HEADER INTRAMOLECULAR OXIDOREDUCTASE 23-APR-91 7TIM
TITLE STRUCTURE OF THE TRIOSEPHOSPHATE ISOMERASE-
TITLE 2 PHOSPHOGLYCOLOHYDROXAMATE COMPLEX: AN ANALOGUE OF THE
TITLE 3 INTERMEDIATE ON THE REACTION PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.3.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS INTRAMOLECULAR OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.C.DAVENPORT,P.A.BASH,B.A.SEATON,M.KARPLUS,G.A.PETSKO,
AUTHOR 2 D.RINGE
REVDAT 2 24-FEB-09 7TIM 1 VERSN
REVDAT 1 31-OCT-93 7TIM 0
JRNL AUTH R.C.DAVENPORT,P.A.BASH,B.A.SEATON,M.KARPLUS,
JRNL AUTH 2 G.A.PETSKO,D.RINGE
JRNL TITL STRUCTURE OF THE TRIOSEPHOSPHATE
JRNL TITL 2 ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX: AN
JRNL TITL 3 ANALOGUE OF THE INTERMEDIATE ON THE REACTION
JRNL TITL 4 PATHWAY.
JRNL REF BIOCHEMISTRY V. 30 5821 1991
JRNL REFN ISSN 0006-2960
JRNL PMID 2043623
JRNL DOI 10.1021/BI00238A002
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ, X-PLOR
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3766
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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: NULL
REMARK 4
REMARK 4 7TIM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
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 41.75000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 OE2 GLU A 77 O HOH A 820 2.04
REMARK 500 O HOH A 710 O HOH A 711 2.06
REMARK 500 OG SER A 96 O HOH A 666 2.09
REMARK 500 OD1 ASP A 81 NE2 GLN A 119 2.09
REMARK 500 NH1 ARG A 145 O HOH A 797 2.13
REMARK 500 OE1 GLN B 82 O HOH B 727 2.13
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 O HOH A 672 O HOH A 701 1554 1.88
REMARK 500 O HOH B 747 O HOH B 795 1556 2.05
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 22 CD GLU A 22 OE1 0.066
REMARK 500 GLU A 25 CD GLU A 25 OE1 0.074
REMARK 500 GLU A 34 CD GLU A 34 OE2 0.070
REMARK 500 GLU A 129 CD GLU A 129 OE2 0.075
REMARK 500 GLU A 132 CD GLU A 132 OE2 0.077
REMARK 500 GLU A 133 CD GLU A 133 OE2 0.072
REMARK 500 GLU A 144 CD GLU A 144 OE2 0.069
REMARK 500 GLU A 152 CD GLU A 152 OE1 0.082
REMARK 500 GLU A 153 CD GLU A 153 OE1 0.070
REMARK 500 GLU A 203 CD GLU A 203 OE1 0.069
REMARK 500 GLU B 22 CD GLU B 22 OE2 0.069
REMARK 500 GLU B 25 CD GLU B 25 OE2 0.071
REMARK 500 GLU B 34 CD GLU B 34 OE1 0.070
REMARK 500 GLU B 37 CD GLU B 37 OE1 0.067
REMARK 500 GLU B 97 CD GLU B 97 OE2 0.073
REMARK 500 GLU B 104 CD GLU B 104 OE1 0.066
REMARK 500 GLU B 132 CD GLU B 132 OE2 0.066
REMARK 500 GLU B 133 CD GLU B 133 OE1 0.069
REMARK 500 GLU B 152 CD GLU B 152 OE1 0.069
REMARK 500 GLU B 179 CD GLU B 179 OE1 0.066
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 3 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU A 22 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 ASP A 48 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ALA A 163 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 ASP B 105 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 141 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG B 145 CD - NE - CZ ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 205 NE - CZ - NH2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 242 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 242 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG B 247 NE - CZ - NH1 ANGL. DEV. = -5.7 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 12 -147.81 67.83
REMARK 500 ASN A 35 49.65 -94.47
REMARK 500 ASN A 65 156.20 178.01
REMARK 500 LYS B 12 -151.55 61.08
REMARK 500 ARG B 145 -72.58 -51.94
REMARK 500 LYS B 155 -37.00 -130.62
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 796 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH A 749 DISTANCE = 5.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGH A 249
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGH B 249
DBREF 7TIM A 2 248 UNP P00942 TPIS_YEAST 1 247
DBREF 7TIM B 2 248 UNP P00942 TPIS_YEAST 1 247
SEQRES 1 A 247 ALA ARG THR PHE PHE VAL GLY GLY ASN PHE LYS LEU ASN
SEQRES 2 A 247 GLY SER LYS GLN SER ILE LYS GLU ILE VAL GLU ARG LEU
SEQRES 3 A 247 ASN THR ALA SER ILE PRO GLU ASN VAL GLU VAL VAL ILE
SEQRES 4 A 247 CYS PRO PRO ALA THR TYR LEU ASP TYR SER VAL SER LEU
SEQRES 5 A 247 VAL LYS LYS PRO GLN VAL THR VAL GLY ALA GLN ASN ALA
SEQRES 6 A 247 TYR LEU LYS ALA SER GLY ALA PHE THR GLY GLU ASN SER
SEQRES 7 A 247 VAL ASP GLN ILE LYS ASP VAL GLY ALA LYS TRP VAL ILE
SEQRES 8 A 247 LEU GLY HIS SER GLU ARG ARG SER TYR PHE HIS GLU ASP
SEQRES 9 A 247 ASP LYS PHE ILE ALA ASP LYS THR LYS PHE ALA LEU GLY
SEQRES 10 A 247 GLN GLY VAL GLY VAL ILE LEU CYS ILE GLY GLU THR LEU
SEQRES 11 A 247 GLU GLU LYS LYS ALA GLY LYS THR LEU ASP VAL VAL GLU
SEQRES 12 A 247 ARG GLN LEU ASN ALA VAL LEU GLU GLU VAL LYS ASP TRP
SEQRES 13 A 247 THR ASN VAL VAL VAL ALA TYR GLU PRO VAL TRP ALA ILE
SEQRES 14 A 247 GLY THR GLY LEU ALA ALA THR PRO GLU ASP ALA GLN ASP
SEQRES 15 A 247 ILE HIS ALA SER ILE ARG LYS PHE LEU ALA SER LYS LEU
SEQRES 16 A 247 GLY ASP LYS ALA ALA SER GLU LEU ARG ILE LEU TYR GLY
SEQRES 17 A 247 GLY SER ALA ASN GLY SER ASN ALA VAL THR PHE LYS ASP
SEQRES 18 A 247 LYS ALA ASP VAL ASP GLY PHE LEU VAL GLY GLY ALA SER
SEQRES 19 A 247 LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN SER ARG ASN
SEQRES 1 B 247 ALA ARG THR PHE PHE VAL GLY GLY ASN PHE LYS LEU ASN
SEQRES 2 B 247 GLY SER LYS GLN SER ILE LYS GLU ILE VAL GLU ARG LEU
SEQRES 3 B 247 ASN THR ALA SER ILE PRO GLU ASN VAL GLU VAL VAL ILE
SEQRES 4 B 247 CYS PRO PRO ALA THR TYR LEU ASP TYR SER VAL SER LEU
SEQRES 5 B 247 VAL LYS LYS PRO GLN VAL THR VAL GLY ALA GLN ASN ALA
SEQRES 6 B 247 TYR LEU LYS ALA SER GLY ALA PHE THR GLY GLU ASN SER
SEQRES 7 B 247 VAL ASP GLN ILE LYS ASP VAL GLY ALA LYS TRP VAL ILE
SEQRES 8 B 247 LEU GLY HIS SER GLU ARG ARG SER TYR PHE HIS GLU ASP
SEQRES 9 B 247 ASP LYS PHE ILE ALA ASP LYS THR LYS PHE ALA LEU GLY
SEQRES 10 B 247 GLN GLY VAL GLY VAL ILE LEU CYS ILE GLY GLU THR LEU
SEQRES 11 B 247 GLU GLU LYS LYS ALA GLY LYS THR LEU ASP VAL VAL GLU
SEQRES 12 B 247 ARG GLN LEU ASN ALA VAL LEU GLU GLU VAL LYS ASP TRP
SEQRES 13 B 247 THR ASN VAL VAL VAL ALA TYR GLU PRO VAL TRP ALA ILE
SEQRES 14 B 247 GLY THR GLY LEU ALA ALA THR PRO GLU ASP ALA GLN ASP
SEQRES 15 B 247 ILE HIS ALA SER ILE ARG LYS PHE LEU ALA SER LYS LEU
SEQRES 16 B 247 GLY ASP LYS ALA ALA SER GLU LEU ARG ILE LEU TYR GLY
SEQRES 17 B 247 GLY SER ALA ASN GLY SER ASN ALA VAL THR PHE LYS ASP
SEQRES 18 B 247 LYS ALA ASP VAL ASP GLY PHE LEU VAL GLY GLY ALA SER
SEQRES 19 B 247 LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN SER ARG ASN
HET PGH A 249 10
HET PGH B 249 10
HETNAM PGH PHOSPHOGLYCOLOHYDROXAMIC ACID
FORMUL 3 PGH 2(C2 H6 N O6 P)
FORMUL 5 HOH *247(H2 O)
HELIX 1 AA LYS A 17 THR A 29 1 13
HELIX 2 AB ALA A 44 LEU A 53 1 10
HELIX 3 AC VAL A 80 VAL A 86 1 7
HELIX 4 AD1 SER A 96 TYR A 101 1SUBSTRATE POLARIZING HELIX 6
HELIX 5 AD2 ASP A 106 GLY A 118 1 13
HELIX 6 AE1 LEU A 131 LYS A 135 1 5
HELIX 7 AE2 THR A 139 VAL A 150 1 12
HELIX 8 AF1 PRO A 178 LYS A 195 1 18
HELIX 9 AF2 ASP A 198 GLU A 203 1 6
HELIX 10 AG1 GLY A 214 THR A 219 1 6
HELIX 11 AH1 GLY A 232 LEU A 236 1PHOSPHATE BINDING HELIX 5
HELIX 12 AH2 PRO A 238 ILE A 244 1 7
HELIX 13 BA LYS B 17 THR B 29 1 13
HELIX 14 BB ALA B 44 LEU B 53 1 10
HELIX 15 BC VAL B 80 VAL B 86 1 7
HELIX 16 BD1 SER B 96 TYR B 101 1SUBSTRATE POLARIZING HELIX 6
HELIX 17 BD2 ASP B 106 GLY B 118 1 13
HELIX 18 BE1 LEU B 131 LYS B 135 1 5
HELIX 19 BE2 THR B 139 VAL B 150 1 12
HELIX 20 BF1 PRO B 178 LYS B 195 1 18
HELIX 21 BF2 ASP B 198 GLU B 203 1 6
HELIX 22 BG1 GLY B 214 THR B 219 1 6
HELIX 23 BH1 GLY B 232 LEU B 236 1PHOSPHATE BINDING HELIX 5
HELIX 24 BH2 PRO B 238 ILE B 244 1 7
SHEET 1 A 9 PHE A 5 ASN A 10 0
SHEET 2 A 9 VAL A 36 CYS A 41 1 O GLU A 37 N VAL A 7
SHEET 3 A 9 VAL A 59 ALA A 63 1 O THR A 60 N ILE A 40
SHEET 4 A 9 TRP A 90 LEU A 93 1 O TRP A 90 N ALA A 63
SHEET 5 A 9 GLY A 122 ILE A 127 1 O GLY A 122 N VAL A 91
SHEET 6 A 9 VAL A 160 TYR A 164 1 N VAL A 161 O VAL A 123
SHEET 7 A 9 ILE A 206 GLY A 209 1 N LEU A 207 O VAL A 162
SHEET 8 A 9 GLY A 228 VAL A 231 1 O GLY A 228 N TYR A 208
SHEET 9 A 9 PHE A 5 ASN A 10 1 O PHE A 6 N PHE A 229
SHEET 1 B 9 PHE B 5 ASN B 10 0
SHEET 2 B 9 VAL B 36 CYS B 41 1 O GLU B 37 N VAL B 7
SHEET 3 B 9 VAL B 59 ALA B 63 1 N THR B 60 O VAL B 38
SHEET 4 B 9 TRP B 90 LEU B 93 1 O TRP B 90 N ALA B 63
SHEET 5 B 9 GLY B 122 ILE B 127 1 O GLY B 122 N VAL B 91
SHEET 6 B 9 VAL B 160 TYR B 164 1 N VAL B 161 O VAL B 123
SHEET 7 B 9 ILE B 206 GLY B 209 1 N LEU B 207 O VAL B 162
SHEET 8 B 9 GLY B 228 VAL B 231 1 O GLY B 228 N TYR B 208
SHEET 9 B 9 PHE B 5 ASN B 10 1 O PHE B 6 N PHE B 229
SITE 1 AC1 15 ASN A 10 LYS A 12 HIS A 95 GLU A 165
SITE 2 AC1 15 ALA A 169 ILE A 170 GLY A 171 SER A 211
SITE 3 AC1 15 LEU A 230 GLY A 232 GLY A 233 HOH A 620
SITE 4 AC1 15 HOH A 621 HOH A 622 HOH A 623
SITE 1 AC2 14 ASN B 10 LYS B 12 HIS B 95 GLU B 165
SITE 2 AC2 14 ALA B 169 ILE B 170 GLY B 171 SER B 211
SITE 3 AC2 14 LEU B 230 GLY B 232 GLY B 233 HOH B 629
SITE 4 AC2 14 HOH B 630 HOH B 634
CRYST1 74.000 83.500 38.400 90.00 99.55 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 0.013514 0.000000 0.002274 0.00000
SCALE2 0.000000 0.011976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026408 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
END
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