Header list of 1bmr.pdb file
Complete list - b 16 2 Bytes
HEADER TOXIN 24-JUL-98 1BMR
TITLE ALPHA-LIKE TOXIN LQH III FROM SCORPION LEIURUS QUINQUESTRIATUS
TITLE 2 HEBRAEUS, NMR, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LQH III ALPHA-LIKE TOXIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: AMIDATED AT THE C-TERMINAL POSITION (CONH2) . THIS
COMPND 5 STRUCTURE IS IN EQUILIBRIUM WITH THE PRO9-GLU10 CIS ISOMER
COMPND 6 (PDB:1FH3).
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEIURUS QUINQUESTRIATUS HEBRAEUS;
SOURCE 3 ORGANISM_TAXID: 6884;
SOURCE 4 STRAIN: HEBRAEUS;
SOURCE 5 ORGAN: VENOMOUS APPARATUS;
SOURCE 6 SECRETION: VENOM
KEYWDS ALPHA-LIKE TOXIN, SCORPION TOXIN, SODIUM CHANNEL INHIBITOR, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR I.KRIMM,N.GILLES,P.SAUTIERE,M.STANKIEWICZ,M.PELHATE,D.GORDON,J.-
AUTHOR 2 M.LANCELIN
REVDAT 5 16-FEB-22 1BMR 1 REMARK LINK
REVDAT 4 24-FEB-09 1BMR 1 VERSN
REVDAT 3 03-NOV-00 1BMR 1 COMPND
REVDAT 2 27-APR-99 1BMR 3 HET COMPND REMARK TITLE
REVDAT 2 2 3 HETATM DBREF SSBOND HEADER
REVDAT 2 3 3 TER LINK SOURCE SEQRES
REVDAT 2 4 3 ENDMDL FORMUL JRNL KEYWDS
REVDAT 2 5 3 HETSYN CONECT
REVDAT 1 16-FEB-99 1BMR 0
JRNL AUTH I.KRIMM,N.GILLES,P.SAUTIERE,M.STANKIEWICZ,M.PELHATE,
JRNL AUTH 2 D.GORDON,J.M.LANCELIN
JRNL TITL NMR STRUCTURES AND ACTIVITY OF A NOVEL ALPHA-LIKE TOXIN FROM
JRNL TITL 2 THE SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS.
JRNL REF J.MOL.BIOL. V. 285 1749 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 9917409
JRNL DOI 10.1006/JMBI.1998.2418
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.SAUTIERE,S.CESTELE,C.KOPEYAN,A.MARTINAGE,H.DROBECQ,
REMARK 1 AUTH 2 Y.DOLJANSKY,D.GORDON
REMARK 1 TITL NEW TOXINS ACTING ON SODIUM CHANNELS FROM THE SCORPION
REMARK 1 TITL 2 LEIURUS QUINQUESTRIATUS HEBRAEUS SUGGEST A CLUE TO MAMMALIAN
REMARK 1 TITL 3 VS INSECT SELECTIVITY
REMARK 1 REF TOXICON V. 36 1141 1998
REMARK 1 REFN ISSN 0041-0101
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.GORDON
REMARK 1 TITL SODIUM CHANNELS AS TARGETS FOR NEUROTOXINS. MODES OF ACTION
REMARK 1 TITL 2 AND INTERACTION OF NEUROTOXINS WITH RECEPTOR SITES ON SODIUM
REMARK 1 TITL 3 CHANNELS
REMARK 1 EDIT Y.GUTMAN, P.LAZAROVICI
REMARK 1 REF TOXINS AND SIGNAL 119 1997
REMARK 1 REF 2 TRANSDUCTION (IN: CELLULAR
REMARK 1 REF 3 AND MOLECULAR MECHANISMS OF
REMARK 1 REF 4 TOXIN ACTION, V.1)
REMARK 1 PUBL AMSTERDAM : HARWOOD ACADEMIC PUBLISHERS
REMARK 1 REFN ISSN 90-5702-078-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BMR 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_1000171918.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 311
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 100 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY TOCSY/HOHAHA NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE DRX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.2, BRUKER XWINNMR
REMARK 210 XWINNMR, X-PLOR 3.851
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY/
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TWO-DIMENSIONAL NMR ON
REMARK 210 A NATURAL UNLABELLED SAMPLE OF LQH III ALPHA LIKE TOXIN FROM THE
REMARK 210 SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS VENOM.
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 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 GLN A 8 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 1 GLY A 19 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 1 GLY A 35 N - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 1 VAL A 60 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 2 ASP A 3 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 2 GLY A 19 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 2 SER A 20 N - CA - CB ANGL. DEV. = 9.2 DEGREES
REMARK 500 2 GLY A 57 N - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 3 ASP A 3 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 3 ASN A 11 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 3 GLY A 19 N - CA - C ANGL. DEV. = -15.9 DEGREES
REMARK 500 3 GLY A 38 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 3 ALA A 51 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 4 GLY A 19 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 4 GLY A 38 N - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 4 GLY A 57 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 5 ASN A 11 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 5 HIS A 15 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 5 GLY A 57 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 6 PHE A 39 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 7 TYR A 14 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 7 GLY A 19 N - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 7 GLY A 62 N - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 7 CYS A 65 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 8 ASN A 11 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 8 CYS A 16 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 8 GLY A 19 N - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 9 GLY A 38 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 9 GLY A 57 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 10 ASP A 3 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 10 GLN A 8 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 10 ASN A 11 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 10 LYS A 40 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 10 LEU A 45 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 10 CYS A 65 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 11 TYR A 14 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500 11 CYS A 16 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 11 PHE A 17 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 11 GLY A 19 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 12 GLY A 19 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 12 GLY A 57 N - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 13 ASP A 3 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 13 ALA A 51 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 14 ASP A 3 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 14 CYS A 12 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 15 GLY A 42 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 15 GLY A 44 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 16 ASP A 3 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 16 TYR A 14 N - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 16 GLY A 19 N - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 79 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 ALA A 7 -150.98 -134.87
REMARK 500 1 GLU A 10 46.85 -86.37
REMARK 500 1 CYS A 12 -162.64 -122.38
REMARK 500 1 PRO A 18 96.47 -56.34
REMARK 500 1 HIS A 43 -69.85 -108.94
REMARK 500 1 ALA A 51 49.73 73.90
REMARK 500 1 ILE A 58 -144.25 -146.21
REMARK 500 1 GLU A 63 -144.80 -102.32
REMARK 500 2 ALA A 7 -159.19 -144.09
REMARK 500 2 ASN A 11 37.40 73.24
REMARK 500 2 CYS A 12 -162.33 -108.94
REMARK 500 2 SER A 20 -34.91 122.80
REMARK 500 2 HIS A 36 -154.51 -177.76
REMARK 500 2 HIS A 43 -71.67 -114.97
REMARK 500 2 ALA A 51 72.58 65.01
REMARK 500 2 ILE A 58 -140.64 -152.32
REMARK 500 2 GLU A 61 -54.80 62.41
REMARK 500 3 ALA A 7 -144.76 -94.30
REMARK 500 3 GLU A 10 -76.35 -88.40
REMARK 500 3 ASN A 11 144.02 -176.84
REMARK 500 3 CYS A 12 -153.48 160.69
REMARK 500 3 TYR A 14 -148.89 -86.01
REMARK 500 3 PRO A 18 103.82 -53.03
REMARK 500 3 HIS A 36 -153.04 -156.66
REMARK 500 3 HIS A 43 -64.71 -125.10
REMARK 500 3 ALA A 51 135.40 90.06
REMARK 500 3 ILE A 58 -153.81 -117.97
REMARK 500 3 GLU A 63 -169.40 -168.89
REMARK 500 4 ALA A 7 -128.61 -135.77
REMARK 500 4 PRO A 9 35.14 -74.89
REMARK 500 4 CYS A 12 -160.26 -116.89
REMARK 500 4 TYR A 14 -154.27 -96.62
REMARK 500 4 PRO A 18 98.69 -51.43
REMARK 500 4 SER A 21 -71.48 -39.59
REMARK 500 4 HIS A 36 -157.43 -155.86
REMARK 500 4 ALA A 51 54.94 77.02
REMARK 500 4 ILE A 58 -126.65 -139.66
REMARK 500 4 GLU A 61 -166.22 150.31
REMARK 500 4 GLU A 63 -47.44 69.54
REMARK 500 5 ALA A 7 -149.94 -109.59
REMARK 500 5 PRO A 9 29.81 -75.58
REMARK 500 5 GLU A 10 -78.74 -120.35
REMARK 500 5 CYS A 12 -157.09 173.42
REMARK 500 5 CYS A 16 -151.01 -160.45
REMARK 500 5 HIS A 43 -73.88 -117.48
REMARK 500 5 ALA A 51 47.67 77.36
REMARK 500 5 ILE A 58 -156.46 -146.81
REMARK 500 5 GLU A 61 -110.51 64.08
REMARK 500 5 GLU A 63 -71.40 -101.18
REMARK 500 6 ALA A 7 -161.44 -111.16
REMARK 500
REMARK 500 THIS ENTRY HAS 221 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 GLN A 8 PRO A 9 1 -143.16
REMARK 500 SER A 20 SER A 21 1 -145.30
REMARK 500 GLN A 8 PRO A 9 3 -145.17
REMARK 500 ALA A 51 LEU A 52 3 149.17
REMARK 500 GLN A 8 PRO A 9 5 -141.29
REMARK 500 GLN A 8 PRO A 9 6 -135.21
REMARK 500 GLN A 8 PRO A 9 9 -142.58
REMARK 500 GLY A 19 SER A 20 9 -147.09
REMARK 500 GLN A 8 PRO A 9 10 -135.72
REMARK 500 LYS A 40 VAL A 41 10 149.86
REMARK 500 GLN A 8 PRO A 9 11 -149.60
REMARK 500 GLN A 8 PRO A 9 15 -149.55
REMARK 500 GLN A 8 PRO A 9 21 -141.25
REMARK 500 GLN A 8 PRO A 9 23 -145.44
REMARK 500 GLN A 8 PRO A 9 24 -136.29
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 5 0.08 SIDE CHAIN
REMARK 500 2 TYR A 5 0.07 SIDE CHAIN
REMARK 500 6 TYR A 5 0.09 SIDE CHAIN
REMARK 500 7 TYR A 5 0.08 SIDE CHAIN
REMARK 500 8 TYR A 5 0.11 SIDE CHAIN
REMARK 500 10 TYR A 5 0.08 SIDE CHAIN
REMARK 500 11 TYR A 5 0.07 SIDE CHAIN
REMARK 500 13 TYR A 14 0.08 SIDE CHAIN
REMARK 500 14 TYR A 5 0.10 SIDE CHAIN
REMARK 500 16 TYR A 5 0.08 SIDE CHAIN
REMARK 500 24 TYR A 5 0.07 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 68
DBREF 1BMR A 1 67 UNP P56678 SCL3_LEIQH 1 67
SEQRES 1 A 68 VAL ARG ASP GLY TYR ILE ALA GLN PRO GLU ASN CYS VAL
SEQRES 2 A 68 TYR HIS CYS PHE PRO GLY SER SER GLY CYS ASP THR LEU
SEQRES 3 A 68 CYS LYS GLU LYS GLY GLY THR SER GLY HIS CYS GLY PHE
SEQRES 4 A 68 LYS VAL GLY HIS GLY LEU ALA CYS TRP CYS ASN ALA LEU
SEQRES 5 A 68 PRO ASP ASN VAL GLY ILE ILE VAL GLU GLY GLU LYS CYS
SEQRES 6 A 68 HIS SER NH2
HET NH2 A 68 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 SER A 21 LYS A 30 1 10
SHEET 1 A 3 SER A 34 LYS A 40 0
SHEET 2 A 3 GLY A 44 LEU A 52 -1 N ASN A 50 O SER A 34
SHEET 3 A 3 ARG A 2 ILE A 6 -1 N ILE A 6 O CYS A 47
SSBOND 1 CYS A 12 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 16 CYS A 37 1555 1555 2.02
SSBOND 3 CYS A 23 CYS A 47 1555 1555 2.01
SSBOND 4 CYS A 27 CYS A 49 1555 1555 2.02
LINK C SER A 67 N NH2 A 68 1555 1555 1.36
SITE 1 AC1 1 SER A 67
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 - b 16 2 Bytes