HEADER OXIDOREDUCTASE 17-MAR-05 1Z53
TITLE THE 1.13 ANGSTROM STRUCTURE OF IRON-FREE CYTOCHROME C PEROXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CCP;
COMPND 5 EC: 1.11.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: CCP1, CCP, CPO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: POULOS VECTOR (MODIFIED PT7)
KEYWDS CCP, HEME PEROXIDASE, IRON-FREE PROTOPORPHYRIN IX, TRP CATION
KEYWDS 2 RADICAL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BHASKAR,T.L.POULOS
REVDAT 4 03-APR-24 1Z53 1 REMARK
REVDAT 3 14-FEB-24 1Z53 1 REMARK
REVDAT 2 24-FEB-09 1Z53 1 VERSN
REVDAT 1 21-JUN-05 1Z53 0
JRNL AUTH B.BHASKAR,T.L.POULOS
JRNL TITL THE 1.13-A STRUCTURE OF IRON-FREE CYTOCHROME C PEROXIDASE.
JRNL REF J.BIOL.INORG.CHEM. V. 10 425 2005
JRNL REFN ISSN 0949-8257
JRNL PMID 15900441
JRNL DOI 10.1007/S00775-005-0654-4
REMARK 2
REMARK 2 RESOLUTION. 1.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.134
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.147
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.500
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 5123
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 153609
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.125
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.135
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.300
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3831
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 115429
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2367
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 530
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2935.4
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2223.1
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 16
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 23795
REMARK 3 NUMBER OF RESTRAINTS : 28345
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.089
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.098
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.069
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.051
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-03
REMARK 200 TEMPERATURE (KELVIN) : 116
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.78
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 189599
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.130
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 8.625
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.550
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: ATOMIC RESOLUTION STRUCTURE OF WILD TYPE CCP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% 2-METHYL-2,4-PENTANEDIOL (MPD), 50
REMARK 280 MM TRIS-PHOSPHATE, PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 53.42600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.52050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.86800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.52050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.42600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.86800
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 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 THR A 1
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 SER A 225 CB SER A 225 OG -0.079
REMARK 500 LEU A 294 C LEU A 294 OXT 0.211
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 PRO A 3 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 LEU A 4 C - N - CA ANGL. DEV. = 30.0 DEGREES
REMARK 500 PHE A 77 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 PHE A 91 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 143 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 143 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 166 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 210 CB - CG - OD2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 LYS A 264 CD - CE - NZ ANGL. DEV. = 16.3 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 ASP A 33 56.69 -92.76
REMARK 500 ALA A 194 59.59 -103.92
REMARK 500 ASP A 254 89.49 -156.71
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 PP9 A 296
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CYP RELATED DB: PDB
REMARK 900 ORIGINAL CCP STRUCTURE
REMARK 900 RELATED ID: 1KOK RELATED DB: PDB
REMARK 900 WILD TYPE CCP COMPLEXED WITH MESOPORPHYRIN
DBREF 1Z53 A 1 294 UNP P00431 CCPR_YEAST 68 361
SEQRES 1 A 294 THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU LYS GLY
SEQRES 2 A 294 ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE
SEQRES 3 A 294 ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR
SEQRES 4 A 294 ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS
SEQRES 5 A 294 THR SER GLY THR TRP ASP LYS HIS ASP ASN THR GLY GLY
SEQRES 6 A 294 SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU PHE ASN
SEQRES 7 A 294 ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE
SEQRES 8 A 294 LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE SER SER
SEQRES 9 A 294 GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA VAL GLN
SEQRES 10 A 294 GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG
SEQRES 11 A 294 VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN GLY ARG
SEQRES 12 A 294 LEU PRO ASP ALA ASP LYS ASP ALA ASP TYR VAL ARG THR
SEQRES 13 A 294 PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU VAL VAL
SEQRES 14 A 294 ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR HIS LEU
SEQRES 15 A 294 LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA ALA ASN
SEQRES 16 A 294 ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU LEU ASN
SEQRES 17 A 294 GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU
SEQRES 18 A 294 GLN TRP ASP SER LYS SER GLY TYR MET MET LEU PRO THR
SEQRES 19 A 294 ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU SER ILE
SEQRES 20 A 294 VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS
SEQRES 21 A 294 ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU ASN GLY
SEQRES 22 A 294 ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE ILE PHE
SEQRES 23 A 294 LYS THR LEU GLU GLU GLN GLY LEU
HET PP9 A 296 42
HETNAM PP9 PROTOPORPHYRIN IX
FORMUL 2 PP9 C34 H34 N4 O4
FORMUL 3 HOH *530(H2 O)
HELIX 1 1 SER A 15 ASP A 33 1 19
HELIX 2 2 GLU A 35 ILE A 40 1 6
HELIX 3 3 TYR A 42 GLY A 55 1 14
HELIX 4 4 GLY A 69 ARG A 72 5 4
HELIX 5 5 PHE A 73 ASN A 78 1 6
HELIX 6 6 ASP A 79 GLY A 84 5 6
HELIX 7 7 LEU A 85 PHE A 99 1 15
HELIX 8 8 SER A 103 MET A 119 1 17
HELIX 9 9 PRO A 134 THR A 138 5 5
HELIX 10 10 ASP A 150 ARG A 160 1 11
HELIX 11 11 ASN A 164 GLY A 173 1 10
HELIX 12 12 ALA A 174 LEU A 177 5 4
HELIX 13 13 HIS A 181 GLY A 186 1 6
HELIX 14 14 ASN A 200 GLU A 209 1 10
HELIX 15 15 LEU A 232 ASP A 241 1 10
HELIX 16 16 ASP A 241 ASN A 253 1 13
HELIX 17 17 ASP A 254 ASN A 272 1 19
HELIX 18 18 THR A 288 GLY A 293 1 6
SHEET 1 A 2 HIS A 6 VAL A 7 0
SHEET 2 A 2 ILE A 274 THR A 275 1 O THR A 275 N HIS A 6
SHEET 1 B 2 LYS A 179 THR A 180 0
SHEET 2 B 2 GLY A 189 PRO A 190 -1 O GLY A 189 N THR A 180
SHEET 1 C 3 TRP A 211 LYS A 215 0
SHEET 2 C 3 GLU A 221 SER A 225 -1 O GLN A 222 N GLU A 214
SHEET 3 C 3 MET A 230 MET A 231 -1 O MET A 231 N TRP A 223
SITE 1 AC1 25 PRO A 44 VAL A 45 ARG A 48 TRP A 51
SITE 2 AC1 25 ASP A 146 ALA A 147 LEU A 171 MET A 172
SITE 3 AC1 25 ALA A 174 HIS A 175 LEU A 177 GLY A 178
SITE 4 AC1 25 LYS A 179 THR A 180 HIS A 181 ASN A 184
SITE 5 AC1 25 SER A 185 TRP A 191 LEU A 232 THR A 234
SITE 6 AC1 25 HOH A1035 HOH A1037 HOH A1067 HOH A1085
SITE 7 AC1 25 HOH A1343
CRYST1 106.852 75.736 51.041 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 0.009359 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013204 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019592 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
