HEADER ELECTRON TRANSPORT 17-SEP-97 6FD1
TITLE 7-FE FERREDOXIN FROM AZOTOBACTER VINELANDII LOW TEMPERATURE, 1.35 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7-FE FERREDOXIN I (FD1);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FD1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;
SOURCE 3 ORGANISM_TAXID: 354
KEYWDS ELECTRON TRANSPORT, IRON-SULFUR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.STOUT,E.A.STURA,D.E.MCREE
REVDAT 4 09-AUG-23 6FD1 1 REMARK LINK
REVDAT 3 24-MAR-09 6FD1 1 ATOM CONECT
REVDAT 2 24-FEB-09 6FD1 1 VERSN
REVDAT 1 12-NOV-97 6FD1 0
JRNL AUTH C.D.STOUT,E.A.STURA,D.E.MCREE
JRNL TITL STRUCTURE OF AZOTOBACTER VINELANDII 7FE FERREDOXIN AT 1.35 A
JRNL TITL 2 RESOLUTION AND DETERMINATION OF THE [FE-S] BONDS WITH 0.01 A
JRNL TITL 3 ACCURACY.
JRNL REF J.MOL.BIOL. V. 278 629 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9600844
JRNL DOI 10.1006/JMBI.1998.1732
REMARK 2
REMARK 2 RESOLUTION. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 CROSS-VALIDATION METHOD : R-FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : EVERY 20TH REFLECTION
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.150
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.153
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1544
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 30880
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.138
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.139
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1218
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 24118
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 841
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1011.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 776.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 1
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 9211
REMARK 3 NUMBER OF RESTRAINTS : 10844
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 ANGLE DISTANCES (A) : 0.040
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.020
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.200
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.200
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.200
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.020
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.020
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.300
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.200
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: FE CLUSTERS NOT RESTRAINED
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FREE R USED UNTIL LAST CYCLE WHEN ALL
REMARK 3 DATA WAS INCLUDED.
REMARK 4
REMARK 4 6FD1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179818.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : APR-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57315
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.74700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: TRIVIAL CASE
REMARK 200 STARTING MODEL: PDB ENTRY 5FD1
REMARK 200
REMARK 200 REMARK: ALL DATA INCLUDING NEGATIVE I'S WERE USED WERE PROCESSED
REMARK 200 IN POINT GROUP 422 - PRESERVE BIJVOET PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CRYSTALLIZED FROM 4.8M
REMARK 280 AMMONIUM SULFATE, 0.45M TRIS-HCL, PH 7.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.32000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.42000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.42000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.16000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.42000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.42000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.48000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.42000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.42000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.16000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.42000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.42000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 69.48000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 46.32000
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 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 ASP A 15 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 HIS A 35 CB - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 90 C - N - CA ANGL. DEV. = -15.1 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 THR A 5 -169.17 -117.40
REMARK 500 ASP A 90 41.20 -99.57
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 F3S A 108 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 F3S A 108 S1 111.9
REMARK 620 3 F3S A 108 S3 116.1 103.9
REMARK 620 4 F3S A 108 S4 109.0 111.4 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 108 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 16 SG
REMARK 620 2 F3S A 108 S1 113.7
REMARK 620 3 F3S A 108 S2 106.8 113.6
REMARK 620 4 F3S A 108 S3 116.0 100.4 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 SF4 A 107 S1 108.5
REMARK 620 3 SF4 A 107 S2 122.1 102.3
REMARK 620 4 SF4 A 107 S3 113.9 104.0 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 SF4 A 107 S2 119.6
REMARK 620 3 SF4 A 107 S3 118.3 106.0
REMARK 620 4 SF4 A 107 S4 103.2 103.8 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 42 SG
REMARK 620 2 SF4 A 107 S1 99.4
REMARK 620 3 SF4 A 107 S3 119.3 106.7
REMARK 620 4 SF4 A 107 S4 121.5 103.8 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 107 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 SF4 A 107 S1 110.6
REMARK 620 3 SF4 A 107 S2 119.9 104.4
REMARK 620 4 SF4 A 107 S4 111.8 104.7 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 108 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 49 SG
REMARK 620 2 F3S A 108 S2 112.2
REMARK 620 3 F3S A 108 S3 108.0 105.8
REMARK 620 4 F3S A 108 S4 112.6 114.8 102.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 108
DBREF 6FD1 A 1 106 UNP P00214 FER1_AZOVI 1 106
SEQRES 1 A 106 ALA PHE VAL VAL THR ASP ASN CYS ILE LYS CYS LYS TYR
SEQRES 2 A 106 THR ASP CYS VAL GLU VAL CYS PRO VAL ASP CYS PHE TYR
SEQRES 3 A 106 GLU GLY PRO ASN PHE LEU VAL ILE HIS PRO ASP GLU CYS
SEQRES 4 A 106 ILE ASP CYS ALA LEU CYS GLU PRO GLU CYS PRO ALA GLN
SEQRES 5 A 106 ALA ILE PHE SER GLU ASP GLU VAL PRO GLU ASP MET GLN
SEQRES 6 A 106 GLU PHE ILE GLN LEU ASN ALA GLU LEU ALA GLU VAL TRP
SEQRES 7 A 106 PRO ASN ILE THR GLU LYS LYS ASP PRO LEU PRO ASP ALA
SEQRES 8 A 106 GLU ASP TRP ASP GLY VAL LYS GLY LYS LEU GLN HIS LEU
SEQRES 9 A 106 GLU ARG
HET SF4 A 107 8
HET F3S A 108 7
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
FORMUL 2 SF4 FE4 S4
FORMUL 3 F3S FE3 S4
FORMUL 4 HOH *162(H2 O)
HELIX 1 1 ASP A 6 CYS A 8 5 3
HELIX 2 2 ASP A 15 VAL A 19 5 5
HELIX 3 3 GLU A 46 GLU A 48 5 3
HELIX 4 4 GLU A 57 GLU A 59 5 3
HELIX 5 5 GLU A 62 GLU A 76 5 15
HELIX 6 6 ALA A 91 TRP A 94 1 4
HELIX 7 7 LYS A 100 HIS A 103 5 4
SHEET 1 A 2 PHE A 2 VAL A 4 0
SHEET 2 A 2 ILE A 54 SER A 56 -1 N PHE A 55 O VAL A 3
SHEET 1 B 2 PHE A 25 GLU A 27 0
SHEET 2 B 2 LEU A 32 ILE A 34 -1 N VAL A 33 O TYR A 26
LINK SG CYS A 8 FE3 F3S A 108 1555 1555 2.29
LINK SG CYS A 16 FE1 F3S A 108 1555 1555 2.31
LINK SG CYS A 20 FE4 SF4 A 107 1555 1555 2.29
LINK SG CYS A 39 FE1 SF4 A 107 1555 1555 2.30
LINK SG CYS A 42 FE2 SF4 A 107 1555 1555 2.27
LINK SG CYS A 45 FE3 SF4 A 107 1555 1555 2.26
LINK SG CYS A 49 FE4 F3S A 108 1555 1555 2.32
SITE 1 AC1 10 PHE A 2 CYS A 20 VAL A 22 CYS A 24
SITE 2 AC1 10 PHE A 25 CYS A 39 ILE A 40 CYS A 42
SITE 3 AC1 10 ALA A 43 CYS A 45
SITE 1 AC2 7 CYS A 8 LYS A 12 TYR A 13 THR A 14
SITE 2 AC2 7 ASP A 15 CYS A 16 CYS A 49
CRYST1 54.840 54.840 92.640 90.00 90.00 90.00 P 41 21 2 8
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 0.018235 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010794 0.00000
(ATOM LINES ARE NOT SHOWN.)
END