HEADER LYASE 21-DEC-15 5FH0
TITLE THE STRUCTURE OF RAT CYTOSOLIC PEPCK VARIANT E89A COMPLEX WITH GTP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP];
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PEPCK-C;
COMPND 5 EC: 4.1.1.32;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PCK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, GLUCONEOGENESIS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.JOHNSON,T.HOLYOAK
REVDAT 4 27-SEP-23 5FH0 1 LINK
REVDAT 3 04-DEC-19 5FH0 1 REMARK
REVDAT 2 20-SEP-17 5FH0 1 JRNL REMARK
REVDAT 1 09-NOV-16 5FH0 0
JRNL AUTH T.A.JOHNSON,M.J.MCLEOD,T.HOLYOAK
JRNL TITL UTILIZATION OF SUBSTRATE INTRINSIC BINDING ENERGY FOR
JRNL TITL 2 CONFORMATIONAL CHANGE AND CATALYTIC FUNCTION IN
JRNL TITL 3 PHOSPHOENOLPYRUVATE CARBOXYKINASE.
JRNL REF BIOCHEMISTRY V. 55 575 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 26709450
JRNL DOI 10.1021/ACS.BIOCHEM.5B01215
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 77001
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4053
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4860
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 393
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.171
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5FH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81130
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 0.34400
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: 3DT2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M HEPES PH 7.4, 8MM
REMARK 280 MNCL2, 10MM GTP, 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 30.21400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.20750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.85500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.20750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.21400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.85500
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 TOTAL BURIED SURFACE AREA: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 466
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 OG SER A 286 O HOH A 802 1.92
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 HIS A 6 -147.88 -132.72
REMARK 500 ASP A 84 55.95 -118.06
REMARK 500 ARG A 129 -59.38 -123.08
REMARK 500 LYS A 244 -40.07 -133.39
REMARK 500 SER A 286 140.46 -38.53
REMARK 500 ASP A 311 -43.89 -149.23
REMARK 500 PHE A 333 77.71 -107.04
REMARK 500 ASN A 344 69.39 -165.58
REMARK 500 PHE A 530 -123.94 59.26
REMARK 500 ASN A 573 81.38 -69.92
REMARK 500 ASN A 601 -108.07 42.92
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 704 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 63 OE2
REMARK 620 2 HIS A 502 NE2 14.3
REMARK 620 3 GLU A 607 OE1 12.2 4.5
REMARK 620 4 GLU A 607 OE2 10.6 4.5 2.0
REMARK 620 5 HOH A 807 O 155.5 148.1 146.9 148.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 706 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 79 O
REMARK 620 2 ASN A 208 O 108.4
REMARK 620 3 HOH A 887 O 91.6 158.7
REMARK 620 4 HOH A1032 O 94.6 88.0 83.0
REMARK 620 5 HOH A1118 O 105.0 85.2 96.9 160.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 702 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 244 NZ
REMARK 620 2 HIS A 264 NE2 83.5
REMARK 620 3 ASP A 311 OD1 100.3 92.7
REMARK 620 4 GTP A 703 O1G 176.0 95.1 83.5
REMARK 620 5 HOH A 997 O 92.0 96.3 165.6 84.4
REMARK 620 6 HOH A1096 O 89.9 172.9 86.0 91.8 86.5
REMARK 620 N 1 2 3 4 5
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 THR A 291 OG1
REMARK 620 2 GTP A 703 O2G 176.3
REMARK 620 3 GTP A 703 O2B 88.5 94.0
REMARK 620 4 HOH A 826 O 84.0 93.5 86.6
REMARK 620 5 HOH A 830 O 84.7 92.8 173.0 94.6
REMARK 620 6 HOH A 939 O 98.2 84.5 90.0 176.0 89.0
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 706
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FH1 RELATED DB: PDB
REMARK 900 RELATED ID: 5FH2 RELATED DB: PDB
REMARK 900 RELATED ID: 5FH3 RELATED DB: PDB
REMARK 900 RELATED ID: 5FH4 RELATED DB: PDB
REMARK 900 RELATED ID: 5FH5 RELATED DB: PDB
DBREF 5FH0 A 1 622 UNP P07379 PCKGC_RAT 1 622
SEQADV 5FH0 ALA A 89 UNP P07379 GLU 89 ENGINEERED MUTATION
SEQRES 1 A 622 MET PRO PRO GLN LEU HIS ASN GLY LEU ASP PHE SER ALA
SEQRES 2 A 622 LYS VAL ILE GLN GLY SER LEU ASP SER LEU PRO GLN GLU
SEQRES 3 A 622 VAL ARG LYS PHE VAL GLU GLY ASN ALA GLN LEU CYS GLN
SEQRES 4 A 622 PRO GLU TYR ILE HIS ILE CYS ASP GLY SER GLU GLU GLU
SEQRES 5 A 622 TYR GLY ARG LEU LEU ALA HIS MET GLN GLU GLU GLY VAL
SEQRES 6 A 622 ILE ARG LYS LEU LYS LYS TYR ASP ASN CYS TRP LEU ALA
SEQRES 7 A 622 LEU THR ASP PRO ARG ASP VAL ALA ARG ILE ALA SER LYS
SEQRES 8 A 622 THR VAL ILE ILE THR GLN GLU GLN ARG ASP THR VAL PRO
SEQRES 9 A 622 ILE PRO LYS SER GLY GLN SER GLN LEU GLY ARG TRP MET
SEQRES 10 A 622 SER GLU GLU ASP PHE GLU LYS ALA PHE ASN ALA ARG PHE
SEQRES 11 A 622 PRO GLY CYS MET LYS GLY ARG THR MET TYR VAL ILE PRO
SEQRES 12 A 622 PHE SER MET GLY PRO LEU GLY SER PRO LEU ALA LYS ILE
SEQRES 13 A 622 GLY ILE GLU LEU THR ASP SER PRO TYR VAL VAL ALA SER
SEQRES 14 A 622 MET ARG ILE MET THR ARG MET GLY THR SER VAL LEU GLU
SEQRES 15 A 622 ALA LEU GLY ASP GLY GLU PHE ILE LYS CYS LEU HIS SER
SEQRES 16 A 622 VAL GLY CYS PRO LEU PRO LEU LYS LYS PRO LEU VAL ASN
SEQRES 17 A 622 ASN TRP ALA CYS ASN PRO GLU LEU THR LEU ILE ALA HIS
SEQRES 18 A 622 LEU PRO ASP ARG ARG GLU ILE ILE SER PHE GLY SER GLY
SEQRES 19 A 622 TYR GLY GLY ASN SER LEU LEU GLY LYS LYS CYS PHE ALA
SEQRES 20 A 622 LEU ARG ILE ALA SER ARG LEU ALA LYS GLU GLU GLY TRP
SEQRES 21 A 622 LEU ALA GLU HIS MET LEU ILE LEU GLY ILE THR ASN PRO
SEQRES 22 A 622 GLU GLY LYS LYS LYS TYR LEU ALA ALA ALA PHE PRO SER
SEQRES 23 A 622 ALA CYS GLY LYS THR ASN LEU ALA MET MET ASN PRO THR
SEQRES 24 A 622 LEU PRO GLY TRP LYS VAL GLU CYS VAL GLY ASP ASP ILE
SEQRES 25 A 622 ALA TRP MET LYS PHE ASP ALA GLN GLY ASN LEU ARG ALA
SEQRES 26 A 622 ILE ASN PRO GLU ASN GLY PHE PHE GLY VAL ALA PRO GLY
SEQRES 27 A 622 THR SER VAL LYS THR ASN PRO ASN ALA ILE LYS THR ILE
SEQRES 28 A 622 GLN LYS ASN THR ILE PHE THR ASN VAL ALA GLU THR SER
SEQRES 29 A 622 ASP GLY GLY VAL TYR TRP GLU GLY ILE ASP GLU PRO LEU
SEQRES 30 A 622 ALA PRO GLY VAL THR ILE THR SER TRP LYS ASN LYS GLU
SEQRES 31 A 622 TRP ARG PRO GLN ASP GLU GLU PRO CYS ALA HIS PRO ASN
SEQRES 32 A 622 SER ARG PHE CYS THR PRO ALA SER GLN CYS PRO ILE ILE
SEQRES 33 A 622 ASP PRO ALA TRP GLU SER PRO GLU GLY VAL PRO ILE GLU
SEQRES 34 A 622 GLY ILE ILE PHE GLY GLY ARG ARG PRO ALA GLY VAL PRO
SEQRES 35 A 622 LEU VAL TYR GLU ALA LEU SER TRP GLN HIS GLY VAL PHE
SEQRES 36 A 622 VAL GLY ALA ALA MET ARG SER GLU ALA THR ALA ALA ALA
SEQRES 37 A 622 GLU HIS LYS GLY LYS VAL ILE MET HIS ASP PRO PHE ALA
SEQRES 38 A 622 MET ARG PRO PHE PHE GLY TYR ASN PHE GLY LYS TYR LEU
SEQRES 39 A 622 ALA HIS TRP LEU SER MET ALA HIS ARG PRO ALA ALA LYS
SEQRES 40 A 622 LEU PRO LYS ILE PHE HIS VAL ASN TRP PHE ARG LYS ASP
SEQRES 41 A 622 LYS ASN GLY LYS PHE LEU TRP PRO GLY PHE GLY GLU ASN
SEQRES 42 A 622 SER ARG VAL LEU GLU TRP MET PHE GLY ARG ILE GLU GLY
SEQRES 43 A 622 GLU ASP SER ALA LYS LEU THR PRO ILE GLY TYR VAL PRO
SEQRES 44 A 622 LYS GLU ASP ALA LEU ASN LEU LYS GLY LEU GLY ASP VAL
SEQRES 45 A 622 ASN VAL GLU GLU LEU PHE GLY ILE SER LYS GLU PHE TRP
SEQRES 46 A 622 GLU LYS GLU VAL GLU GLU ILE ASP LYS TYR LEU GLU ASP
SEQRES 47 A 622 GLN VAL ASN ALA ASP LEU PRO TYR GLU ILE GLU ARG GLU
SEQRES 48 A 622 LEU ARG ALA LEU LYS GLN ARG ILE SER GLN MET
HET MN A 701 1
HET MN A 702 1
HET GTP A 703 32
HET MN A 704 1
HET EPE A 705 15
HET NA A 706 1
HETNAM MN MANGANESE (II) ION
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM NA SODIUM ION
HETSYN EPE HEPES
FORMUL 2 MN 3(MN 2+)
FORMUL 4 GTP C10 H16 N5 O14 P3
FORMUL 6 EPE C8 H18 N2 O4 S
FORMUL 7 NA NA 1+
FORMUL 8 HOH *393(H2 O)
HELIX 1 AA1 PHE A 11 ALA A 13 5 3
HELIX 2 AA2 SER A 19 LEU A 23 5 5
HELIX 3 AA3 PRO A 24 GLN A 39 1 16
HELIX 4 AA4 SER A 49 GLU A 63 1 15
HELIX 5 AA5 ASP A 81 VAL A 85 5 5
HELIX 6 AA6 ILE A 88 SER A 90 5 3
HELIX 7 AA7 GLU A 98 VAL A 103 1 6
HELIX 8 AA8 SER A 118 ALA A 128 1 11
HELIX 9 AA9 SER A 163 THR A 174 1 12
HELIX 10 AB1 GLY A 177 GLY A 185 1 9
HELIX 11 AB2 ASN A 213 THR A 217 5 5
HELIX 12 AB3 PRO A 223 ARG A 225 5 3
HELIX 13 AB4 TYR A 235 SER A 239 5 5
HELIX 14 AB5 LEU A 248 GLY A 259 1 12
HELIX 15 AB6 GLY A 289 MET A 295 1 7
HELIX 16 AB7 ASN A 344 ILE A 351 1 8
HELIX 17 AB8 SER A 411 CYS A 413 5 3
HELIX 18 AB9 SER A 449 ALA A 459 1 11
HELIX 19 AC1 PRO A 479 MET A 482 5 4
HELIX 20 AC2 ASN A 489 MET A 500 1 12
HELIX 21 AC3 ALA A 501 ARG A 503 5 3
HELIX 22 AC4 GLY A 529 GLU A 532 5 4
HELIX 23 AC5 ASN A 533 GLU A 545 1 13
HELIX 24 AC6 ASN A 573 GLY A 579 1 7
HELIX 25 AC7 SER A 581 VAL A 600 1 20
HELIX 26 AC8 ASN A 601 LEU A 604 5 4
HELIX 27 AC9 PRO A 605 GLN A 621 1 17
SHEET 1 AA1 9 VAL A 15 GLN A 17 0
SHEET 2 AA1 9 TYR A 42 ILE A 45 1 O ILE A 43 N ILE A 16
SHEET 3 AA1 9 THR A 138 MET A 146 1 O MET A 139 N TYR A 42
SHEET 4 AA1 9 LYS A 155 THR A 161 -1 O LYS A 155 N MET A 146
SHEET 5 AA1 9 ILE A 190 SER A 195 1 O CYS A 192 N ILE A 158
SHEET 6 AA1 9 GLU A 227 PHE A 231 1 O ILE A 228 N LEU A 193
SHEET 7 AA1 9 LEU A 218 LEU A 222 -1 N LEU A 222 O GLU A 227
SHEET 8 AA1 9 THR A 92 ILE A 95 1 N ILE A 95 O HIS A 221
SHEET 9 AA1 9 TRP A 116 MET A 117 1 O MET A 117 N ILE A 94
SHEET 1 AA2 4 VAL A 15 GLN A 17 0
SHEET 2 AA2 4 TYR A 42 ILE A 45 1 O ILE A 43 N ILE A 16
SHEET 3 AA2 4 THR A 138 MET A 146 1 O MET A 139 N TYR A 42
SHEET 4 AA2 4 ARG A 175 MET A 176 -1 O ARG A 175 N SER A 145
SHEET 1 AA3 5 ARG A 67 LYS A 68 0
SHEET 2 AA3 5 TRP A 76 ALA A 78 -1 O LEU A 77 N ARG A 67
SHEET 3 AA3 5 ILE A 356 THR A 358 1 O PHE A 357 N TRP A 76
SHEET 4 AA3 5 ARG A 405 PRO A 409 -1 O ARG A 405 N THR A 358
SHEET 5 AA3 5 GLY A 331 VAL A 335 -1 N PHE A 332 O THR A 408
SHEET 1 AA4 7 LEU A 261 GLU A 263 0
SHEET 2 AA4 7 ALA A 313 PHE A 317 -1 O MET A 315 N LEU A 261
SHEET 3 AA4 7 LEU A 323 ILE A 326 -1 O ARG A 324 N LYS A 316
SHEET 4 AA4 7 VAL A 426 GLY A 434 -1 O ILE A 428 N LEU A 323
SHEET 5 AA4 7 LYS A 277 ALA A 283 1 N TYR A 279 O GLU A 429
SHEET 6 AA4 7 LEU A 266 THR A 271 -1 N ILE A 270 O LYS A 278
SHEET 7 AA4 7 LYS A 304 GLY A 309 -1 O GLU A 306 N GLY A 269
SHEET 1 AA5 6 LEU A 261 GLU A 263 0
SHEET 2 AA5 6 ALA A 313 PHE A 317 -1 O MET A 315 N LEU A 261
SHEET 3 AA5 6 LEU A 323 ILE A 326 -1 O ARG A 324 N LYS A 316
SHEET 4 AA5 6 VAL A 426 GLY A 434 -1 O ILE A 428 N LEU A 323
SHEET 5 AA5 6 LYS A 510 VAL A 514 1 O VAL A 514 N PHE A 433
SHEET 6 AA5 6 VAL A 444 GLU A 446 -1 N TYR A 445 O HIS A 513
SHEET 1 AA6 4 VAL A 368 TYR A 369 0
SHEET 2 AA6 4 ALA A 361 THR A 363 -1 N ALA A 361 O TYR A 369
SHEET 3 AA6 4 ILE A 383 THR A 384 -1 O THR A 384 N GLU A 362
SHEET 4 AA6 4 GLU A 390 TRP A 391 -1 O TRP A 391 N ILE A 383
SHEET 1 AA7 2 ARG A 461 ALA A 464 0
SHEET 2 AA7 2 VAL A 474 HIS A 477 -1 O VAL A 474 N ALA A 464
SHEET 1 AA8 2 ALA A 550 THR A 553 0
SHEET 2 AA8 2 GLY A 556 PRO A 559 -1 O VAL A 558 N LYS A 551
LINK OE2 GLU A 63 MN MN A 704 1555 1555 2.35
LINK O LEU A 79 NA NA A 706 1555 1555 2.28
LINK O ASN A 208 NA NA A 706 1555 1555 2.26
LINK NZ LYS A 244 MN MN A 702 1555 1555 2.30
LINK NE2 HIS A 264 MN MN A 702 1555 1555 2.32
LINK OG1 THR A 291 MN MN A 701 1555 1555 2.15
LINK OD1 ASP A 311 MN MN A 702 1555 1555 2.23
LINK NE2 HIS A 502 MN MN A 704 1555 2454 2.68
LINK OE1BGLU A 607 MN MN A 704 1555 2454 2.66
LINK OE2BGLU A 607 MN MN A 704 1555 2454 2.32
LINK MN MN A 701 O2G GTP A 703 1555 1555 2.15
LINK MN MN A 701 O2B GTP A 703 1555 1555 2.12
LINK MN MN A 701 O HOH A 826 1555 1555 2.33
LINK MN MN A 701 O HOH A 830 1555 1555 2.11
LINK MN MN A 701 O HOH A 939 1555 1555 2.17
LINK MN MN A 702 O1G GTP A 703 1555 1555 2.16
LINK MN MN A 702 O HOH A 997 1555 1555 2.22
LINK MN MN A 702 O HOH A1096 1555 1555 2.19
LINK MN MN A 704 O HOH A 807 1555 2455 2.49
LINK NA NA A 706 O HOH A 887 1555 1555 2.38
LINK NA NA A 706 O HOH A1032 1555 1555 2.25
LINK NA NA A 706 O HOH A1118 1555 1555 2.39
CISPEP 1 LEU A 200 PRO A 201 0 0.07
SITE 1 AC1 5 THR A 291 GTP A 703 HOH A 826 HOH A 830
SITE 2 AC1 5 HOH A 939
SITE 1 AC2 6 LYS A 244 HIS A 264 ASP A 311 GTP A 703
SITE 2 AC2 6 HOH A 997 HOH A1096
SITE 1 AC3 33 HIS A 264 PRO A 285 SER A 286 ALA A 287
SITE 2 AC3 33 CYS A 288 GLY A 289 LYS A 290 THR A 291
SITE 3 AC3 33 ASN A 292 ASP A 311 VAL A 335 ARG A 405
SITE 4 AC3 33 ARG A 436 TRP A 516 PHE A 517 PHE A 525
SITE 5 AC3 33 GLY A 529 PHE A 530 ASN A 533 MN A 701
SITE 6 AC3 33 MN A 702 HOH A 802 HOH A 824 HOH A 826
SITE 7 AC3 33 HOH A 830 HOH A 881 HOH A 888 HOH A 903
SITE 8 AC3 33 HOH A 931 HOH A 939 HOH A 964 HOH A 997
SITE 9 AC3 33 HOH A1036
SITE 1 AC4 4 GLU A 63 HIS A 502 GLU A 607 HOH A 807
SITE 1 AC5 11 ARG A 87 TYR A 235 GLY A 236 GLY A 237
SITE 2 AC5 11 SER A 286 PHE A 333 ASN A 403 ARG A 405
SITE 3 AC5 11 GLU A 469 HOH A 812 HOH A 876
SITE 1 AC6 5 LEU A 79 ASN A 208 HOH A 887 HOH A1032
SITE 2 AC6 5 HOH A1118
CRYST1 60.428 85.710 118.415 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 0.016549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011667 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
