Header list of 1kfp.pdb file
Complete list - 25 20 Bytes
HEADER ANTIBIOTIC 22-NOV-01 1KFP
TITLE SOLUTION STRUCTURE OF THE ANTIMICROBIAL 18-RESIDUE GOMESIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GOMESIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: ACANTHOSCURRIA GOMESIANA;
SOURCE 4 ORGANISM_COMMON: MYGALOMORPHAE SPIDER;
SOURCE 5 ORGANISM_TAXID: 115339
KEYWDS HAIRPIN-LIKE, BETA-SHEET, DISULFIDE BRIDGES, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.MANDARD,P.BULET,A.CAILLE,S.DAFFRE,F.VOVELLE
REVDAT 4 25-DEC-19 1KFP 1 SOURCE REMARK SEQADV SEQRES
REVDAT 4 2 1 LINK
REVDAT 3 24-FEB-09 1KFP 1 VERSN
REVDAT 2 04-DEC-02 1KFP 1 REMARK
REVDAT 1 10-APR-02 1KFP 0
JRNL AUTH N.MANDARD,P.BULET,A.CAILLE,S.DAFFRE,F.VOVELLE
JRNL TITL THE SOLUTION STRUCTURE OF GOMESIN, AN ANTIMICROBIAL
JRNL TITL 2 CYSTEINE-RICH PEPTIDE FROM THE SPIDER.
JRNL REF EUR.J.BIOCHEM. V. 269 1190 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11856345
JRNL DOI 10.1046/J.0014-2956.2002.02760.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.I.SILVA,S.DAFFRE,P.BULET
REMARK 1 TITL ISOLATION AND CHARACTERIZATION OF GOMESIN, AN 18-RESIDUE
REMARK 1 TITL 2 CYSTEINE-RICH DEFENSE PEPTIDE FROM THE SPIDER ACANTHOSCURRIA
REMARK 1 TITL 3 GOMESIANA HEMOCYTES WITH SEQUENCE SIMILARITIES TO HORSESHOE
REMARK 1 TITL 4 CRAB ANTIMICROBIAL PEPTIDES OF THE TACHYPLESIN FAMILY
REMARK 1 REF J.BIOL.CHEM. V. 275 33464 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M001491200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, X-PLOR 3.1
REMARK 3 AUTHORS : GUENTERT (DYANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 20 STRUCTURES ARE BASED ON A TOTAL OF 289 RESTRAINTS, 279 ARE
REMARK 3 NOE-DERIVED DISTANCE CONSTRAINTS, 4 ARE USED FOR HYDROGEN BONDS
REMARK 3 MODELLING AND 6 (I.E. 2X3) ARE USED FOR DISULFIDE BRIDGE MODELLING.
REMARK 3 NO DIHEDRAL ANGLE RESTRAINTS USED.
REMARK 4
REMARK 4 1KFP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014907.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278; 285
REMARK 210 PH : 3.5; 3.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3.3MM GOMESIN; 3.3MM GOMESIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; CLEAN-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS SOLUTION 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: 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 2 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 ARG A 4 NH1 - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 2 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 ARG A 4 NH1 - CZ - NH2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 3 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 3 TYR A 7 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 TYR A 14 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 4 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 5 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 6 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 6 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 6 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 6 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 6 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 7 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 8 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 9 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 9 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 9 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 9 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 10 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 10 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 10 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 11 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 11 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 11 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 12 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 13 ARG A 4 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 13 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 13 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 14 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 14 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 15 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 15 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 15 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 16 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 16 ARG A 4 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 16 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 16 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 17 CYS A 2 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 17 ARG A 3 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 61 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 LYS A 8 25.59 25.14
REMARK 500 1 GLN A 9 -47.03 -175.34
REMARK 500 2 LYS A 8 18.82 39.93
REMARK 500 2 GLN A 9 -47.65 -170.27
REMARK 500 3 TYR A 7 57.40 -102.15
REMARK 500 3 LYS A 8 -47.45 67.98
REMARK 500 4 LYS A 8 11.24 41.03
REMARK 500 4 GLN A 9 -51.97 -158.35
REMARK 500 5 LYS A 8 13.98 36.87
REMARK 500 5 GLN A 9 -53.73 -157.07
REMARK 500 6 TYR A 7 78.32 -101.91
REMARK 500 6 LYS A 8 34.98 18.68
REMARK 500 6 GLN A 9 -40.10 178.04
REMARK 500 7 TYR A 7 79.24 -102.98
REMARK 500 7 LYS A 8 40.52 16.41
REMARK 500 7 GLN A 9 -39.32 172.19
REMARK 500 8 LYS A 8 9.77 39.54
REMARK 500 8 GLN A 9 -52.84 -144.81
REMARK 500 9 LYS A 8 14.57 43.29
REMARK 500 9 GLN A 9 -55.49 -161.58
REMARK 500 10 TYR A 7 65.28 -101.30
REMARK 500 10 LYS A 8 12.85 38.68
REMARK 500 10 GLN A 9 -51.83 -149.59
REMARK 500 11 LYS A 8 73.76 21.99
REMARK 500 11 GLN A 9 -55.12 129.05
REMARK 500 12 TYR A 7 61.76 -106.78
REMARK 500 12 LYS A 8 42.75 30.43
REMARK 500 12 GLN A 9 -64.12 -176.64
REMARK 500 13 TYR A 7 74.47 -101.06
REMARK 500 13 LYS A 8 23.62 41.81
REMARK 500 13 GLN A 9 -50.62 -173.77
REMARK 500 14 LYS A 8 76.88 0.72
REMARK 500 14 GLN A 9 -46.87 148.62
REMARK 500 15 LYS A 8 7.58 37.66
REMARK 500 15 GLN A 9 -45.98 -157.30
REMARK 500 16 LYS A 8 -67.66 68.10
REMARK 500 16 GLN A 9 -10.28 -141.49
REMARK 500 17 LYS A 8 44.73 17.50
REMARK 500 17 GLN A 9 -53.06 170.55
REMARK 500 18 LYS A 8 13.92 35.11
REMARK 500 18 GLN A 9 -47.53 -168.38
REMARK 500 19 LYS A 8 51.03 32.04
REMARK 500 19 GLN A 9 -62.55 169.81
REMARK 500 20 LYS A 8 -62.22 69.25
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 3 0.23 SIDE CHAIN
REMARK 500 1 ARG A 4 0.31 SIDE CHAIN
REMARK 500 1 ARG A 10 0.32 SIDE CHAIN
REMARK 500 1 ARG A 16 0.31 SIDE CHAIN
REMARK 500 1 ARG A 18 0.30 SIDE CHAIN
REMARK 500 2 ARG A 3 0.30 SIDE CHAIN
REMARK 500 2 ARG A 4 0.28 SIDE CHAIN
REMARK 500 2 ARG A 10 0.31 SIDE CHAIN
REMARK 500 2 ARG A 16 0.30 SIDE CHAIN
REMARK 500 2 ARG A 18 0.16 SIDE CHAIN
REMARK 500 3 ARG A 3 0.30 SIDE CHAIN
REMARK 500 3 ARG A 4 0.29 SIDE CHAIN
REMARK 500 3 ARG A 10 0.31 SIDE CHAIN
REMARK 500 3 ARG A 16 0.24 SIDE CHAIN
REMARK 500 3 ARG A 18 0.32 SIDE CHAIN
REMARK 500 4 ARG A 3 0.31 SIDE CHAIN
REMARK 500 4 ARG A 4 0.29 SIDE CHAIN
REMARK 500 4 ARG A 10 0.31 SIDE CHAIN
REMARK 500 4 ARG A 16 0.32 SIDE CHAIN
REMARK 500 4 ARG A 18 0.32 SIDE CHAIN
REMARK 500 5 ARG A 3 0.27 SIDE CHAIN
REMARK 500 5 ARG A 4 0.31 SIDE CHAIN
REMARK 500 5 ARG A 10 0.11 SIDE CHAIN
REMARK 500 5 ARG A 16 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.32 SIDE CHAIN
REMARK 500 6 ARG A 3 0.33 SIDE CHAIN
REMARK 500 6 ARG A 4 0.30 SIDE CHAIN
REMARK 500 6 ARG A 10 0.28 SIDE CHAIN
REMARK 500 6 ARG A 16 0.25 SIDE CHAIN
REMARK 500 6 ARG A 18 0.30 SIDE CHAIN
REMARK 500 7 ARG A 3 0.30 SIDE CHAIN
REMARK 500 7 ARG A 4 0.30 SIDE CHAIN
REMARK 500 7 ARG A 10 0.21 SIDE CHAIN
REMARK 500 7 ARG A 16 0.27 SIDE CHAIN
REMARK 500 7 ARG A 18 0.30 SIDE CHAIN
REMARK 500 8 ARG A 3 0.12 SIDE CHAIN
REMARK 500 8 ARG A 4 0.29 SIDE CHAIN
REMARK 500 8 ARG A 10 0.20 SIDE CHAIN
REMARK 500 8 ARG A 16 0.31 SIDE CHAIN
REMARK 500 8 ARG A 18 0.30 SIDE CHAIN
REMARK 500 9 ARG A 3 0.21 SIDE CHAIN
REMARK 500 9 ARG A 4 0.31 SIDE CHAIN
REMARK 500 9 ARG A 16 0.24 SIDE CHAIN
REMARK 500 9 ARG A 18 0.29 SIDE CHAIN
REMARK 500 10 ARG A 3 0.25 SIDE CHAIN
REMARK 500 10 ARG A 4 0.31 SIDE CHAIN
REMARK 500 10 ARG A 10 0.32 SIDE CHAIN
REMARK 500 10 ARG A 16 0.32 SIDE CHAIN
REMARK 500 10 ARG A 18 0.28 SIDE CHAIN
REMARK 500 11 ARG A 3 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 99 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 19
DBREF 1KFP A 1 18 UNP P82358 GOME_ACAGO 1 18
SEQRES 1 A 19 PCA CYS ARG ARG LEU CYS TYR LYS GLN ARG CYS VAL THR
SEQRES 2 A 19 TYR CYS ARG GLY ARG NH2
MODRES 1KFP PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HET NH2 A 19 3
HETNAM PCA PYROGLUTAMIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 PCA C5 H7 N O3
FORMUL 1 NH2 H2 N
SHEET 1 A 2 CYS A 2 TYR A 7 0
SHEET 2 A 2 ARG A 10 CYS A 15 -1 O VAL A 12 N LEU A 5
SSBOND 1 CYS A 2 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 11 1555 1555 2.02
LINK C PCA A 1 N CYS A 2 1555 1555 1.29
LINK C ARG A 18 N NH2 A 19 1555 1555 1.30
SITE 1 AC1 1 ARG A 18
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 - 25 20 Bytes