HEADER ELECTRON TRANSPORT/OXIDOREDUCTASE 12-APR-99 1QFN
TITLE GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GLUTAREDOXIN 1);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GRX 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: INTERMOLECULAR DISULFIDE BRIDGE BETWEEN; CYS 11 A AND
COMPND 8 CYS 148 B;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN (RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1);
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: APHA CHAIN, B1 SUBUNIT;
COMPND 13 SYNONYM: RIBONUCLEOTIDE REDUCTASE, B1 PROTEIN, R1 PROTEIN;
COMPND 14 EC: 1.17.4.1;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: YES;
COMPND 17 OTHER_DETAILS: INTERMOLECULAR DISULFIDE BRIDGE CYS759
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUTAREDOXIN, RIBONUCLEOTIDE REDUCTASE, DISULFIDE, ELECTRON TRANSFER,
KEYWDS 2 ELECTRON TRANSPORT-OXIDOREDUCTASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.J.BERARDI,J.H.BUSHWELLER
REVDAT 5 27-DEC-23 1QFN 1 REMARK
REVDAT 4 03-NOV-21 1QFN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1QFN 1 VERSN
REVDAT 2 01-APR-03 1QFN 1 JRNL
REVDAT 1 01-JAN-00 1QFN 0
JRNL AUTH M.J.BERARDI,J.H.BUSHWELLER
JRNL TITL BINDING SPECIFICITY AND MECHANISTIC INSIGHT INTO
JRNL TITL 2 GLUTAREDOXIN-CATALYZED PROTEIN DISULFIDE REDUCTION.
JRNL REF J.MOL.BIOL. V. 292 151 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10493864
JRNL DOI 10.1006/JMBI.1999.3067
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL V2.6
REMARK 3 AUTHORS : P.LUGINBUHL,P.GUNTERT,M.BILLETER,K.WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QFN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000832.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : RESTRICTED TORSIONAL ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
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
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
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 8 NH1 - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 1 ARG A 39 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 TYR A 13 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 39 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 TYR A 72 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 3 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ASP B 140 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 4 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 4 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 5 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 TYR A 13 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 5 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 5 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 TYR A 72 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 5 CYS B 148 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 6 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 6 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 7 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 7 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 7 TYR A 72 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 7 CYS B 148 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 8 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 8 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 8 ARG A 39 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 9 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 9 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 9 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 98 ANGLE DEVIATIONS.
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 SER A 9 72.63 -65.49
REMARK 500 1 PRO A 55 107.38 -56.98
REMARK 500 1 ASP A 65 53.23 35.82
REMARK 500 1 GLN B 139 118.82 -14.52
REMARK 500 1 ASP B 141 4.93 -156.30
REMARK 500 1 ALA B 147 18.58 54.76
REMARK 500 1 LYS B 149 179.15 177.06
REMARK 500 2 SER A 9 92.49 -62.39
REMARK 500 2 ASP A 65 41.94 35.47
REMARK 500 2 GLN A 66 2.63 83.32
REMARK 500 2 ASN A 82 -60.59 -93.80
REMARK 500 2 ILE B 138 41.02 -80.06
REMARK 500 2 GLN B 139 132.68 -39.91
REMARK 500 2 ASP B 141 -93.47 -163.27
REMARK 500 2 ALA B 147 19.36 51.27
REMARK 500 3 ASP A 65 6.69 52.96
REMARK 500 3 GLN A 66 9.37 95.76
REMARK 500 3 TYR A 72 -54.26 -29.93
REMARK 500 3 ASN A 82 -60.98 -101.95
REMARK 500 3 LEU B 134 94.32 -50.10
REMARK 500 3 ASP B 141 9.04 -155.33
REMARK 500 3 ALA B 147 15.42 50.96
REMARK 500 4 PRO A 55 85.43 -69.64
REMARK 500 4 ASP A 65 45.70 34.97
REMARK 500 4 ASP A 84 5.90 -69.01
REMARK 500 4 GLN B 139 102.97 6.86
REMARK 500 4 ASP B 141 -91.15 -142.30
REMARK 500 4 ALA B 147 16.64 50.81
REMARK 500 4 LYS B 149 171.69 179.87
REMARK 500 5 GLU A 57 -11.01 -140.20
REMARK 500 5 ASP A 65 46.66 37.11
REMARK 500 5 ASP B 141 -156.51 -165.43
REMARK 500 5 GLU B 144 -92.72 -96.19
REMARK 500 5 SER B 145 164.41 -48.59
REMARK 500 5 LYS B 149 169.83 176.68
REMARK 500 6 ALA A 40 -32.39 -136.26
REMARK 500 6 ASP A 65 17.69 52.80
REMARK 500 6 GLN A 66 5.93 94.56
REMARK 500 6 TYR A 72 -35.55 -33.63
REMARK 500 6 LYS B 149 176.91 176.74
REMARK 500 7 ILE A 38 -51.68 -129.43
REMARK 500 7 PRO A 55 77.39 -66.75
REMARK 500 7 GLN A 66 3.32 57.22
REMARK 500 7 LEU B 134 97.05 -65.93
REMARK 500 7 ASP B 141 -148.14 -163.12
REMARK 500 7 ALA B 147 18.25 54.02
REMARK 500 7 LYS B 149 166.59 177.27
REMARK 500 8 ASP A 37 86.66 -69.93
REMARK 500 8 ASP A 65 17.09 49.73
REMARK 500 8 GLN B 139 97.66 -170.06
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
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 1 TYR A 35 0.07 SIDE CHAIN
REMARK 500 2 TYR A 35 0.08 SIDE CHAIN
REMARK 500 3 TYR A 35 0.08 SIDE CHAIN
REMARK 500 4 TYR A 35 0.09 SIDE CHAIN
REMARK 500 4 ARG A 39 0.11 SIDE CHAIN
REMARK 500 4 TYR A 72 0.07 SIDE CHAIN
REMARK 500 5 TYR A 35 0.12 SIDE CHAIN
REMARK 500 5 TYR A 72 0.14 SIDE CHAIN
REMARK 500 6 TYR A 35 0.12 SIDE CHAIN
REMARK 500 7 TYR A 35 0.09 SIDE CHAIN
REMARK 500 7 TYR A 72 0.17 SIDE CHAIN
REMARK 500 8 TYR A 35 0.13 SIDE CHAIN
REMARK 500 9 TYR A 33 0.07 SIDE CHAIN
REMARK 500 9 TYR A 35 0.10 SIDE CHAIN
REMARK 500 9 ARG A 39 0.10 SIDE CHAIN
REMARK 500 10 TYR A 33 0.07 SIDE CHAIN
REMARK 500 10 TYR A 35 0.10 SIDE CHAIN
REMARK 500 10 ARG A 39 0.10 SIDE CHAIN
REMARK 500 11 ARG A 28 0.09 SIDE CHAIN
REMARK 500 11 TYR A 33 0.07 SIDE CHAIN
REMARK 500 11 TYR A 35 0.11 SIDE CHAIN
REMARK 500 12 ARG A 16 0.12 SIDE CHAIN
REMARK 500 12 TYR A 35 0.12 SIDE CHAIN
REMARK 500 12 ARG A 39 0.14 SIDE CHAIN
REMARK 500 12 TYR A 72 0.15 SIDE CHAIN
REMARK 500 13 TYR A 35 0.10 SIDE CHAIN
REMARK 500 13 TYR A 72 0.13 SIDE CHAIN
REMARK 500 14 TYR A 35 0.09 SIDE CHAIN
REMARK 500 15 TYR A 13 0.07 SIDE CHAIN
REMARK 500 15 TYR A 35 0.09 SIDE CHAIN
REMARK 500 16 TYR A 35 0.08 SIDE CHAIN
REMARK 500 16 TYR A 72 0.20 SIDE CHAIN
REMARK 500 18 TYR A 33 0.07 SIDE CHAIN
REMARK 500 18 TYR A 35 0.11 SIDE CHAIN
REMARK 500 19 TYR A 35 0.08 SIDE CHAIN
REMARK 500 19 TYR A 72 0.21 SIDE CHAIN
REMARK 500 20 TYR A 35 0.11 SIDE CHAIN
REMARK 500 20 ARG A 39 0.15 SIDE CHAIN
REMARK 500 20 TYR A 72 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QFN A 1 85 UNP P68688 GLRX1_ECOLI 1 85
DBREF 1QFN B 126 150 UNP P00452 RIR1_ECOLI 737 761
SEQADV 1QFN SER A 14 UNP P68688 CYS 14 ENGINEERED MUTATION
SEQRES 1 A 85 MET GLN THR VAL ILE PHE GLY ARG SER GLY CYS PRO TYR
SEQRES 2 A 85 SER VAL ARG ALA LYS ASP LEU ALA GLU LYS LEU SER ASN
SEQRES 3 A 85 GLU ARG ASP ASP PHE GLN TYR GLN TYR VAL ASP ILE ARG
SEQRES 4 A 85 ALA GLU GLY ILE THR LYS GLU ASP LEU GLN GLN LYS ALA
SEQRES 5 A 85 GLY LYS PRO VAL GLU THR VAL PRO GLN ILE PHE VAL ASP
SEQRES 6 A 85 GLN GLN HIS ILE GLY GLY TYR THR ASP PHE ALA ALA TRP
SEQRES 7 A 85 VAL LYS GLU ASN LEU ASP ALA
SEQRES 1 B 25 GLY ALA GLU ASP ALA GLN ASP ASP LEU VAL PRO SER ILE
SEQRES 2 B 25 GLN ASP ASP GLY SER GLU SER GLY ALA CYS LYS ILE
HELIX 1 1 PRO A 12 GLU A 27 1 16
HELIX 2 2 LYS A 45 ALA A 52 1 8
HELIX 3 3 TYR A 72 LEU A 83 1 12
SHEET 1 A 3 GLN A 32 VAL A 36 0
SHEET 2 A 3 GLN A 2 PHE A 6 1 N THR A 3 O GLN A 32
SHEET 3 A 3 ILE A 62 VAL A 64 -1 N PHE A 63 O VAL A 4
SSBOND 1 CYS A 11 CYS B 148 1555 1555 2.02
CISPEP 1 VAL A 59 PRO A 60 1 7.69
CISPEP 2 VAL A 59 PRO A 60 2 -0.83
CISPEP 3 VAL A 59 PRO A 60 3 -0.10
CISPEP 4 VAL A 59 PRO A 60 4 -4.11
CISPEP 5 VAL A 59 PRO A 60 5 -8.10
CISPEP 6 VAL A 59 PRO A 60 6 4.07
CISPEP 7 VAL A 59 PRO A 60 7 -5.18
CISPEP 8 VAL A 59 PRO A 60 8 6.90
CISPEP 9 VAL A 59 PRO A 60 9 1.87
CISPEP 10 VAL A 59 PRO A 60 10 1.87
CISPEP 11 VAL A 59 PRO A 60 11 8.56
CISPEP 12 VAL A 59 PRO A 60 12 7.99
CISPEP 13 VAL A 59 PRO A 60 13 8.02
CISPEP 14 VAL A 59 PRO A 60 14 -3.41
CISPEP 15 VAL A 59 PRO A 60 15 8.00
CISPEP 16 VAL A 59 PRO A 60 16 -1.11
CISPEP 17 VAL A 59 PRO A 60 17 7.86
CISPEP 18 VAL A 59 PRO A 60 18 0.60
CISPEP 19 VAL A 59 PRO A 60 19 4.31
CISPEP 20 VAL A 59 PRO A 60 20 4.58
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
