Header list of 1lqq.pdb file
Complete list - b 23 2 Bytes
HEADER NEUROTOXIN 18-MAY-97 1LQQ
TITLE ANTI-MAMMAL AND ANTI-INSECT LQQIII SCORPION TOXIN, NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LQQIII;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEIURUS QUINQUESTRIATUS QUINQUESTRIATUS;
SOURCE 3 ORGANISM_COMMON: EGYPTIAN SCORPION;
SOURCE 4 ORGANISM_TAXID: 6885;
SOURCE 5 STRAIN: QUINQUESTRIATUS
KEYWDS NEUROTOXIN, LQQIII, SCORPION TOXIN, CSALPHA-BETA MOTIF, SODIUM
KEYWDS 2 CHANNEL INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.LANDON,P.SODANO,F.VOVELLE,M.PTAK
REVDAT 3 23-FEB-22 1LQQ 1 REMARK
REVDAT 2 24-FEB-09 1LQQ 1 VERSN
REVDAT 1 20-MAY-98 1LQQ 0
JRNL AUTH C.LANDON,B.CORNET,J.M.BONMATIN,C.KOPEYAN,H.ROCHAT,F.VOVELLE,
JRNL AUTH 2 M.PTAK
JRNL TITL 1H-NMR-DERIVED SECONDARY STRUCTURE AND THE OVERALL FOLD OF
JRNL TITL 2 THE POTENT ANTI-MAMMAL AND ANTI-INSECT TOXIN III FROM THE
JRNL TITL 3 SCORPION LEIURUS QUINQUESTRIATUS QUINQUESTRIATUS.
JRNL REF EUR.J.BIOCHEM. V. 236 395 1996
JRNL REFN ISSN 0014-2956
JRNL PMID 8612608
JRNL DOI 10.1111/J.1432-1033.1996.00395.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.LANDON,P.SODANO,B.CORNET,J.M.BONMATIN,C.KOPEYAN,H.ROCHAT,
REMARK 1 AUTH 2 F.VOVELLE,M.PTAK
REMARK 1 TITL REFINED SOLUTION STRUCTURE OF THE ANTI-MAMMAL AND
REMARK 1 TITL 2 ANTI-INSECT LQQIII SCORPION TOXIN: COMPARISON WITH OTHER
REMARK 1 TITL 3 SCORPION TOXINS
REMARK 1 REF PROTEINS V. 28 360 1997
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.KOPEYAN,P.MANSUELLE,M.F.MARTIN-EAUCLAIRE,H.ROCHAT,
REMARK 1 AUTH 2 F.MIRANDA
REMARK 1 TITL CHARACTERIZATION OF TOXIN III OF THE SCORPION LEIURUS
REMARK 1 TITL 2 QUINQUESTRIATUS QUINQUESTRIATUS: A NEW TYPE OF ALPHA-TOXIN
REMARK 1 TITL 3 HIGHLY TOXIC BOTH TO MAMMALS AND INSECTS
REMARK 1 REF NAT.TOXINS V. 1 308 1993
REMARK 1 REFN ISSN 1056-9014
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LQQ 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_1000174802.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS,
REMARK 210 LEAST RESIDUAL DEVIATIONS FROM
REMARK 210 IDEALIZED GEOMETRY
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 11 HIS A 64 NE2 HIS A 64 CD2 -0.066
REMARK 500 12 HIS A 64 NE2 HIS A 64 CD2 -0.067
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 38 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 1 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 1 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 1 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 1 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 TYR A 14 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 2 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 2 TRP A 38 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 2 TRP A 38 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 2 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 3 TRP A 38 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 3 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 3 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 4 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 4 TYR A 42 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 4 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 4 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 5 TRP A 38 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 5 TRP A 38 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 5 TYR A 42 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 6 ASP A 3 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 6 CYS A 16 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 6 TRP A 38 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 6 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 6 TRP A 38 NE1 - CE2 - CZ2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 6 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 6 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 6 LEU A 51 N - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 7 ASP A 3 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 7 ARG A 18 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 7 TRP A 38 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 7 TRP A 38 CD1 - NE1 - CE2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 7 TRP A 38 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 7 TYR A 42 CB - CG - CD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 7 TYR A 42 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 7 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 7 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 7 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 8 ASP A 3 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 101 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 4 -178.65 -171.21
REMARK 500 1 LYS A 8 -68.77 -120.86
REMARK 500 1 ASN A 9 -58.39 -135.11
REMARK 500 1 VAL A 13 -168.27 -111.24
REMARK 500 1 ALA A 39 -75.63 -140.58
REMARK 500 1 PRO A 52 176.67 -37.28
REMARK 500 1 PRO A 56 107.42 -56.86
REMARK 500 1 VAL A 59 39.89 -153.84
REMARK 500 2 ALA A 4 -175.30 178.83
REMARK 500 2 LYS A 8 -72.49 -105.23
REMARK 500 2 ASN A 9 -43.67 -142.65
REMARK 500 2 VAL A 13 -166.00 -129.86
REMARK 500 2 GLU A 15 86.06 -63.57
REMARK 500 2 ASN A 23 -18.29 -48.19
REMARK 500 2 ALA A 39 -56.24 -129.31
REMARK 500 2 PRO A 52 175.68 -34.72
REMARK 500 2 ILE A 57 -175.49 -64.99
REMARK 500 2 ARG A 58 156.20 -34.98
REMARK 500 3 LYS A 8 -82.84 -121.45
REMARK 500 3 ASN A 9 -35.22 -135.86
REMARK 500 3 ASP A 19 -53.32 -23.28
REMARK 500 3 ALA A 39 77.82 33.50
REMARK 500 3 LYS A 41 -38.16 -151.84
REMARK 500 3 ALA A 45 172.00 163.34
REMARK 500 3 PRO A 52 21.52 -74.22
REMARK 500 3 ASP A 53 -18.27 72.31
REMARK 500 3 PRO A 56 82.72 -69.50
REMARK 500 3 ILE A 57 -168.53 -69.75
REMARK 500 4 ALA A 4 179.88 179.51
REMARK 500 4 LYS A 8 -71.38 -123.22
REMARK 500 4 ASN A 9 -43.58 -134.85
REMARK 500 4 GLU A 15 83.45 -56.81
REMARK 500 4 ASP A 19 -47.68 -28.41
REMARK 500 4 ALA A 39 -80.61 -130.86
REMARK 500 4 PRO A 52 176.86 -37.48
REMARK 500 4 PRO A 56 103.71 -56.89
REMARK 500 4 VAL A 59 53.47 -149.16
REMARK 500 4 PRO A 60 -145.54 -89.39
REMARK 500 5 LYS A 8 -63.74 -123.52
REMARK 500 5 ASN A 9 -54.23 -135.72
REMARK 500 5 ASP A 19 -49.55 -26.42
REMARK 500 5 ALA A 39 -107.46 -122.97
REMARK 500 5 ALA A 45 -172.79 172.33
REMARK 500 5 PRO A 52 31.14 -80.36
REMARK 500 5 ASP A 53 -12.89 60.67
REMARK 500 5 VAL A 59 59.97 -148.55
REMARK 500 6 ALA A 4 -177.69 -179.10
REMARK 500 6 ASN A 9 -76.28 -115.30
REMARK 500 6 ASN A 11 31.74 71.66
REMARK 500 6 VAL A 13 -161.14 -117.37
REMARK 500
REMARK 500 THIS ENTRY HAS 153 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 2 0.10 SIDE CHAIN
REMARK 500 1 ARG A 18 0.15 SIDE CHAIN
REMARK 500 1 ARG A 58 0.09 SIDE CHAIN
REMARK 500 2 ARG A 2 0.18 SIDE CHAIN
REMARK 500 2 ARG A 18 0.13 SIDE CHAIN
REMARK 500 2 ARG A 58 0.11 SIDE CHAIN
REMARK 500 3 ARG A 2 0.12 SIDE CHAIN
REMARK 500 3 ARG A 18 0.09 SIDE CHAIN
REMARK 500 3 ARG A 58 0.10 SIDE CHAIN
REMARK 500 4 ARG A 2 0.08 SIDE CHAIN
REMARK 500 4 ARG A 18 0.12 SIDE CHAIN
REMARK 500 5 ARG A 2 0.12 SIDE CHAIN
REMARK 500 5 ARG A 18 0.08 SIDE CHAIN
REMARK 500 6 ARG A 2 0.09 SIDE CHAIN
REMARK 500 6 ARG A 58 0.14 SIDE CHAIN
REMARK 500 7 ARG A 2 0.09 SIDE CHAIN
REMARK 500 7 ARG A 18 0.20 SIDE CHAIN
REMARK 500 8 ARG A 2 0.14 SIDE CHAIN
REMARK 500 9 ARG A 2 0.15 SIDE CHAIN
REMARK 500 10 ARG A 18 0.13 SIDE CHAIN
REMARK 500 11 ARG A 2 0.19 SIDE CHAIN
REMARK 500 11 ARG A 18 0.09 SIDE CHAIN
REMARK 500 12 ARG A 2 0.16 SIDE CHAIN
REMARK 500 12 ARG A 18 0.15 SIDE CHAIN
REMARK 500 12 ARG A 58 0.15 SIDE CHAIN
REMARK 500 13 ARG A 2 0.15 SIDE CHAIN
REMARK 500 14 ARG A 18 0.09 SIDE CHAIN
REMARK 500 14 ARG A 58 0.17 SIDE CHAIN
REMARK 500 15 ARG A 2 0.17 SIDE CHAIN
REMARK 500 15 ARG A 58 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LQQ A 1 64 UNP P01487 SCX3_LEIQU 1 64
SEQRES 1 A 64 VAL ARG ASP ALA TYR ILE ALA LYS ASN TYR ASN CYS VAL
SEQRES 2 A 64 TYR GLU CYS PHE ARG ASP SER TYR CYS ASN ASP LEU CYS
SEQRES 3 A 64 THR LYS ASN GLY ALA SER SER GLY TYR CYS GLN TRP ALA
SEQRES 4 A 64 GLY LYS TYR GLY ASN ALA CYS TRP CYS TYR ALA LEU PRO
SEQRES 5 A 64 ASP ASN VAL PRO ILE ARG VAL PRO GLY LYS CYS HIS
HELIX 1 H1 ARG A 18 ASN A 29 1 12
SHEET 1 S1 3 ARG A 2 ILE A 6 0
SHEET 2 S1 3 GLY A 43 LEU A 51 -1
SHEET 3 S1 3 SER A 33 ALA A 39 -1
SSBOND 1 CYS A 12 CYS A 63 1555 1555 2.02
SSBOND 2 CYS A 16 CYS A 36 1555 1555 2.02
SSBOND 3 CYS A 22 CYS A 46 1555 1555 2.02
SSBOND 4 CYS A 26 CYS A 48 1555 1555 2.02
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 23 2 Bytes