HEADER ELECTRON TRANSPORT 27-JUL-06 2HV4
TITLE NMR SOLUTION STRUCTURE REFINEMENT OF YEAST ISO-1-FERROCYTOCHROME C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C ISO-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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: CYC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEME PROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR M.ASSFALG,I.BERTINI,R.DEL CONTE,P.TURANO
REVDAT 4 20-OCT-21 2HV4 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2HV4 1 VERSN
REVDAT 2 04-NOV-08 2HV4 1 JRNL
REVDAT 1 26-SEP-06 2HV4 0
JRNL AUTH M.ASSFALG,I.BERTINI,R.DEL CONTE,A.GIACHETTI,P.TURANO
JRNL TITL CYTOCHROME C AND ORGANIC MOLECULES: SOLUTION STRUCTURE OF
JRNL TITL 2 THE P-AMINOPHENOL ADDUCT.
JRNL REF BIOCHEMISTRY V. 46 6232 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17488096
JRNL DOI 10.1021/BI7002857
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, AMBER 8.0
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HV4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038798.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2-3 MM CYTOCHROME C, 50 MM
REMARK 210 PHOSPHATE BUFFER, PH 7.0, 90%
REMARK 210 H2O, 10% D2O; 2-3 MM CYTOCHROME
REMARK 210 C U-15N, 50 MM PHOSPHATE BUFFER,
REMARK 210 PH 7.0, 90% H2O, 10% D2O; 2-3 MM
REMARK 210 CYTOCHROME C U-15N,13C, 50 MM
REMARK 210 PHOSPHATE BUFFER, PH 7.0, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION
REMARK 210 ANGLE SPACE FOLLOWED BY
REMARK 210 RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE PRESENT STRUCTURE IS A REFINEMENT OF 1YFC OBTAINED
REMARK 210 THROUGH HETERONUCLEAR NMR EXPERIMENTS AT HIGHER MAGNETIC FIELD,
REMARK 210 AND ADDITIONAL STRUCTURAL CONSTRAINTS. RESONANCES ASSIGNMENT WAS
REMARK 210 BASED ON HNCA, HN(CO)CA, (H)CCH-TOCSY, H(C)CH-TOCSY, CBCA(CO)NH,
REMARK 210 AND CCC(CO)NH EXPERIMENTS
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: CLOSE CONTACTS
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 HH TYR A 48 O2A HEC A 104 1.55
REMARK 500 HG1 THR A 49 O2D HEC A 104 1.58
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 1 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 5 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 5 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 15 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 20 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 20 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 22 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 25 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 26 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 26 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 27 ARG A 91 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 29 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 30 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 31 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 33 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 33 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 34 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.1 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 1 GLU A -4 91.46 -160.31
REMARK 500 1 PHE A -3 73.77 -63.73
REMARK 500 1 LYS A -2 93.82 -68.45
REMARK 500 1 ARG A 13 -43.15 -141.64
REMARK 500 1 VAL A 20 -6.28 -145.83
REMARK 500 1 LYS A 27 -117.55 -142.16
REMARK 500 1 PRO A 30 -178.01 -69.25
REMARK 500 1 HIS A 33 92.40 -66.20
REMARK 500 1 TYR A 48 -162.49 -70.83
REMARK 500 1 LYS A 54 -7.61 -59.18
REMARK 500 1 ASN A 56 59.72 17.83
REMARK 500 1 PHE A 82 -75.87 -39.53
REMARK 500 2 GLU A -4 -70.69 -125.04
REMARK 500 2 ALA A -1 117.24 -32.77
REMARK 500 2 ARG A 13 -54.42 -129.15
REMARK 500 2 LYS A 27 -137.60 -119.62
REMARK 500 2 GLU A 44 64.76 -62.99
REMARK 500 2 ASN A 56 62.34 22.51
REMARK 500 2 TRP A 59 86.60 -68.38
REMARK 500 2 ASN A 70 89.37 -153.60
REMARK 500 2 ALA A 81 2.03 -60.91
REMARK 500 2 PHE A 82 170.96 -56.72
REMARK 500 3 ALA A -1 178.85 58.28
REMARK 500 3 CYS A 14 -46.31 -138.12
REMARK 500 3 VAL A 20 -30.60 -135.79
REMARK 500 3 LYS A 27 -154.37 -68.41
REMARK 500 3 HIS A 33 -94.87 20.80
REMARK 500 3 TYR A 48 -117.30 -72.62
REMARK 500 3 ASN A 56 58.87 23.65
REMARK 500 3 ASN A 70 88.02 -153.06
REMARK 500 3 PHE A 82 -105.93 -53.27
REMARK 500 4 PHE A -3 79.58 -57.34
REMARK 500 4 HIS A 26 80.13 -69.77
REMARK 500 4 LYS A 27 -87.62 -72.34
REMARK 500 4 GLU A 44 82.40 -68.38
REMARK 500 4 TYR A 48 -111.25 -96.07
REMARK 500 4 ASN A 56 64.66 30.06
REMARK 500 4 MET A 80 83.17 -67.98
REMARK 500 4 PHE A 82 -31.22 -38.86
REMARK 500 5 GLU A -4 -39.80 -35.15
REMARK 500 5 ALA A -1 164.85 60.02
REMARK 500 5 LYS A 22 97.74 -65.07
REMARK 500 5 LYS A 27 -85.46 -117.49
REMARK 500 5 LEU A 32 22.13 -73.58
REMARK 500 5 HIS A 33 -94.28 -63.72
REMARK 500 5 GLU A 44 82.71 -60.13
REMARK 500 5 TYR A 48 -162.52 -62.07
REMARK 500 5 ASN A 56 62.66 22.11
REMARK 500 5 ASN A 70 70.04 -163.59
REMARK 500 5 PRO A 76 95.02 -68.85
REMARK 500
REMARK 500 THIS ENTRY HAS 353 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A -4 PHE A -3 6 144.08
REMARK 500 GLU A -4 PHE A -3 7 144.08
REMARK 500 THR A -5 GLU A -4 10 -144.85
REMARK 500 LYS A 100 ALA A 101 14 149.01
REMARK 500 THR A -5 GLU A -4 22 143.58
REMARK 500 THR A -5 GLU A -4 27 -148.54
REMARK 500 GLU A -4 PHE A -3 28 138.77
REMARK 500 GLU A 21 LYS A 22 30 149.31
REMARK 500 GLU A -4 PHE A -3 31 144.60
REMARK 500 GLN A 42 ALA A 43 33 149.49
REMARK 500 THR A -5 GLU A -4 34 -143.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 TYR A 46 0.07 SIDE CHAIN
REMARK 500 2 TYR A 48 0.08 SIDE CHAIN
REMARK 500 3 ARG A 13 0.08 SIDE CHAIN
REMARK 500 3 TYR A 48 0.07 SIDE CHAIN
REMARK 500 4 TYR A 97 0.08 SIDE CHAIN
REMARK 500 5 TYR A 67 0.08 SIDE CHAIN
REMARK 500 8 TYR A 46 0.08 SIDE CHAIN
REMARK 500 8 TYR A 48 0.10 SIDE CHAIN
REMARK 500 9 TYR A 46 0.08 SIDE CHAIN
REMARK 500 9 TYR A 48 0.10 SIDE CHAIN
REMARK 500 12 ARG A 13 0.10 SIDE CHAIN
REMARK 500 15 ARG A 13 0.12 SIDE CHAIN
REMARK 500 15 TYR A 46 0.08 SIDE CHAIN
REMARK 500 15 ARG A 91 0.08 SIDE CHAIN
REMARK 500 16 TYR A 48 0.07 SIDE CHAIN
REMARK 500 16 ARG A 91 0.15 SIDE CHAIN
REMARK 500 18 TYR A 46 0.07 SIDE CHAIN
REMARK 500 18 TYR A 74 0.07 SIDE CHAIN
REMARK 500 18 ARG A 91 0.09 SIDE CHAIN
REMARK 500 19 ARG A 91 0.10 SIDE CHAIN
REMARK 500 20 TYR A 46 0.07 SIDE CHAIN
REMARK 500 20 TYR A 74 0.07 SIDE CHAIN
REMARK 500 22 ARG A 13 0.09 SIDE CHAIN
REMARK 500 22 TYR A 48 0.10 SIDE CHAIN
REMARK 500 24 ARG A 38 0.12 SIDE CHAIN
REMARK 500 24 TYR A 48 0.08 SIDE CHAIN
REMARK 500 25 TYR A 48 0.09 SIDE CHAIN
REMARK 500 29 TYR A 67 0.07 SIDE CHAIN
REMARK 500 30 TYR A 97 0.08 SIDE CHAIN
REMARK 500 31 TYR A 46 0.07 SIDE CHAIN
REMARK 500 31 TYR A 48 0.08 SIDE CHAIN
REMARK 500 33 TYR A 48 0.07 SIDE CHAIN
REMARK 500 33 TYR A 74 0.07 SIDE CHAIN
REMARK 500 34 TYR A 48 0.08 SIDE CHAIN
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 HEC A 104 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 104 NA 88.3
REMARK 620 3 HEC A 104 NB 93.6 91.2
REMARK 620 4 HEC A 104 NC 86.7 174.9 90.4
REMARK 620 5 HEC A 104 ND 82.0 89.2 175.5 88.8
REMARK 620 6 MET A 80 SD 171.2 92.8 95.2 92.0 89.2
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 HEC A 104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YCC RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION REFINEMENT OF YEAST ISO-1-CYTOCHROME C AND
REMARK 900 COMPARISONS WITH OTHER EUKARYOTIC CYTOCHROMES C
REMARK 900 RELATED ID: 1YFC RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF A YEAST ISO-1-FERROCYTOCHROME C
DBREF 2HV4 A -5 103 UNP P00044 CYC1_YEAST 1 108
SEQADV 2HV4 THR A 102 UNP P00044 CYS 107 ENGINEERED MUTATION
SEQRES 1 A 108 THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR
SEQRES 2 A 108 LEU PHE LYS THR ARG CYS LEU GLN CYS HIS THR VAL GLU
SEQRES 3 A 108 LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY
SEQRES 4 A 108 ILE PHE GLY ARG HIS SER GLY GLN ALA GLU GLY TYR SER
SEQRES 5 A 108 TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP
SEQRES 6 A 108 GLU ASN ASN MET SER GLU TYR LEU THR ASN PRO LYS LYS
SEQRES 7 A 108 TYR ILE PRO GLY THR LYS MET ALA PHE GLY GLY LEU LYS
SEQRES 8 A 108 LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS
SEQRES 9 A 108 LYS ALA THR GLU
HET HEC A 104 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 SER A 2 LYS A 11 1 10
HELIX 2 2 THR A 49 ASN A 56 1 8
HELIX 3 3 ASP A 60 ASN A 70 1 11
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 ALA A 101 1 15
LINK SG CYS A 14 CAB HEC A 104 1555 1555 1.81
LINK SG CYS A 17 CAC HEC A 104 1555 1555 1.82
LINK NE2 HIS A 18 FE HEC A 104 1555 1555 2.16
LINK SD MET A 80 FE HEC A 104 1555 1555 2.39
SITE 1 AC1 18 ARG A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 18 VAL A 28 LEU A 32 SER A 40 GLY A 41
SITE 3 AC1 18 TYR A 48 THR A 49 ASN A 52 TRP A 59
SITE 4 AC1 18 TYR A 67 LEU A 68 THR A 78 LYS A 79
SITE 5 AC1 18 MET A 80 LEU A 85
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
