HEADER LYASE 14-APR-00 1EUA
TITLE SCHIFF BASE INTERMEDIATE IN KDPG ALDOLASE FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KDPG ALDOLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 4.1.2.14
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS BETA BARREL, TRIMER, CARBINOLAMINE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ALLARD,P.GROCHULSKI,J.SYGUSCH
REVDAT 6 15-NOV-23 1EUA 1 REMARK LINK ATOM
REVDAT 5 21-JAN-15 1EUA 1 REMARK VERSN
REVDAT 4 24-FEB-09 1EUA 1 VERSN
REVDAT 3 01-APR-03 1EUA 1 JRNL
REVDAT 2 04-APR-01 1EUA 1 JRNL
REVDAT 1 07-FEB-01 1EUA 0
JRNL AUTH J.ALLARD,P.GROCHULSKI,J.SYGUSCH
JRNL TITL COVALENT INTERMEDIATE TRAPPED IN 2-KETO-3-DEOXY-6-
JRNL TITL 2 PHOSPHOGLUCONATE (KDPG) ALDOLASE STRUCTURE AT 1.95-A
JRNL TITL 3 RESOLUTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 3679 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11274385
JRNL DOI 10.1073/PNAS.071380898
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 44409
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 SET) : 0.201
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2226
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4698
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 616
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.56700
REMARK 3 B22 (A**2) : 1.13100
REMARK 3 B33 (A**2) : 8.43500
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.315
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.302 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.954 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.151 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.105 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 51.53
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PYR.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : ACT.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PYR.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : ACT.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EUA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010897.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 190
REMARK 200 PH : 4.6
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) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44409
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.94
REMARK 200 R MERGE FOR SHELL (I) : 0.29300
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULFATE, SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 27.20500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.59500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.59500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.20500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.86000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 NZ LYS C 133 CB PYR C 2103 2.08
REMARK 500 NZ LYS C 133 O3 PYR C 2103 2.08
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 2239 O HOH B 2430 4446 2.18
REMARK 500 O HOH B 2399 O HOH B 2434 4446 2.19
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 ASN C 168 -10.03 -142.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 2102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR C 2103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EUN RELATED DB: PDB
DBREF 1EUA A 1 213 UNP P0A955 ALKH_ECOLI 1 213
DBREF 1EUA B 1 213 UNP P0A955 ALKH_ECOLI 1 213
DBREF 1EUA C 1 213 UNP P0A955 ALKH_ECOLI 1 213
SEQRES 1 A 213 MET LYS ASN TRP LYS THR SER ALA GLU SER ILE LEU THR
SEQRES 2 A 213 THR GLY PRO VAL VAL PRO VAL ILE VAL VAL LYS LYS LEU
SEQRES 3 A 213 GLU HIS ALA VAL PRO MET ALA LYS ALA LEU VAL ALA GLY
SEQRES 4 A 213 GLY VAL ARG VAL LEU GLU VAL THR LEU ARG THR GLU CYS
SEQRES 5 A 213 ALA VAL ASP ALA ILE ARG ALA ILE ALA LYS GLU VAL PRO
SEQRES 6 A 213 GLU ALA ILE VAL GLY ALA GLY THR VAL LEU ASN PRO GLN
SEQRES 7 A 213 GLN LEU ALA GLU VAL THR GLU ALA GLY ALA GLN PHE ALA
SEQRES 8 A 213 ILE SER PRO GLY LEU THR GLU PRO LEU LEU LYS ALA ALA
SEQRES 9 A 213 THR GLU GLY THR ILE PRO LEU ILE PRO GLY ILE SER THR
SEQRES 10 A 213 VAL SER GLU LEU MET LEU GLY MET ASP TYR GLY LEU LYS
SEQRES 11 A 213 GLU PHE LYS PHE PHE PRO ALA GLU ALA ASN GLY GLY VAL
SEQRES 12 A 213 LYS ALA LEU GLN ALA ILE ALA GLY PRO PHE SER GLN VAL
SEQRES 13 A 213 ARG PHE CYS PRO THR GLY GLY ILE SER PRO ALA ASN TYR
SEQRES 14 A 213 ARG ASP TYR LEU ALA LEU LYS SER VAL LEU CYS ILE GLY
SEQRES 15 A 213 GLY SER TRP LEU VAL PRO ALA ASP ALA LEU GLU ALA GLY
SEQRES 16 A 213 ASP TYR ASP ARG ILE THR LYS LEU ALA ARG GLU ALA VAL
SEQRES 17 A 213 GLU GLY ALA LYS LEU
SEQRES 1 B 213 MET LYS ASN TRP LYS THR SER ALA GLU SER ILE LEU THR
SEQRES 2 B 213 THR GLY PRO VAL VAL PRO VAL ILE VAL VAL LYS LYS LEU
SEQRES 3 B 213 GLU HIS ALA VAL PRO MET ALA LYS ALA LEU VAL ALA GLY
SEQRES 4 B 213 GLY VAL ARG VAL LEU GLU VAL THR LEU ARG THR GLU CYS
SEQRES 5 B 213 ALA VAL ASP ALA ILE ARG ALA ILE ALA LYS GLU VAL PRO
SEQRES 6 B 213 GLU ALA ILE VAL GLY ALA GLY THR VAL LEU ASN PRO GLN
SEQRES 7 B 213 GLN LEU ALA GLU VAL THR GLU ALA GLY ALA GLN PHE ALA
SEQRES 8 B 213 ILE SER PRO GLY LEU THR GLU PRO LEU LEU LYS ALA ALA
SEQRES 9 B 213 THR GLU GLY THR ILE PRO LEU ILE PRO GLY ILE SER THR
SEQRES 10 B 213 VAL SER GLU LEU MET LEU GLY MET ASP TYR GLY LEU LYS
SEQRES 11 B 213 GLU PHE LYS PHE PHE PRO ALA GLU ALA ASN GLY GLY VAL
SEQRES 12 B 213 LYS ALA LEU GLN ALA ILE ALA GLY PRO PHE SER GLN VAL
SEQRES 13 B 213 ARG PHE CYS PRO THR GLY GLY ILE SER PRO ALA ASN TYR
SEQRES 14 B 213 ARG ASP TYR LEU ALA LEU LYS SER VAL LEU CYS ILE GLY
SEQRES 15 B 213 GLY SER TRP LEU VAL PRO ALA ASP ALA LEU GLU ALA GLY
SEQRES 16 B 213 ASP TYR ASP ARG ILE THR LYS LEU ALA ARG GLU ALA VAL
SEQRES 17 B 213 GLU GLY ALA LYS LEU
SEQRES 1 C 213 MET LYS ASN TRP LYS THR SER ALA GLU SER ILE LEU THR
SEQRES 2 C 213 THR GLY PRO VAL VAL PRO VAL ILE VAL VAL LYS LYS LEU
SEQRES 3 C 213 GLU HIS ALA VAL PRO MET ALA LYS ALA LEU VAL ALA GLY
SEQRES 4 C 213 GLY VAL ARG VAL LEU GLU VAL THR LEU ARG THR GLU CYS
SEQRES 5 C 213 ALA VAL ASP ALA ILE ARG ALA ILE ALA LYS GLU VAL PRO
SEQRES 6 C 213 GLU ALA ILE VAL GLY ALA GLY THR VAL LEU ASN PRO GLN
SEQRES 7 C 213 GLN LEU ALA GLU VAL THR GLU ALA GLY ALA GLN PHE ALA
SEQRES 8 C 213 ILE SER PRO GLY LEU THR GLU PRO LEU LEU LYS ALA ALA
SEQRES 9 C 213 THR GLU GLY THR ILE PRO LEU ILE PRO GLY ILE SER THR
SEQRES 10 C 213 VAL SER GLU LEU MET LEU GLY MET ASP TYR GLY LEU LYS
SEQRES 11 C 213 GLU PHE LYS PHE PHE PRO ALA GLU ALA ASN GLY GLY VAL
SEQRES 12 C 213 LYS ALA LEU GLN ALA ILE ALA GLY PRO PHE SER GLN VAL
SEQRES 13 C 213 ARG PHE CYS PRO THR GLY GLY ILE SER PRO ALA ASN TYR
SEQRES 14 C 213 ARG ASP TYR LEU ALA LEU LYS SER VAL LEU CYS ILE GLY
SEQRES 15 C 213 GLY SER TRP LEU VAL PRO ALA ASP ALA LEU GLU ALA GLY
SEQRES 16 C 213 ASP TYR ASP ARG ILE THR LYS LEU ALA ARG GLU ALA VAL
SEQRES 17 C 213 GLU GLY ALA LYS LEU
HET ACT A2001 4
HET ACT A2002 4
HET SO4 A2202 5
HET PYR A2101 6
HET SO4 B2201 5
HET PYR B2102 6
HET SO4 C2203 5
HET PYR C2103 6
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM PYR PYRUVIC ACID
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 6 SO4 3(O4 S 2-)
FORMUL 7 PYR 3(C3 H4 O3)
FORMUL 12 HOH *616(H2 O)
HELIX 1 1 SER A 7 THR A 14 1 8
HELIX 2 2 LYS A 25 GLU A 27 5 3
HELIX 3 3 HIS A 28 GLY A 39 1 12
HELIX 4 4 CYS A 52 VAL A 64 1 13
HELIX 5 5 ASN A 76 GLY A 87 1 12
HELIX 6 6 THR A 97 GLY A 107 1 11
HELIX 7 7 THR A 117 TYR A 127 1 11
HELIX 8 8 PRO A 136 GLY A 141 1 6
HELIX 9 9 GLY A 141 ALA A 150 1 10
HELIX 10 10 ASN A 168 ALA A 174 1 7
HELIX 11 11 PRO A 188 ALA A 194 1 7
HELIX 12 12 ASP A 196 ALA A 211 1 16
HELIX 13 13 SER B 7 THR B 14 1 8
HELIX 14 14 LYS B 25 GLU B 27 5 3
HELIX 15 15 HIS B 28 GLY B 39 1 12
HELIX 16 16 CYS B 52 VAL B 64 1 13
HELIX 17 17 ASN B 76 ALA B 86 1 11
HELIX 18 18 THR B 97 GLY B 107 1 11
HELIX 19 19 THR B 117 TYR B 127 1 11
HELIX 20 20 GLY B 141 GLY B 151 1 11
HELIX 21 21 ASN B 168 ALA B 174 1 7
HELIX 22 22 PRO B 188 ALA B 194 1 7
HELIX 23 23 ASP B 196 ALA B 211 1 16
HELIX 24 24 SER C 7 THR C 14 1 8
HELIX 25 25 LYS C 25 GLU C 27 5 3
HELIX 26 26 HIS C 28 GLY C 39 1 12
HELIX 27 27 CYS C 52 VAL C 64 1 13
HELIX 28 28 ASN C 76 ALA C 86 1 11
HELIX 29 29 THR C 97 GLY C 107 1 11
HELIX 30 30 THR C 117 TYR C 127 1 11
HELIX 31 31 PRO C 136 GLY C 141 1 6
HELIX 32 32 GLY C 141 ALA C 150 1 10
HELIX 33 33 ASN C 168 ALA C 174 1 7
HELIX 34 34 PRO C 188 GLY C 195 1 8
HELIX 35 35 ASP C 196 ALA C 211 1 16
SHEET 1 A 4 ILE A 68 GLY A 72 0
SHEET 2 A 4 VAL A 43 THR A 47 1 O LEU A 44 N GLY A 70
SHEET 3 A 4 VAL A 17 ILE A 21 1 O PRO A 19 N GLU A 45
SHEET 4 A 4 ILE A 181 GLY A 183 1 O ILE A 181 N VAL A 18
SHEET 1 B 4 ALA A 91 SER A 93 0
SHEET 2 B 4 LEU A 111 ILE A 115 1 N ILE A 112 O ALA A 91
SHEET 3 B 4 GLU A 131 PHE A 134 1 N LYS A 133 O PRO A 113
SHEET 4 B 4 ARG A 157 PRO A 160 1 O ARG A 157 N PHE A 132
SHEET 1 C 4 ILE B 68 GLY B 72 0
SHEET 2 C 4 VAL B 43 THR B 47 1 O LEU B 44 N GLY B 70
SHEET 3 C 4 VAL B 17 ILE B 21 1 O PRO B 19 N GLU B 45
SHEET 4 C 4 ILE B 181 GLY B 183 1 O ILE B 181 N VAL B 18
SHEET 1 D 4 ALA B 91 SER B 93 0
SHEET 2 D 4 LEU B 111 ILE B 115 1 N ILE B 112 O ALA B 91
SHEET 3 D 4 GLU B 131 PHE B 134 1 N LYS B 133 O PRO B 113
SHEET 4 D 4 ARG B 157 PRO B 160 1 O ARG B 157 N PHE B 132
SHEET 1 E 4 ILE C 68 GLY C 72 0
SHEET 2 E 4 VAL C 43 THR C 47 1 O LEU C 44 N GLY C 70
SHEET 3 E 4 VAL C 17 ILE C 21 1 O PRO C 19 N GLU C 45
SHEET 4 E 4 ILE C 181 GLY C 183 1 O ILE C 181 N VAL C 18
SHEET 1 F 4 ALA C 91 SER C 93 0
SHEET 2 F 4 LEU C 111 ILE C 115 1 N ILE C 112 O ALA C 91
SHEET 3 F 4 GLU C 131 PHE C 134 1 N LYS C 133 O PRO C 113
SHEET 4 F 4 ARG C 157 PRO C 160 1 O ARG C 157 N PHE C 132
LINK NZ LYS A 133 CA PYR A2101 1555 1555 1.48
LINK NZ LYS A 133 CB PYR A2101 1555 1555 1.88
LINK NZ LYS B 133 CA PYR B2102 1555 1555 1.45
LINK NZ LYS C 133 CA PYR C2103 1555 1555 1.23
CISPEP 1 PHE A 135 PRO A 136 0 -0.95
CISPEP 2 PHE B 135 PRO B 136 0 -0.57
CISPEP 3 PHE C 135 PRO C 136 0 -0.83
SITE 1 AC1 3 LEU A 96 HOH A2380 SER B 119
SITE 1 AC2 6 VAL A 23 LYS A 24 LYS A 25 HIS A 28
SITE 2 AC2 6 LEU A 192 HOH A2309
SITE 1 AC3 8 GLY B 162 GLY B 163 SER B 184 HOH B2226
SITE 2 AC3 8 HOH B2257 HOH B2340 HOH B2351 HOH B2444
SITE 1 AC4 7 GLY A 162 GLY A 163 SER A 184 HOH A2248
SITE 2 AC4 7 HOH A2299 HOH A2326 HOH A2376
SITE 1 AC5 7 GLY C 162 GLY C 163 SER C 184 HOH C2205
SITE 2 AC5 7 HOH C2234 HOH C2265 HOH C2333
SITE 1 AC6 9 VAL A 20 GLU A 45 ARG A 49 GLY A 72
SITE 2 AC6 9 THR A 73 ILE A 92 SER A 93 PRO A 94
SITE 3 AC6 9 LYS A 133
SITE 1 AC7 8 GLU B 45 ARG B 49 THR B 73 ILE B 92
SITE 2 AC7 8 SER B 93 PRO B 94 LYS B 133 HOH B2244
SITE 1 AC8 8 GLU C 45 ARG C 49 GLY C 72 THR C 73
SITE 2 AC8 8 ILE C 92 SER C 93 PRO C 94 LYS C 133
CRYST1 54.410 85.720 133.190 90.00 90.00 90.00 P 21 21 21 12
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 0.018379 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007508 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
