Header list of 1quz.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 05-JUL-99 1QUZ
TITLE SOLUTION STRUCTURE OF THE POTASSIUM CHANNEL SCORPION TOXIN HSTX1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HSTX1 TOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE CHEMICAL SYNTHESIS USING THE FMOC
SOURCE 4 METHODOLOGY. THE SEQUENCE OF THIS PEPTIDE OCCURS NATURALLY IN
SOURCE 5 SCORPIONS (SCORPIONIDAE).
KEYWDS SCORPION TOXIN, ALPHA BETA, MOLECULAR MODELING, POTASSIUM CHANNEL,
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.SAVARIN,R.ROMI-LEBRUN,S.ZINN-JUSTIN,B.LEBRUN,T.NAKAJIMA,B.GILQUIN,
AUTHOR 2 A.MENEZ
REVDAT 4 02-MAR-22 1QUZ 1 REMARK LINK
REVDAT 3 24-FEB-09 1QUZ 1 VERSN
REVDAT 2 20-DEC-05 1QUZ 3 JRNL REMARK ATOM
REVDAT 1 07-JUL-00 1QUZ 0
JRNL AUTH P.SAVARIN,R.ROMI-LEBRUN,S.ZINN-JUSTIN,B.LEBRUN,T.NAKAJIMA,
JRNL AUTH 2 B.GILQUIN,A.MENEZ
JRNL TITL STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF THE PRESENCE OF A
JRNL TITL 2 FOURTH DISULFIDE BRIDGE IN THE SCORPION SHORT TOXINS:
JRNL TITL 3 SOLUTION STRUCTURE OF THE POTASSIUM CHANNEL INHIBITOR HSTX1.
JRNL REF PROTEIN SCI. V. 8 2672 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10631983
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.LEBRUN,R.ROMI-LEBRUN,M.F.MARTIN-EAUCLAIRE,A.YASUDA,
REMARK 1 AUTH 2 M.ISHIGURO,Y.OYAMA,O.PONGS,T.NAKAJIMA
REMARK 1 TITL A FOUR-DISULFIDE-BRIDGED TOXIN, WITH HIGH AFFINITY TOWARDS
REMARK 1 TITL 2 VOLTAGE-GATEDC K+ CHANNELS, ISOLATED FROM HETEROMETRUS
REMARK 1 TITL 3 SPINNIFER (SCORPIONIDAE) VENOM
REMARK 1 REF BIOCHEM.J. V. 328 321 1997
REMARK 1 REFN ISSN 0264-6021
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.ROCHAT,R.KHARRAT,J.M.SABATIER,P.MANSUELLE,M.CREST,
REMARK 1 AUTH 2 M.F.MARTIN-EAUCLAIRE,F.SAMPIERI,R.OUGHIDENI,K.MABROUK,
REMARK 1 AUTH 3 G.JACQUET,J.VAN RIETSCHOTEN,M.EL AYEB
REMARK 1 TITL MAUROTOXIN, A FOUR DISULFIDE BRIDGES SCORPION TOXIN ACTING
REMARK 1 TITL 2 ON K+ CHANNELS.
REMARK 1 REF TOXICON V. 36 1609 1998
REMARK 1 REFN ISSN 0041-0101
REMARK 1 DOI 10.1016/S0041-0101(98)00153-6
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.ROMI-LEBRUN,B.LEBRUN,M.F.MARTIN-EAUCLAIRE,M.ISHIGURO,
REMARK 1 AUTH 2 P.ESCOUBAS,F.Q.WU,M.HISADA,O.PONGS,T.NAKAJIMA
REMARK 1 TITL PURIFICATION, CHARACTERIZATION, AND SYNTHESIS OF THREE NOVEL
REMARK 1 TITL 2 TOXINS FROM THE CHINESE SCORPION BUTHUS MARTENSI, WHICH ACT
REMARK 1 TITL 3 ON K+ CHANNELS
REMARK 1 REF BIOCHEMISTRY V. 36 13473 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI971044W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97, X-PLOR 3.1
REMARK 3 AUTHORS : BIOSYM (FELIX), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QUZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000009290.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5 MG HSTX1; TSP; HCL FOR PH; 5
REMARK 210 MG HSTX1; TSP; DCL FOR PD
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; OFF
REMARK 210 -RESONANCE ROESY (35)
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : A COMPLETLY EXTENDED
REMARK 210 CONFORMATION WAS USED AS THE
REMARK 210 STARTING STRUCTURE. 25
REMARK 210 ITERATIONS WERE MADE. 500
REMARK 210 STRUCTURES WERE CALCULATED.
REMARK 210 RESTRAINED MOLECULAR DYNAMICS AT
REMARK 210 600K A SLOW COOLING.
REMARK 210 MINIMIZATION WERE MADE WITH AN
REMARK 210 ELECTROSTATIC TERM
REMARK 210 TOPALLH22X.PRO AND PARALLH22X.PRO
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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: 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 HG1 THR A 17 O ASN A 32 1.57
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 4 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 TYR A 21 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 TYR A 21 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 ARG A 27 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 TYR A 21 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 TYR A 21 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 ARG A 4 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 TYR A 21 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 TYR A 21 CB - CG - CD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 3 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 TYR A 21 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 5 TYR A 21 CB - CG - CD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 5 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 6 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 6 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 6 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 7 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 8 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 8 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 CYS A 13 CA - CB - SG ANGL. DEV. = 8.4 DEGREES
REMARK 500 9 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 9 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 9 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 10 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 TYR A 21 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 13 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 13 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 14 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 14 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 15 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 15 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 17 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 63 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 PRO A 20 56.59 -91.86
REMARK 500 2 PRO A 20 48.81 -73.67
REMARK 500 2 ASN A 26 100.92 77.84
REMARK 500 2 ARG A 27 -2.19 75.15
REMARK 500 3 ARG A 4 -56.91 -125.79
REMARK 500 3 PRO A 20 42.88 -76.59
REMARK 500 3 ARG A 27 13.24 84.10
REMARK 500 4 THR A 17 -60.72 -107.62
REMARK 500 4 TYR A 21 65.14 -109.92
REMARK 500 4 ARG A 27 12.59 80.92
REMARK 500 5 ARG A 4 -54.47 -128.69
REMARK 500 5 PRO A 20 31.24 -66.73
REMARK 500 5 ARG A 27 7.38 84.76
REMARK 500 6 ASN A 26 84.82 74.14
REMARK 500 6 ASN A 32 -159.43 -119.82
REMARK 500 7 ARG A 4 -59.42 -120.41
REMARK 500 7 THR A 17 -91.20 -101.91
REMARK 500 7 TYR A 21 55.40 -110.84
REMARK 500 7 ASN A 32 -151.58 -105.09
REMARK 500 8 ARG A 4 -60.93 -125.76
REMARK 500 8 CYS A 9 45.11 -90.22
REMARK 500 8 ARG A 27 14.41 83.05
REMARK 500 9 THR A 17 47.17 -144.61
REMARK 500 9 MET A 25 50.38 -105.55
REMARK 500 9 ASN A 26 79.29 83.26
REMARK 500 9 ARG A 27 -9.52 64.19
REMARK 500 10 ARG A 4 -59.34 -142.88
REMARK 500 10 THR A 17 47.84 -142.61
REMARK 500 10 MET A 25 71.83 -106.59
REMARK 500 10 ARG A 27 3.00 87.13
REMARK 500 11 THR A 17 -93.18 -97.04
REMARK 500 11 TYR A 21 56.13 -110.92
REMARK 500 11 MET A 25 47.43 -97.36
REMARK 500 11 ASN A 26 104.09 81.26
REMARK 500 11 ARG A 27 -30.15 72.80
REMARK 500 12 ASN A 26 86.69 78.59
REMARK 500 13 CYS A 9 46.02 -109.26
REMARK 500 13 ALA A 10 -66.00 -91.53
REMARK 500 13 PRO A 20 45.38 -89.81
REMARK 500 13 ARG A 27 7.74 80.75
REMARK 500 14 PRO A 20 39.16 -93.72
REMARK 500 14 MET A 25 55.86 -117.85
REMARK 500 14 ASN A 26 90.10 85.79
REMARK 500 14 ARG A 27 -9.10 62.56
REMARK 500 15 ARG A 4 -56.79 -132.78
REMARK 500 15 ARG A 27 -7.92 90.38
REMARK 500 16 ARG A 4 -58.32 -126.00
REMARK 500 16 PRO A 20 44.13 -76.76
REMARK 500 16 ARG A 27 1.23 84.74
REMARK 500 17 ARG A 4 -64.71 -131.73
REMARK 500
REMARK 500 THIS ENTRY HAS 61 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 ARG A 33 0.09 SIDE CHAIN
REMARK 500 2 ARG A 14 0.17 SIDE CHAIN
REMARK 500 7 ARG A 14 0.20 SIDE CHAIN
REMARK 500 10 ARG A 14 0.16 SIDE CHAIN
REMARK 500 10 ARG A 27 0.09 SIDE CHAIN
REMARK 500 11 ARG A 27 0.10 SIDE CHAIN
REMARK 500 11 ARG A 33 0.08 SIDE CHAIN
REMARK 500 13 ARG A 33 0.14 SIDE CHAIN
REMARK 500 14 ARG A 14 0.10 SIDE CHAIN
REMARK 500 17 ARG A 27 0.09 SIDE CHAIN
REMARK 500 17 ARG A 33 0.08 SIDE CHAIN
REMARK 500 19 ARG A 14 0.24 SIDE CHAIN
REMARK 500 20 ARG A 33 0.15 SIDE CHAIN
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 35
DBREF 1QUZ A 1 34 UNP P59867 SCK1_HETSP 1 34
SEQRES 1 A 35 ALA SER CYS ARG THR PRO LYS ASP CYS ALA ASP PRO CYS
SEQRES 2 A 35 ARG LYS GLU THR GLY CYS PRO TYR GLY LYS CYS MET ASN
SEQRES 3 A 35 ARG LYS CYS LYS CYS ASN ARG CYS NH2
HET NH2 A 35 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 THR A 5 ASP A 8 5 4
HELIX 2 2 CYS A 9 THR A 17 1 9
SHEET 1 A 2 GLY A 22 CYS A 24 0
SHEET 2 A 2 CYS A 29 CYS A 31 -1 N LYS A 30 O LYS A 23
SSBOND 1 CYS A 3 CYS A 24 1555 1555 2.03
SSBOND 2 CYS A 9 CYS A 29 1555 1555 2.04
SSBOND 3 CYS A 13 CYS A 31 1555 1555 2.03
SSBOND 4 CYS A 19 CYS A 34 1555 1555 2.02
LINK C CYS A 34 N NH2 A 35 1555 1555 1.35
SITE 1 AC1 2 ARG A 33 CYS A 34
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 - 2 20 Bytes