HEADER ELECTRON TRANSPORT 08-OCT-91 1EGR
TITLE SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE
TITLE 2 THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.SODANO,T.-H.XIA,J.H.BUSHWELLER,O.BJORNBERG,A.HOLMGREN,M.BILLETER,
AUTHOR 2 K.WUTHRICH
REVDAT 4 16-FEB-22 1EGR 1 REMARK
REVDAT 3 24-FEB-09 1EGR 1 VERSN
REVDAT 2 01-APR-03 1EGR 1 JRNL
REVDAT 1 31-OCT-93 1EGR 0
JRNL AUTH P.SODANO,T.H.XIA,J.H.BUSHWELLER,O.BJORNBERG,A.HOLMGREN,
JRNL AUTH 2 M.BILLETER,K.WUTHRICH
JRNL TITL SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF
JRNL TITL 2 THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI
JRNL TITL 3 GLUTAREDOXIN.
JRNL REF J.MOL.BIOL. V. 221 1311 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1942053
JRNL DOI 10.1016/0022-2836(91)90935-Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.-H.XIA,J.H.BUSHWELLER,P.SODANO,M.BILLETER,O.BJORNBERG,
REMARK 1 AUTH 2 A.HOLMGREN,K.WUTHRICH
REMARK 1 TITL THE NMR STRUCTURE OF OXIDIZED E. COLI GLUTAREDOXIN.
REMARK 1 TITL 2 COMPARISON WITH REDUCED E. COLI GLUTAREDOXIN AND
REMARK 1 TITL 3 FUNCTIONALLY RELATED PROTEINS
REMARK 1 REF PROTEIN SCI. V. 1 310 1992
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.SODANO,K.V.R.CHARY,O.BJORNBERG,A.HOLMGREN,B.KREN,
REMARK 1 AUTH 2 J.A.FUCHS,K.WUTHRICH
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE STUDIES OF RECOMBINANT
REMARK 1 TITL 2 ESCHERICHIA COLI GLUTAREDOXIN: SEQUENCE-SPECIFIC ASSIGNMENTS
REMARK 1 TITL 3 AND SECONDARY STRUCTURE DETERMINATION FOR THE OXIDIZED FORM
REMARK 1 REF EUR.J.BIOCHEM. V. 200 369 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 3
REMARK 1 AUTH O.BJORNBERG,A.HOLMGREN
REMARK 1 TITL CHARACTERIZATION OF HOMOGENEOUS RECOMBINANT GLUTAREDOXIN
REMARK 1 TITL 2 FROM ESCHERICHIA COLI: PURIFICATION FROM AN INDUCIBLE
REMARK 1 TITL 3 LAMBDA-P(L) EXPRESSION SYSTEM AND PROPERTIES OF A NOVEL
REMARK 1 TITL 4 ELONGATED FORM PROTEIN EXPRESSION AND PURIFICATION
REMARK 1 REF PROTEIN EXPR.PURIF. V. 2 287 1991
REMARK 1 REFN ISSN 1046-5928
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRAUN,WUTHRICH (DIANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173048.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 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 1 HIS A 68 NE2 HIS A 68 CD2 -0.072
REMARK 500 2 HIS A 68 NE2 HIS A 68 CD2 -0.075
REMARK 500 3 HIS A 68 NE2 HIS A 68 CD2 -0.074
REMARK 500 4 HIS A 68 NE2 HIS A 68 CD2 -0.073
REMARK 500 5 HIS A 68 NE2 HIS A 68 CD2 -0.078
REMARK 500 6 HIS A 68 NE2 HIS A 68 CD2 -0.075
REMARK 500 7 HIS A 68 NE2 HIS A 68 CD2 -0.077
REMARK 500 8 HIS A 68 NE2 HIS A 68 CD2 -0.073
REMARK 500 9 HIS A 68 NE2 HIS A 68 CD2 -0.077
REMARK 500 10 HIS A 68 NE2 HIS A 68 CD2 -0.074
REMARK 500 11 HIS A 68 NE2 HIS A 68 CD2 -0.075
REMARK 500 12 HIS A 68 NE2 HIS A 68 CD2 -0.080
REMARK 500 13 HIS A 68 NE2 HIS A 68 CD2 -0.079
REMARK 500 14 HIS A 68 NE2 HIS A 68 CD2 -0.077
REMARK 500 15 HIS A 68 NE2 HIS A 68 CD2 -0.075
REMARK 500 16 HIS A 68 NE2 HIS A 68 CD2 -0.078
REMARK 500 17 HIS A 68 NE2 HIS A 68 CD2 -0.083
REMARK 500 18 HIS A 68 NE2 HIS A 68 CD2 -0.077
REMARK 500 19 HIS A 68 NE2 HIS A 68 CD2 -0.076
REMARK 500 20 HIS A 68 NE2 HIS A 68 CD2 -0.078
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 TRP A 78 CG - CD2 - CE3 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 9 ARG A 39 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 10 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 13 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 13 TRP A 78 CG - CD2 - CE3 ANGL. DEV. = -5.8 DEGREES
REMARK 500 15 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 16 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 17 ARG A 8 NE - CZ - NH2 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 PRO A 12 51.27 -69.77
REMARK 500 1 ASP A 29 3.68 -63.88
REMARK 500 1 ALA A 40 -39.91 -39.09
REMARK 500 1 LYS A 54 76.03 37.20
REMARK 500 1 PRO A 55 33.79 -90.35
REMARK 500 1 VAL A 56 -102.17 32.06
REMARK 500 1 ASP A 65 -79.37 54.93
REMARK 500 2 ARG A 8 -162.04 -113.62
REMARK 500 2 TYR A 13 -73.54 -112.92
REMARK 500 2 GLU A 57 -64.06 -26.14
REMARK 500 2 THR A 58 -154.50 -116.79
REMARK 500 2 ASP A 65 -94.76 57.41
REMARK 500 3 ASP A 29 12.27 -62.17
REMARK 500 3 THR A 44 -92.77 -118.70
REMARK 500 3 LYS A 45 -55.16 -138.45
REMARK 500 3 GLU A 57 -43.08 -133.65
REMARK 500 3 THR A 58 -148.31 -114.54
REMARK 500 3 GLN A 66 -56.40 -122.95
REMARK 500 3 ASN A 82 -41.79 -143.68
REMARK 500 3 ASP A 84 -134.70 -103.26
REMARK 500 4 ARG A 8 -114.37 -135.88
REMARK 500 4 SER A 9 -74.81 -113.58
REMARK 500 4 GLU A 27 -48.47 -133.62
REMARK 500 4 ASP A 29 35.04 -80.90
REMARK 500 4 GLU A 57 -109.69 -101.65
REMARK 500 4 THR A 58 -73.48 -120.26
REMARK 500 4 ASP A 65 -75.83 70.90
REMARK 500 5 CYS A 11 165.44 108.82
REMARK 500 5 PRO A 12 75.99 -54.76
REMARK 500 5 TYR A 13 -77.89 -113.82
REMARK 500 5 ASP A 30 41.19 -82.86
REMARK 500 5 PRO A 55 94.70 -41.92
REMARK 500 5 VAL A 56 -95.04 33.32
REMARK 500 5 GLU A 57 -170.21 109.14
REMARK 500 5 THR A 58 -152.49 -104.03
REMARK 500 5 ASP A 65 -81.25 51.08
REMARK 500 5 GLU A 81 -45.47 -140.21
REMARK 500 5 ASP A 84 46.62 -89.08
REMARK 500 6 PRO A 12 48.53 -72.55
REMARK 500 6 ASN A 26 40.36 -98.30
REMARK 500 6 GLU A 27 -52.30 -142.53
REMARK 500 6 ASP A 29 -40.55 71.51
REMARK 500 6 THR A 58 -169.27 -116.08
REMARK 500 6 ASP A 65 -72.72 65.50
REMARK 500 6 TYR A 72 -55.85 -137.97
REMARK 500 6 ASN A 82 -36.11 -147.50
REMARK 500 6 ASP A 84 -64.82 -93.29
REMARK 500 7 SER A 9 73.35 -54.98
REMARK 500 7 VAL A 15 -12.74 -44.75
REMARK 500 7 GLU A 27 -65.70 -121.17
REMARK 500
REMARK 500 THIS ENTRY HAS 168 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 LYS A 54 PRO A 55 4 138.15
REMARK 500 LYS A 54 PRO A 55 8 -138.78
REMARK 500 LYS A 54 PRO A 55 9 143.41
REMARK 500 LYS A 54 PRO A 55 11 96.83
REMARK 500 LYS A 54 PRO A 55 12 128.16
REMARK 500 LYS A 54 PRO A 55 13 146.22
REMARK 500 CYS A 11 PRO A 12 14 -122.27
REMARK 500 LYS A 54 PRO A 55 14 147.85
REMARK 500 CYS A 11 PRO A 12 15 -127.22
REMARK 500 LYS A 54 PRO A 55 15 131.96
REMARK 500 LYS A 54 PRO A 55 16 137.34
REMARK 500 LYS A 54 PRO A 55 17 -143.09
REMARK 500 CYS A 11 PRO A 12 19 -147.36
REMARK 500 LYS A 54 PRO A 55 20 127.18
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 ARG A 8 0.29 SIDE CHAIN
REMARK 500 1 ARG A 16 0.19 SIDE CHAIN
REMARK 500 1 ARG A 28 0.32 SIDE CHAIN
REMARK 500 1 ARG A 39 0.27 SIDE CHAIN
REMARK 500 2 ARG A 8 0.29 SIDE CHAIN
REMARK 500 2 ARG A 16 0.22 SIDE CHAIN
REMARK 500 2 ARG A 28 0.26 SIDE CHAIN
REMARK 500 2 ARG A 39 0.25 SIDE CHAIN
REMARK 500 3 ARG A 8 0.32 SIDE CHAIN
REMARK 500 3 ARG A 16 0.19 SIDE CHAIN
REMARK 500 3 ARG A 28 0.22 SIDE CHAIN
REMARK 500 3 ARG A 39 0.30 SIDE CHAIN
REMARK 500 4 ARG A 8 0.19 SIDE CHAIN
REMARK 500 4 ARG A 16 0.19 SIDE CHAIN
REMARK 500 4 ARG A 28 0.26 SIDE CHAIN
REMARK 500 4 ARG A 39 0.29 SIDE CHAIN
REMARK 500 5 ARG A 8 0.30 SIDE CHAIN
REMARK 500 5 ARG A 16 0.24 SIDE CHAIN
REMARK 500 5 ARG A 28 0.14 SIDE CHAIN
REMARK 500 5 ARG A 39 0.17 SIDE CHAIN
REMARK 500 6 ARG A 8 0.31 SIDE CHAIN
REMARK 500 6 ARG A 16 0.32 SIDE CHAIN
REMARK 500 6 ARG A 28 0.32 SIDE CHAIN
REMARK 500 6 ARG A 39 0.27 SIDE CHAIN
REMARK 500 7 ARG A 8 0.30 SIDE CHAIN
REMARK 500 7 ARG A 16 0.26 SIDE CHAIN
REMARK 500 7 ARG A 28 0.33 SIDE CHAIN
REMARK 500 7 ARG A 39 0.28 SIDE CHAIN
REMARK 500 8 ARG A 8 0.26 SIDE CHAIN
REMARK 500 8 ARG A 16 0.32 SIDE CHAIN
REMARK 500 8 ARG A 28 0.26 SIDE CHAIN
REMARK 500 8 ARG A 39 0.25 SIDE CHAIN
REMARK 500 9 ARG A 8 0.30 SIDE CHAIN
REMARK 500 9 ARG A 16 0.27 SIDE CHAIN
REMARK 500 9 ARG A 28 0.32 SIDE CHAIN
REMARK 500 9 ARG A 39 0.30 SIDE CHAIN
REMARK 500 10 ARG A 8 0.30 SIDE CHAIN
REMARK 500 10 ARG A 16 0.30 SIDE CHAIN
REMARK 500 10 ARG A 28 0.23 SIDE CHAIN
REMARK 500 10 ARG A 39 0.31 SIDE CHAIN
REMARK 500 11 ARG A 8 0.20 SIDE CHAIN
REMARK 500 11 ARG A 16 0.31 SIDE CHAIN
REMARK 500 11 ARG A 39 0.32 SIDE CHAIN
REMARK 500 12 ARG A 8 0.24 SIDE CHAIN
REMARK 500 12 ARG A 16 0.23 SIDE CHAIN
REMARK 500 12 ARG A 28 0.19 SIDE CHAIN
REMARK 500 12 TYR A 35 0.06 SIDE CHAIN
REMARK 500 12 ARG A 39 0.29 SIDE CHAIN
REMARK 500 13 ARG A 8 0.31 SIDE CHAIN
REMARK 500 13 ARG A 16 0.23 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 81 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EGR A 1 85 UNP P68688 GLRX1_ECOLI 1 85
SEQRES 1 A 85 MET GLN THR VAL ILE PHE GLY ARG SER GLY CYS PRO TYR
SEQRES 2 A 85 CYS 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
HELIX 1 H1 TYR A 13 ARG A 28 1ALPHA HELIX 16
HELIX 2 H2 THR A 44 GLY A 53 1ALPHA HELIX 10
HELIX 3 H3 GLY A 71 LEU A 83 1ALPHA HELIX 13
SHEET 1 S1 4 GLN A 32 ASP A 37 0
SHEET 2 S1 4 GLN A 2 GLY A 7 1 N ILE A 5 O GLN A 34
SHEET 3 S1 4 GLN A 61 VAL A 64 -1 N PHE A 63 O VAL A 4
SHEET 4 S1 4 GLN A 67 ILE A 69 -1 N ILE A 69 O ILE A 62
CISPEP 1 VAL A 59 PRO A 60 1 -7.27
CISPEP 2 VAL A 59 PRO A 60 2 -18.26
CISPEP 3 VAL A 59 PRO A 60 3 -11.45
CISPEP 4 VAL A 59 PRO A 60 4 -6.89
CISPEP 5 VAL A 59 PRO A 60 5 10.99
CISPEP 6 VAL A 59 PRO A 60 6 -7.86
CISPEP 7 VAL A 59 PRO A 60 7 17.09
CISPEP 8 VAL A 59 PRO A 60 8 -18.58
CISPEP 9 VAL A 59 PRO A 60 9 7.90
CISPEP 10 VAL A 59 PRO A 60 10 -25.67
CISPEP 11 VAL A 59 PRO A 60 11 0.13
CISPEP 12 VAL A 59 PRO A 60 12 -28.58
CISPEP 13 VAL A 59 PRO A 60 13 9.94
CISPEP 14 VAL A 59 PRO A 60 14 -20.23
CISPEP 15 VAL A 59 PRO A 60 15 2.41
CISPEP 16 VAL A 59 PRO A 60 16 -0.18
CISPEP 17 VAL A 59 PRO A 60 17 2.58
CISPEP 18 VAL A 59 PRO A 60 18 -8.95
CISPEP 19 VAL A 59 PRO A 60 19 -5.86
CISPEP 20 VAL A 59 PRO A 60 20 -9.29
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
