYRUVATE CARBOXYLASE, 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, XANTHINE, INHIBITOR, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.DUNTEN
REVDAT 5 14-FEB-24 2GMV 1 REMARK SEQADV LINK
REVDAT 4 24-JUL-19 2GMV 1 REMARK
REVDAT 3 24-FEB-09 2GMV 1 VERSN
REVDAT 2 21-AUG-07 2GMV 1 JRNL
REVDAT 1 29-MAY-07 2GMV 0
JRNL AUTH S.L.PIETRANICO,L.H.FOLEY,N.HUBY,W.YUN,P.DUNTEN,J.VERMEULEN,
JRNL AUTH 2 P.WANG,K.TOTH,G.RAMSEY,M.L.GUBLER,S.J.WERTHEIMER
JRNL TITL C-8 MODIFICATIONS OF 3-ALKYL-1,8-DIBENZYLXANTHINES AS
JRNL TITL 2 INHIBITORS OF HUMAN CYTOSOLIC PHOSPHOENOLPYRUVATE
JRNL TITL 3 CARBOXYKINASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 3835 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17532214
JRNL DOI 10.1016/J.BMCL.2007.05.013
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.H.FOLEY,P.WANG,P.DUNTEN,G.RAMSEY,M.L.GUBLER,S.J.WERTHEIMER
REMARK 1 TITL X-RAY STRUCTURES OF TWO XANTHINE INHIBITORS BOUND TO PEPCK
REMARK 1 TITL 2 AND N-3 MODIFICATIONS OF SUBSTITUTED 1,8-DIBENZYLXANTHINES.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 13 3871 2003
REMARK 1 REFN ISSN 0960-894X
REMARK 1 PMID 14552798
REMARK 1 DOI 10.1016/S0960-894X(03)00723-6
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.DUNTEN,C.BELUNIS,R.CROWTHER,K.HOLLFELDER,U.KAMMLOTT,
REMARK 1 AUTH 2 W.LEVIN,M.HANSPETER,G.B.RAMSEY,A.SWAIN,D.WEBER,
REMARK 1 AUTH 3 S.J.WERTHEIMER
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC PHOSPHOENOLPYRUVATE
REMARK 1 TITL 2 CARBOXYKINASE REVEALS A NEW GTP-BINDING SITE.
REMARK 1 REF J.MOL.BIOL. V. 316 257 2002
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 11851336
REMARK 1 DOI 10.1006/JMBI.2001.5364
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.7
REMARK 3 NUMBER OF REFLECTIONS : 44751
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2231
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 2.3500 - 2.3000 0.29 1097 49 0.2640 0.3853
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 SOLVENT RADIUS : 1.40
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.252
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.77500
REMARK 3 B22 (A**2) : -5.20700
REMARK 3 B33 (A**2) : -4.60300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.51200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 11.950 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GMV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 33.06700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE ENZYME IS ACTIVE AS A MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 465 SER A 549
REMARK 465 GLY B -2
REMARK 465 GLU B -1
REMARK 465 LEU B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 PRO B 3
REMARK 465 GLN B 4
REMARK 465 LEU B 5
REMARK 465 GLN B 6
REMARK 465 ASN B 7
REMARK 465 GLY B 8
REMARK 465 LEU B 9
REMARK 465 THR B 465
REMARK 465 ALA B 466
REMARK 465 ALA B 467
REMARK 465 ALA B 468
REMARK 465 GLU B 469
REMARK 465 HIS B 470
REMARK 465 LYS B 471
REMARK 465 GLY B 472
REMARK 465 LYS B 547
REMARK 465 ALA B 548
REMARK 465 SER B 549
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 ARG A 129 -49.28 -135.11
REMARK 500 LYS A 243 -81.02 -78.67
REMARK 500 TRP A 260 -167.25 -123.48
REMARK 500 PRO A 285 -176.25 -68.42
REMARK 500 ASP A 311 -53.92 -142.75
REMARK 500 PHE A 333 64.90 -116.12
REMARK 500 ASN A 344 76.01 -174.84
REMARK 500 ALA A 378 173.01 -58.06
REMARK 500 PHE A 530 -126.17 46.39
REMARK 500 ASN A 601 -121.59 59.23
REMARK 500 ASN B 74 51.20 35.68
REMARK 500 ARG B 129 -54.58 -120.17
REMARK 500 ASN B 208 26.92 48.29
REMARK 500 LYS B 243 -88.23 -68.42
REMARK 500 PHE B 246 -65.95 -92.11
REMARK 500 THR B 271 -162.55 -66.46
REMARK 500 PRO B 285 -163.64 -76.54
REMARK 500 CYS B 288 -7.46 -146.06
REMARK 500 LYS B 290 -57.78 -29.74
REMARK 500 ASP B 311 -48.75 -146.10
REMARK 500 ASN B 354 51.71 35.91
REMARK 500 ALA B 378 170.98 -56.02
REMARK 500 ASP B 395 24.46 -71.95
REMARK 500 ASP B 417 158.63 -44.77
REMARK 500 PHE B 433 -144.24 -90.26
REMARK 500 LEU B 448 -83.09 -50.49
REMARK 500 SER B 449 -139.48 -107.99
REMARK 500 PHE B 480 13.69 59.02
REMARK 500 ASN B 515 121.42 173.96
REMARK 500 PHE B 517 53.92 -108.79
REMARK 500 ASP B 520 -122.07 -119.00
REMARK 500 PHE B 530 -122.73 54.26
REMARK 500 SER B 534 -7.48 -54.13
REMARK 500 ASN B 565 89.27 -49.02
REMARK 500 ASN B 601 -129.11 51.42
REMARK 500 GLU B 607 -8.63 -59.16
REMARK 500 ARG B 618 13.45 -61.71
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 97.9
REMARK 620 3 ASP A 311 OD1 86.7 79.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 701 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 244 NZ
REMARK 620 2 HIS B 264 NE2 92.1
REMARK 620 3 ASP B 311 OD1 86.8 72.7
REMARK 620 N 1 2
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 MN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UN8 A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KHB RELATED DB: PDB
REMARK 900 PEPCK COMPLEX WITH A GTP ANALOG
REMARK 900 RELATED ID: 1NHX RELATED DB: PDB
REMARK 900 PEPCK COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 1M51 RELATED DB: PDB
REMARK 900 PEPCK COMPLEX WITH AN INHIBITOR
DBREF 2GMV A 1 622 UNP P35558 PPCKC_HUMAN 1 622
DBREF 2GMV B 1 622 UNP P35558 PPCKC_HUMAN 1 622
SEQADV 2GMV GLY A -2 UNP P35558 CLONING ARTIFACT
SEQADV 2GMV GLU A -1 UNP P35558 CLONING ARTIFACT
SEQADV 2GMV LEU A 0 UNP P35558 CLONING ARTIFACT
SEQADV 2GMV LEU A 184 UNP P35558 VAL 184 VARIANT
SEQADV 2GMV VAL A 267 UNP P35558 ILE 267 VARIANT
SEQADV 2GMV ASP A 586 UNP P35558 GLU 586 VARIANT
SEQADV 2GMV VAL A 597 UNP P35558 GLU 597 VARIANT
SEQADV 2GMV GLY B -2 UNP P35558 CLONING ARTIFACT
SEQADV 2GMV GLU B -1 UNP P35558 CLONING ARTIFACT
SEQADV 2GMV LEU B 0 UNP P35558 CLONING ARTIFACT
SEQADV 2GMV LEU B 184 UNP P35558 VAL 184 VARIANT
SEQADV 2GMV VAL B 267 UNP P35558 ILE 267 VARIANT
SEQADV 2GMV ASP B 586 UNP P35558 GLU 586 VARIANT
SEQADV 2GMV VAL B 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
SEQRES 1 B 625 GLY GLU LEU MET PRO PRO GLN LEU GLN ASN GLY LEU ASN
SEQRES 2 B 625 LEU SER ALA LYS VAL VAL GLN GLY SER LEU ASP SER LEU
SEQRES 3 B 625 PRO GLN ALA VAL ARG GLU PHE LEU GLU ASN ASN ALA GLU
SEQRES 4 B 625 LEU CYS GLN PRO ASP HIS ILE HIS ILE CYS ASP GLY SER
SEQRES 5 B 625 GLU GLU GLU ASN GLY ARG LEU LEU GLY GLN MET GLU GLU
SEQRES 6 B 625 GLU GLY ILE LEU ARG ARG LEU LYS LYS TYR ASP ASN CYS
SEQRES 7 B 625 TRP LEU ALA LEU THR ASP PRO ARG ASP VAL ALA ARG ILE
SEQRES 8 B 625 GLU SER LYS THR VAL ILE VAL THR GLN GLU GLN ARG ASP
SEQRES 9 B 625 THR VAL PRO ILE PRO LYS THR GLY LEU SER GLN LEU GLY
SEQRES 10 B 625 ARG TRP MET SER GLU GLU ASP PHE GLU LYS ALA PHE ASN
SEQRES 11 B 625 ALA ARG PHE PRO GLY CYS MET LYS GLY ARG THR MET TYR
SEQRES 12 B 625 VAL ILE PRO PHE SER MET GLY PRO LEU GLY SER PRO LEU
SEQRES 13 B 625 SER LYS ILE GLY ILE GLU LEU THR ASP SER PRO TYR VAL
SEQRES 14 B 625 VAL ALA SER MET ARG ILE MET THR ARG MET GLY THR PRO
SEQRES 15 B 625 VAL LEU GLU ALA LEU GLY ASP GLY GLU PHE VAL LYS CYS
SEQRES 16 B 625 LEU HIS SER VAL GLY CYS PRO LEU PRO LEU GLN LYS PRO
SEQRES 17 B 625 LEU VAL ASN ASN TRP PRO CYS ASN PRO GLU LEU THR LEU
SEQRES 18 B 625 ILE ALA HIS LEU PRO ASP ARG ARG GLU ILE ILE SER PHE
SEQRES 19 B 625 GLY SER GLY TYR GLY GLY ASN SER LEU LEU GLY LYS LYS
SEQRES 20 B 625 CYS PHE ALA LEU ARG MET ALA SER ARG LEU ALA LYS GLU
SEQRES 21 B 625 GLU GLY TRP LEU ALA GLU HIS MET LEU VAL LEU GLY ILE
SEQRES 22 B 625 THR ASN PRO GLU GLY GLU LYS LYS TYR LEU ALA ALA ALA
SEQRES 23 B 625 PHE PRO SER ALA CYS GLY LYS THR ASN LEU ALA MET MET
SEQRES 24 B 625 ASN PRO SER LEU PRO GLY TRP LYS VAL GLU CYS VAL GLY
SEQRES 25 B 625 ASP ASP ILE ALA TRP MET LYS PHE ASP ALA GLN GLY HIS
SEQRES 26 B 625 LEU ARG ALA ILE ASN PRO GLU ASN GLY PHE PHE GLY VAL
SEQRES 27 B 625 ALA PRO GLY THR SER VAL LYS THR ASN PRO ASN ALA ILE
SEQRES 28 B 625 LYS THR ILE GLN LYS ASN THR ILE PHE THR ASN VAL ALA
SEQRES 29 B 625 GLU THR SER ASP GLY GLY VAL TYR TRP GLU GLY ILE ASP
SEQRES 30 B 625 GLU PRO LEU ALA SER GLY VAL THR ILE THR SER TRP LYS
SEQRES 31 B 625 ASN LYS GLU TRP SER SER GLU ASP GLY GLU PRO CYS ALA
SEQRES 32 B 625 HIS PRO ASN SER ARG PHE CYS THR PRO ALA SER GLN CYS
SEQRES 33 B 625 PRO ILE ILE ASP ALA ALA TRP GLU SER PRO GLU GLY VAL
SEQRES 34 B 625 PRO ILE GLU GLY ILE ILE PHE GLY GLY ARG ARG PRO ALA
SEQRES 35 B 625 GLY VAL PRO LEU VAL TYR GLU ALA LEU SER TRP GLN HIS
SEQRES 36 B 625 GLY VAL PHE VAL GLY ALA ALA MET ARG SER GLU ALA THR
SEQRES 37 B 625 ALA ALA ALA GLU HIS LYS GLY LYS ILE ILE MET HIS ASP
SEQRES 38 B 625 PRO PHE ALA MET ARG PRO PHE PHE GLY TYR ASN PHE GLY
SEQRES 39 B 625 LYS TYR LEU ALA HIS TRP LEU SER MET ALA GLN HIS PRO
SEQRES 40 B 625 ALA ALA LYS LEU PRO LYS ILE PHE HIS VAL ASN TRP PHE
SEQRES 41 B 625 ARG LYS ASP LYS GLU GLY LYS PHE LEU TRP PRO GLY PHE
SEQRES 42 B 625 GLY GLU ASN SER ARG VAL LEU GLU TRP MET PHE ASN ARG
SEQRES 43 B 625 ILE ASP GLY LYS ALA SER THR LYS LEU THR PRO ILE GLY
SEQRES 44 B 625 TYR ILE PRO LYS GLU ASP ALA LEU ASN LEU LYS GLY LEU
SEQRES 45 B 625 GLY HIS ILE ASN MET MET GLU LEU PHE SER ILE SER LYS
SEQRES 46 B 625 GLU PHE TRP ASP LYS GLU VAL GLU ASP ILE GLU LYS TYR
SEQRES 47 B 625 LEU VAL ASP GLN VAL ASN ALA ASP LEU PRO CYS GLU ILE
SEQRES 48 B 625 GLU ARG GLU ILE LEU ALA LEU LYS GLN ARG ILE SER GLN
SEQRES 49 B 625 MET
HET MN A 701 1
HET PEP A 702 10
HET UN8 A 703 40
HET MN B 701 1
HET PEP B 702 10
HETNAM MN MANGANESE (II) ION
HETNAM PEP PHOSPHOENOLPYRUVATE
HETNAM UN8 N-(4-{[3-BUTYL-1-(2-FLUOROBENZYL)-2,6-DIOXO-2,3,6,7-
HETNAM 2 UN8 TETRAHYDRO-1H-PURIN-8-YL]METHYL}PHENYL)-1-METHYL-1H-
HETNAM 3 UN8 IMIDAZOLE-4-SULFONAMIDE
FORMUL 3 MN 2(MN 2+)
FORMUL 4 PEP 2(C3 H5 O6 P)
FORMUL 5 UN8 C27 H28 F N7 O4 S
FORMUL 8 HOH *132(H2 O)
HELIX 1 1 SER A 19 LEU A 23 5 5
HELIX 2 2 PRO A 24 GLN A 39 1 16
HELIX 3 3 SER A 49 GLU A 63 1 15
HELIX 4 4 ILE A 88 SER A 90 5 3
HELIX 5 5 GLU A 98 THR A 102 5 5
HELIX 6 6 SER A 118 ALA A 128 1 11
HELIX 7 7 SER A 163 THR A 174 1 12
HELIX 8 8 GLY A 177 GLY A 185 1 9
HELIX 9 9 ASN A 213 THR A 217 5 5
HELIX 10 10 TYR A 235 LEU A 240 1 6
HELIX 11 11 LEU A 248 GLY A 259 1 12
HELIX 12 12 GLY A 289 MET A 295 1 7
HELIX 13 13 ASN A 344 ILE A 351 1 8
HELIX 14 14 SER A 411 CYS A 413 5 3
HELIX 15 15 SER A 449 ALA A 459 1 11
HELIX 16 16 PRO A 479 MET A 482 5 4
HELIX 17 17 ASN A 489 MET A 500 1 12
HELIX 18 18 ALA A 501 HIS A 503 5 3
HELIX 19 19 GLY A 529 GLU A 532 5 4
HELIX 20 20 ASN A 533 ASP A 545 1 13
HELIX 21 21 ASN A 573 PHE A 578 1 6
HELIX 22 22 SER A 581 VAL A 600 1 20
HELIX 23 23 ASN A 601 LEU A 604 5 4
HELIX 24 24 PRO A 605 GLN A 621 1 17
HELIX 25 25 ASN B 10 ALA B 13 5 4
HELIX 26 26 SER B 19 LEU B 23 5 5
HELIX 27 27 PRO B 24 GLN B 39 1 16
HELIX 28 28 SER B 49 GLU B 62 1 14
HELIX 29 29 ILE B 88 SER B 90 5 3
HELIX 30 30 GLU B 98 VAL B 103 1 6
HELIX 31 31 SER B 118 ALA B 128 1 11
HELIX 32 32 SER B 163 THR B 174 1 12
HELIX 33 33 GLY B 177 GLY B 185 1 9
HELIX 34 34 PRO B 223 ARG B 225 5 3
HELIX 35 35 TYR B 235 LEU B 240 1 6
HELIX 36 36 LEU B 248 GLY B 259 1 12
HELIX 37 37 GLY B 289 MET B 295 1 7
HELIX 38 38 ASN B 344 ILE B 351 1 8
HELIX 39 39 SER B 392 GLY B 396 5 5
HELIX 40 40 SER B 411 CYS B 413 5 3
HELIX 41 41 SER B 449 ALA B 458 1 10
HELIX 42 42 PRO B 479 MET B 482 5 4
HELIX 43 43 ASN B 489 MET B 500 1 12
HELIX 44 44 ALA B 501 HIS B 503 5 3
HELIX 45 45 GLY B 529 SER B 534 5 6
HELIX 46 46 ARG B 535 GLY B 546 1 12
HELIX 47 47 ASN B 573 PHE B 578 1 6
HELIX 48 48 GLU B 583 VAL B 600 1 18
HELIX 49 49 ASN B 601 LEU B 604 5 4
HELIX 50 50 PRO B 605 GLN B 621 1 17
SHEET 1 A 8 VAL A 15 GLN A 17 0
SHEET 2 A 8 HIS A 42 ILE A 45 1 O ILE A 43 N VAL A 16
SHEET 3 A 8 THR A 138 MET A 146 1 O MET A 139 N HIS A 42
SHEET 4 A 8 LYS A 155 THR A 161 -1 O LYS A 155 N MET A 146
SHEET 5 A 8 VAL A 190 SER A 195 1 O CYS A 192 N LEU A 160
SHEET 6 A 8 GLU A 227 PHE A 231 1 O SER A 230 N LEU A 193
SHEET 7 A 8 LEU A 218 LEU A 222 -1 N LEU A 218 O PHE A 231
SHEET 8 A 8 THR A 92 ILE A 94 1 N VAL A 93 O ILE A 219
SHEET 1 B 4 VAL A 15 GLN A 17 0
SHEET 2 B 4 HIS A 42 ILE A 45 1 O ILE A 43 N VAL A 16
SHEET 3 B 4 THR A 138 MET A 146 1 O MET A 139 N HIS A 42
SHEET 4 B 4 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 CYS A 407 N ILE A 356
SHEET 5 C 5 GLY A 331 VAL A 335 -1 N PHE A 332 O THR A 408
SHEET 1 D 7 LEU A 261 GLU A 263 0
SHEET 2 D 7 ALA A 313 PHE A 317 -1 O MET A 315 N LEU A 261
SHEET 3 D 7 LEU A 323 ILE A 326 -1 O ILE A 326 N TRP A 314
SHEET 4 D 7 VAL A 426 GLY A 434 -1 O ILE A 428 N LEU A 323
SHEET 5 D 7 LYS A 277 ALA A 283 1 N ALA A 281 O ILE A 432
SHEET 6 D 7 LEU A 266 THR A 271 -1 N ILE A 270 O LYS A 278
SHEET 7 D 7 LYS A 304 GLY A 309 -1 O GLU A 306 N GLY A 269
SHEET 1 E 6 LEU A 261 GLU A 263 0
SHEET 2 E 6 ALA A 313 PHE A 317 -1 O MET A 315 N LEU A 261
SHEET 3 E 6 LEU A 323 ILE A 326 -1 O ILE A 326 N TRP A 314
SHEET 4 E 6 VAL A 426 GLY A 434 -1 O ILE A 428 N LEU A 323
SHEET 5 E 6 LYS A 510 VAL A 514 1 O LYS A 510 N ILE A 431
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 LYS A 551 THR A 553 0
SHEET 2 H 2 GLY A 556 ILE A 558 -1 O ILE A 558 N LYS A 551
SHEET 1 I 8 VAL B 15 GLN B 17 0
SHEET 2 I 8 HIS B 42 ILE B 45 1 O ILE B 43 N VAL B 16
SHEET 3 I 8 THR B 138 MET B 146 1 O MET B 139 N HIS B 42
SHEET 4 I 8 LYS B 155 THR B 161 -1 O GLU B 159 N ILE B 142
SHEET 5 I 8 VAL B 190 SER B 195 1 O CYS B 192 N LEU B 160
SHEET 6 I 8 GLU B 227 PHE B 231 1 O ILE B 228 N LEU B 193
SHEET 7 I 8 LEU B 218 LEU B 222 -1 N ALA B 220 O ILE B 229
SHEET 8 I 8 THR B 92 ILE B 94 1 N VAL B 93 O ILE B 219
SHEET 1 J 4 VAL B 15 GLN B 17 0
SHEET 2 J 4 HIS B 42 ILE B 45 1 O ILE B 43 N VAL B 16
SHEET 3 J 4 THR B 138 MET B 146 1 O MET B 139 N HIS B 42
SHEET 4 J 4 ARG B 175 MET B 176 -1 O ARG B 175 N SER B 145
SHEET 1 K 5 LEU B 66 LEU B 69 0
SHEET 2 K 5 CYS B 75 ALA B 78 -1 O LEU B 77 N ARG B 67
SHEET 3 K 5 ILE B 356 THR B 358 1 O PHE B 357 N TRP B 76
SHEET 4 K 5 ARG B 405 PRO B 409 -1 O ARG B 405 N THR B 358
SHEET 5 K 5 GLY B 331 VAL B 335 -1 N PHE B 332 O THR B 408
SHEET 1 L 4 LEU B 261 GLU B 263 0
SHEET 2 L 4 ALA B 313 PHE B 317 -1 O MET B 315 N LEU B 261
SHEET 3 L 4 LEU B 323 ILE B 326 -1 O ARG B 324 N LYS B 316
SHEET 4 L 4 VAL B 426 PRO B 427 -1 O VAL B 426 N ALA B 325
SHEET 1 M 6 VAL B 305 GLY B 309 0
SHEET 2 M 6 LEU B 266 ILE B 270 -1 N VAL B 267 O VAL B 308
SHEET 3 M 6 TYR B 279 ALA B 282 -1 O ALA B 282 N LEU B 266
SHEET 4 M 6 ILE B 431 ILE B 432 1 O ILE B 432 N ALA B 281
SHEET 5 M 6 ILE B 511 VAL B 514 1 O PHE B 512 N ILE B 431
SHEET 6 M 6 VAL B 444 GLU B 446 -1 N TYR B 445 O HIS B 513
SHEET 1 N 4 VAL B 368 TYR B 369 0
SHEET 2 N 4 ALA B 361 THR B 363 -1 N ALA B 361 O TYR B 369
SHEET 3 N 4 ILE B 383 THR B 384 -1 O THR B 384 N GLU B 362
SHEET 4 N 4 GLU B 390 TRP B 391 -1 O TRP B 391 N ILE B 383
SHEET 1 O 2 ARG B 461 GLU B 463 0
SHEET 2 O 2 ILE B 475 HIS B 477 -1 O MET B 476 N SER B 462
LINK NZ LYS A 244 MN MN A 701 1555 1555 2.36
LINK NE2 HIS A 264 MN MN A 701 1555 1555 2.37
LINK OD1 ASP A 311 MN MN A 701 1555 1555 2.30
LINK NZ LYS B 244 MN MN B 701 1555 1555 2.37
LINK NE2 HIS B 264 MN MN B 701 1555 1555 2.57
LINK OD1 ASP B 311 MN MN B 701 1555 1555 2.34
CISPEP 1 LEU A 200 PRO A 201 0 -2.90
CISPEP 2 LEU B 200 PRO B 201 0 5.60
SITE 1 AC1 3 LYS A 244 HIS A 264 ASP A 311
SITE 1 AC2 3 LYS B 244 HIS B 264 ASP B 311
SITE 1 AC3 9 ALA A 86 ARG A 87 TYR A 235 GLY A 236
SITE 2 AC3 9 GLY A 237 LYS A 244 ASN A 403 ARG A 405
SITE 3 AC3 9 HOH A 776
SITE 1 AC4 10 ALA B 86 ARG B 87 TYR B 235 GLY B 236
SITE 2 AC4 10 GLY B 237 LYS B 244 ASN B 403 ARG B 405
SITE 3 AC4 10 PHE B 485 HOH B 715
SITE 1 AC5 13 ALA A 287 CYS A 288 GLY A 289 ASN A 292
SITE 2 AC5 13 LEU A 293 THR A 343 TRP A 516 PHE A 517
SITE 3 AC5 13 PHE A 525 TRP A 527 PHE A 530 ASN A 533
SITE 4 AC5 13 HOH A 740
CRYST1 128.011 66.134 137.360 90.00 145.09 90.00 P 1 21 1 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 0.007812 0.000000 0.011194 0.00000
SCALE2 0.000000 0.015121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
