Header list of 1ews.pdb file
Complete list - 16 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 26-APR-00 1EWS
TITLE THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY
TITLE 2 DEFENSIN, RK-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RK-1 DEFENSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-DEFISIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 ORGAN: KIDNEY
KEYWDS ALPHA DEFENSIN, TRIPLE-STRANDED BETA-SHEET, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.MCMANUS,N.F.DAWSON,J.D.WADE,D.J.CRAIK
REVDAT 4 16-FEB-22 1EWS 1 REMARK
REVDAT 3 24-FEB-09 1EWS 1 VERSN
REVDAT 2 01-APR-03 1EWS 1 JRNL
REVDAT 1 02-MAY-01 1EWS 0
JRNL AUTH A.M.MCMANUS,N.F.DAWSON,J.D.WADE,L.E.CARRINGTON,D.J.WINZOR,
JRNL AUTH 2 D.J.CRAIK
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF RK-1: A NOVEL ALPHA-DEFENSIN
JRNL TITL 2 PEPTIDE.
JRNL REF BIOCHEMISTRY V. 39 15757 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11123900
JRNL DOI 10.1021/BI000457L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.F.DAWSON,D.J.CRAIK,A.M.MCMANUS,S.G.DASHPER,E.G.REYNOLDS,
REMARK 1 AUTH 2 G.W.TREGEAR,L.OTVOS,J.D.WADE
REMARK 1 TITL CHEMICAL SYNTHESIS, CHARACTERIZATION AND ACTIVITY OF RK-1, A
REMARK 1 TITL 2 NOVEL ALPHA-DEFENSIN-RELATED PEPTIDE
REMARK 1 REF J.PEPT.SCI. V. 6 19 2000
REMARK 1 REFN ISSN 1075-2617
REMARK 1 DOI 10.1002/(SICI)1099-1387(200001)6:1<19::AID-PSC230>3.3.CO;2-T
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 509 DISTANCE RESTRAINTS
REMARK 3 CONSISTING OF
REMARK 3 498 NOE-DERIVED DISTANCE RESTRAINTS, 11 RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS AND
REMARK 3 31 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1EWS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000010973.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308; 308
REMARK 210 PH : 3.5; 3.5; 3.5
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM RK1; 1.5 MM RK1; 1.5 MM
REMARK 210 RK1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : ARX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-EASY 1.3.7, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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
REMARK 500 REMARK: NULL
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 20 MET A 1 N MET A 1 CA -0.969
REMARK 500 20 MET A 1 CA MET A 1 CB -1.353
REMARK 500 20 MET A 1 CB MET A 1 CG -1.309
REMARK 500 20 MET A 1 CG MET A 1 SD -1.717
REMARK 500 20 MET A 1 SD MET A 1 CE -1.607
REMARK 500 20 MET A 1 CA MET A 1 C -0.852
REMARK 500 20 MET A 1 C MET A 1 O -0.605
REMARK 500 20 MET A 1 C PRO A 2 N -1.127
REMARK 500 20 PRO A 2 N PRO A 2 CA -0.843
REMARK 500 20 PRO A 2 CA PRO A 2 CB -0.942
REMARK 500 20 PRO A 2 CB PRO A 2 CG -0.727
REMARK 500 20 PRO A 2 CG PRO A 2 CD -1.306
REMARK 500 20 PRO A 2 CD PRO A 2 N -0.704
REMARK 500 20 PRO A 2 C PRO A 2 O -0.128
REMARK 500 20 PRO A 2 C CYS A 3 N -0.159
REMARK 500 20 CYS A 3 CA CYS A 3 CB -0.092
REMARK 500 20 CYS A 3 CB CYS A 3 SG -0.314
REMARK 500 20 CYS A 3 C CYS A 3 O -0.126
REMARK 500 20 SER A 4 CB SER A 4 OG -0.959
REMARK 500 20 LYS A 6 CG LYS A 6 CD -0.684
REMARK 500 20 LYS A 6 CD LYS A 6 CE -0.753
REMARK 500 20 LYS A 6 CE LYS A 6 NZ -1.033
REMARK 500 20 LYS A 7 CB LYS A 7 CG -0.639
REMARK 500 20 LYS A 7 CG LYS A 7 CD -0.864
REMARK 500 20 LYS A 7 CD LYS A 7 CE -0.649
REMARK 500 20 LYS A 7 CE LYS A 7 NZ -0.971
REMARK 500 20 TYR A 8 CB TYR A 8 CG -0.843
REMARK 500 20 TYR A 8 CG TYR A 8 CD2 -0.809
REMARK 500 20 TYR A 8 CG TYR A 8 CD1 -1.294
REMARK 500 20 TYR A 8 CD1 TYR A 8 CE1 -0.788
REMARK 500 20 TYR A 8 CE1 TYR A 8 CZ -0.805
REMARK 500 20 TYR A 8 CZ TYR A 8 OH -0.774
REMARK 500 20 TYR A 8 CZ TYR A 8 CE2 -1.289
REMARK 500 20 TYR A 8 CE2 TYR A 8 CD2 -0.788
REMARK 500 20 TYR A 8 C TYR A 8 O -0.118
REMARK 500 20 ASP A 10 CG ASP A 10 OD1 -0.680
REMARK 500 20 ASP A 10 CG ASP A 10 OD2 -0.673
REMARK 500 20 TRP A 12 CG TRP A 12 CD2 -0.136
REMARK 500 20 TRP A 12 CD1 TRP A 12 NE1 -0.129
REMARK 500 20 TRP A 12 NE1 TRP A 12 CE2 -0.123
REMARK 500 20 TRP A 12 CE2 TRP A 12 CD2 -0.082
REMARK 500 20 GLU A 13 CG GLU A 13 CD -0.338
REMARK 500 20 GLU A 13 CD GLU A 13 OE1 -0.874
REMARK 500 20 GLU A 13 CD GLU A 13 OE2 -0.595
REMARK 500 20 VAL A 14 CB VAL A 14 CG1 -0.619
REMARK 500 20 VAL A 14 CB VAL A 14 CG2 -0.865
REMARK 500 20 ASP A 16 CB ASP A 16 CG -0.440
REMARK 500 20 ASP A 16 CG ASP A 16 OD1 -0.784
REMARK 500 20 ASP A 16 CG ASP A 16 OD2 -0.940
REMARK 500 20 SER A 18 CB SER A 18 OG -0.636
REMARK 500
REMARK 500 THIS ENTRY HAS 96 BOND DEVIATIONS.
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 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 3 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 5 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 6 CYS A 9 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 6 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 7 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 8 CYS A 9 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 8 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 8 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 9 CYS A 9 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 9 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 10 CYS A 9 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 10 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 11 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 12 CYS A 9 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 12 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 13 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 14 CYS A 9 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 14 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 15 CYS A 9 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 15 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 CYS A 9 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 16 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 CYS A 29 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 17 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 18 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 19 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 19 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 20 MET A 1 CB - CA - C ANGL. DEV. = -79.7 DEGREES
REMARK 500 20 MET A 1 N - CA - CB ANGL. DEV. = 39.0 DEGREES
REMARK 500 20 MET A 1 CA - CB - CG ANGL. DEV. = -58.2 DEGREES
REMARK 500 20 MET A 1 CB - CG - SD ANGL. DEV. = -54.9 DEGREES
REMARK 500 20 MET A 1 CG - SD - CE ANGL. DEV. = -23.0 DEGREES
REMARK 500 20 MET A 1 N - CA - C ANGL. DEV. = 68.0 DEGREES
REMARK 500 20 MET A 1 CA - C - O ANGL. DEV. = 44.8 DEGREES
REMARK 500 20 MET A 1 CA - C - N ANGL. DEV. = -58.2 DEGREES
REMARK 500 20 MET A 1 O - C - N ANGL. DEV. = 15.1 DEGREES
REMARK 500 20 PRO A 2 C - N - CA ANGL. DEV. = -59.3 DEGREES
REMARK 500 20 PRO A 2 CA - N - CD ANGL. DEV. = 51.3 DEGREES
REMARK 500 20 PRO A 2 CB - CA - C ANGL. DEV. = 48.9 DEGREES
REMARK 500 20 PRO A 2 N - CA - CB ANGL. DEV. = -75.8 DEGREES
REMARK 500 20 PRO A 2 CA - CB - CG ANGL. DEV. = 56.6 DEGREES
REMARK 500 20 PRO A 2 N - CD - CG ANGL. DEV. = -21.6 DEGREES
REMARK 500 20 PRO A 2 N - CA - C ANGL. DEV. = 51.7 DEGREES
REMARK 500 20 CYS A 3 CA - CB - SG ANGL. DEV. = 11.9 DEGREES
REMARK 500 20 SER A 4 CA - CB - OG ANGL. DEV. = 29.5 DEGREES
REMARK 500 20 LYS A 6 CB - CG - CD ANGL. DEV. = 18.9 DEGREES
REMARK 500 20 LYS A 6 CG - CD - CE ANGL. DEV. = 58.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 128 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 ASP A 16 -18.02 -150.21
REMARK 500 1 PHE A 22 36.42 -90.49
REMARK 500 2 PRO A 2 96.68 -66.00
REMARK 500 2 CYS A 3 -144.49 -143.11
REMARK 500 2 TYR A 8 -148.12 -134.06
REMARK 500 2 ASP A 16 -14.30 -147.07
REMARK 500 2 LEU A 21 -99.99 -89.75
REMARK 500 2 ASN A 23 19.45 57.96
REMARK 500 2 GLU A 31 -53.85 -144.69
REMARK 500 3 TYR A 8 -132.66 -147.42
REMARK 500 3 ASP A 16 -20.97 -148.99
REMARK 500 3 LEU A 21 -113.56 -89.80
REMARK 500 3 ASN A 23 20.97 43.03
REMARK 500 4 ASP A 16 -13.81 -147.24
REMARK 500 4 LEU A 21 -113.01 -89.69
REMARK 500 4 ASN A 23 29.02 41.96
REMARK 500 5 TYR A 8 -122.58 -122.13
REMARK 500 5 ASP A 16 -85.75 -143.03
REMARK 500 5 LEU A 21 -75.98 -90.04
REMARK 500 5 PHE A 22 58.29 -90.30
REMARK 500 5 ASN A 23 26.44 45.44
REMARK 500 6 LEU A 21 -118.84 -89.72
REMARK 500 6 ASN A 23 26.04 42.01
REMARK 500 7 CYS A 3 -160.65 -111.35
REMARK 500 7 ASP A 16 -14.48 -149.36
REMARK 500 7 LEU A 21 -102.96 -89.69
REMARK 500 7 ASN A 23 12.75 57.65
REMARK 500 8 ASP A 16 -55.21 -143.20
REMARK 500 8 LEU A 21 -94.92 -89.72
REMARK 500 9 LEU A 21 -98.36 -89.80
REMARK 500 10 TYR A 8 -155.72 -150.32
REMARK 500 10 ILE A 15 153.55 -47.16
REMARK 500 10 ASP A 16 -22.68 -148.97
REMARK 500 10 LEU A 21 -97.27 -89.77
REMARK 500 10 ASN A 23 24.83 43.09
REMARK 500 11 ASP A 16 -21.32 -149.78
REMARK 500 11 CYS A 19 -168.90 -108.99
REMARK 500 11 LEU A 21 -102.12 -89.61
REMARK 500 11 ASN A 23 18.90 57.01
REMARK 500 12 ASP A 16 -20.08 -149.21
REMARK 500 12 LEU A 21 -98.05 -89.86
REMARK 500 12 ASN A 23 28.63 41.77
REMARK 500 13 ASP A 16 -14.48 -145.08
REMARK 500 13 LEU A 21 -98.18 -89.74
REMARK 500 13 ASN A 23 28.88 42.20
REMARK 500 14 ASP A 16 -24.79 -150.12
REMARK 500 14 LEU A 21 -120.03 -94.01
REMARK 500 14 ASN A 23 28.01 40.21
REMARK 500 14 ARG A 30 56.53 -99.09
REMARK 500 15 PRO A 2 89.32 -64.98
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EWS A 1 32 UNP P81655 RK1_RABIT 1 32
SEQRES 1 A 32 MET PRO CYS SER CYS LYS LYS TYR CYS ASP PRO TRP GLU
SEQRES 2 A 32 VAL ILE ASP GLY SER CYS GLY LEU PHE ASN SER LYS TYR
SEQRES 3 A 32 ILE CYS CYS ARG GLU LYS
SHEET 1 A 3 SER A 4 LYS A 6 0
SHEET 2 A 3 TYR A 26 ARG A 30 -1 O TYR A 26 N LYS A 6
SHEET 3 A 3 GLU A 13 GLY A 17 -1 N VAL A 14 O CYS A 29
SSBOND 1 CYS A 3 CYS A 29 1555 1555 2.02
SSBOND 2 CYS A 5 CYS A 19 1555 1555 2.02
SSBOND 3 CYS A 9 CYS A 28 1555 1555 2.01
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
Complete list - 16 20 Bytes