Header list of 1fh3.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 31-JUL-00 1FH3
TITLE NMR STRUCTURES OF LQH III ALPHA-LIKE SCORPION TOXIN FROM LEIURUS
TITLE 2 QUINQUESTRIATUS CORRESPONDING TO THE MAJOR CONFORMER IN SOLUTION
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 TRANS ISOMER (1BMR).
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEIURUS QUINQUESTRIATUS HEBRAEUS;
SOURCE 3 ORGANISM_TAXID: 6884;
SOURCE 4 STRAIN: HEBRAEUS;
SOURCE 5 SECRETION: VENOM
KEYWDS ALPHA-LIKE TOXIN, SCORPION TOXIN, SODIUM CHANNEL INHIBITOR NON-
KEYWDS 2 PROLINE CIS PEPTIDE BOND, CIS-TRANS ISOMERISM, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 42
AUTHOR I.KRIMM,X.TRIVELLI,J.M.LANCELIN
REVDAT 5 23-FEB-22 1FH3 1 REMARK LINK
REVDAT 4 24-FEB-09 1FH3 1 VERSN
REVDAT 3 08-NOV-00 1FH3 1 COMPND
REVDAT 2 30-AUG-00 1FH3 1 DBREF
REVDAT 1 23-AUG-00 1FH3 0
JRNL AUTH I.KRIMM,X.TRIVELLI,J.M.LANCELIN
JRNL TITL A CIS-TRANS ISOMERISM OF A NON-PROLYL PEPTIDE BOND IN LQH
JRNL TITL 2 III ALPHA-LIKE SCORPION TOXIN REVEALED BY SOLUTION NMR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.KRIMM,N.GILLES,P.SAUTIERE,M.STANKIEWICZ,M.PELHATE,
REMARK 1 AUTH 2 D.GORDON,J.M.LANCELIN
REMARK 1 TITL NMR STRUCTURES AND ACTIVITY OF A NOVEL ALPHA-LIKE TOXIN FROM
REMARK 1 TITL 2 THE SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS
REMARK 1 REF J.MOL.BIOL. V. 285 1749 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2418
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GIFA 4.2, X-PLOR 3.851
REMARK 3 AUTHORS : DELSUC (GIFA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FH3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011581.
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 : NA
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM LQHIII; 100 MM PHOSPHATE
REMARK 210 BUFFER PH 5.8; 90% H2O 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR NA, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 42
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 : 25
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
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 SER A 20 N - CA - CB ANGL. DEV. = 10.2 DEGREES
REMARK 500 1 GLY A 35 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 2 ASN A 11 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 2 GLY A 35 N - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 2 ALA A 51 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 3 ASP A 3 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 3 TYR A 14 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 3 SER A 20 N - CA - CB ANGL. DEV. = 9.2 DEGREES
REMARK 500 3 GLY A 38 N - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 3 GLY A 62 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 4 ASP A 3 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 4 ASN A 11 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 4 GLY A 19 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 4 PHE A 39 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 4 PHE A 39 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 5 ASP A 3 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 5 GLY A 38 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 6 GLN A 8 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 6 GLY A 38 N - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 7 GLY A 44 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 8 ASP A 3 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 8 SER A 20 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 8 ALA A 51 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 9 GLN A 8 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 9 GLY A 19 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 9 HIS A 43 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 9 GLY A 57 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 9 VAL A 60 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 10 ASP A 3 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 10 ASN A 11 N - CA - C ANGL. DEV. = -21.4 DEGREES
REMARK 500 10 GLY A 19 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 10 VAL A 60 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 10 GLY A 62 N - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 11 ASN A 11 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 11 CYS A 12 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 12 ASP A 3 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 12 GLN A 8 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 12 ASN A 11 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 12 SER A 20 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 13 TYR A 14 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 13 GLY A 38 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 13 GLY A 44 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 13 VAL A 60 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 14 ASN A 11 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 14 HIS A 15 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 15 ASP A 3 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 15 ASN A 11 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 15 PHE A 17 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 16 GLY A 19 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 16 GLY A 38 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 144 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 -129.13 -102.60
REMARK 500 1 CYS A 12 -158.19 -118.99
REMARK 500 1 SER A 20 -23.87 119.42
REMARK 500 1 ILE A 58 -152.49 -142.26
REMARK 500 1 GLU A 63 -92.95 -104.71
REMARK 500 1 LYS A 64 177.78 165.77
REMARK 500 1 HIS A 66 -132.59 -110.54
REMARK 500 2 ALA A 7 -169.63 -110.88
REMARK 500 2 CYS A 12 -155.41 -179.79
REMARK 500 2 SER A 20 0.09 92.11
REMARK 500 2 VAL A 41 132.08 73.38
REMARK 500 2 HIS A 43 -77.27 -69.51
REMARK 500 2 ALA A 51 151.02 177.50
REMARK 500 2 GLU A 61 -117.63 61.83
REMARK 500 2 GLU A 63 -74.20 -118.74
REMARK 500 3 ASN A 11 44.19 84.66
REMARK 500 3 SER A 20 -0.84 106.12
REMARK 500 3 HIS A 43 -76.36 -135.62
REMARK 500 3 ALA A 51 46.43 72.94
REMARK 500 3 ILE A 58 -145.51 -143.66
REMARK 500 3 GLU A 61 -129.96 60.61
REMARK 500 3 LYS A 64 -150.74 -106.74
REMARK 500 4 ALA A 7 -129.78 -135.53
REMARK 500 4 CYS A 12 -161.97 -170.08
REMARK 500 4 PRO A 18 103.97 -57.34
REMARK 500 4 VAL A 41 -157.98 -146.69
REMARK 500 4 HIS A 43 -54.34 -129.49
REMARK 500 4 LEU A 45 171.75 73.36
REMARK 500 4 ALA A 51 76.89 59.88
REMARK 500 4 ILE A 58 -156.13 -136.16
REMARK 500 4 GLU A 63 -95.63 -123.87
REMARK 500 5 SER A 20 -12.77 99.64
REMARK 500 5 HIS A 36 -167.65 -160.92
REMARK 500 5 HIS A 43 -83.41 -118.61
REMARK 500 5 ALA A 51 54.79 72.44
REMARK 500 5 ILE A 58 -146.83 -142.31
REMARK 500 5 GLU A 63 -153.30 -95.26
REMARK 500 5 HIS A 66 -147.31 66.76
REMARK 500 6 ALA A 7 -147.94 -100.50
REMARK 500 6 CYS A 12 -159.79 177.05
REMARK 500 6 TYR A 14 -157.44 -89.61
REMARK 500 6 SER A 20 -5.43 86.09
REMARK 500 6 ALA A 51 56.96 73.24
REMARK 500 6 GLU A 61 -124.15 62.24
REMARK 500 6 LYS A 64 -168.64 -163.23
REMARK 500 7 ASN A 11 31.99 80.63
REMARK 500 7 LYS A 40 26.04 -173.07
REMARK 500 7 ASP A 54 32.59 -85.86
REMARK 500 7 ILE A 58 -150.29 -150.55
REMARK 500 7 GLU A 63 -149.32 -94.40
REMARK 500
REMARK 500 THIS ENTRY HAS 346 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 GLY A 57 ILE A 58 1 -141.23
REMARK 500 ALA A 51 LEU A 52 2 149.38
REMARK 500 PHE A 17 PRO A 18 15 -141.59
REMARK 500 GLU A 61 GLY A 62 17 -147.21
REMARK 500 GLU A 61 GLY A 62 18 -146.09
REMARK 500 GLY A 19 SER A 20 25 -148.01
REMARK 500 ILE A 58 ILE A 59 28 -147.27
REMARK 500 SER A 20 SER A 21 36 -147.35
REMARK 500 ALA A 51 LEU A 52 39 141.79
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 2 ARG A 2 0.11 SIDE CHAIN
REMARK 500 2 TYR A 5 0.10 SIDE CHAIN
REMARK 500 6 TYR A 5 0.07 SIDE CHAIN
REMARK 500 10 TYR A 5 0.09 SIDE CHAIN
REMARK 500 11 TYR A 5 0.08 SIDE CHAIN
REMARK 500 17 TYR A 5 0.08 SIDE CHAIN
REMARK 500 18 ARG A 2 0.11 SIDE CHAIN
REMARK 500 19 TYR A 5 0.08 SIDE CHAIN
REMARK 500 20 TYR A 5 0.07 SIDE CHAIN
REMARK 500 23 TYR A 14 0.09 SIDE CHAIN
REMARK 500 25 TYR A 5 0.08 SIDE CHAIN
REMARK 500 26 TYR A 14 0.07 SIDE CHAIN
REMARK 500 27 TYR A 14 0.08 SIDE CHAIN
REMARK 500 28 ARG A 2 0.15 SIDE CHAIN
REMARK 500 29 TYR A 14 0.09 SIDE CHAIN
REMARK 500 30 TYR A 5 0.08 SIDE CHAIN
REMARK 500 33 TYR A 14 0.07 SIDE CHAIN
REMARK 500 34 TYR A 5 0.07 SIDE CHAIN
REMARK 500 39 TYR A 5 0.07 SIDE CHAIN
REMARK 500 41 TYR A 5 0.07 SIDE CHAIN
REMARK 500 42 TYR A 5 0.09 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
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BMR RELATED DB: PDB
REMARK 900 THIS ENTRY CORRESPONDS TO THE STRUCTURE OF LQHIII TOXIN CALCULATED
REMARK 900 WITH A PRO9-GLU10 TRANS PEPTIDE BOND.
DBREF 1FH3 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 20 GLY A 31 1 12
SHEET 1 A 3 ARG A 2 ILE A 6 0
SHEET 2 A 3 GLY A 44 LEU A 52 -1 N CYS A 47 O ILE A 6
SHEET 3 A 3 SER A 34 LYS A 40 -1 O SER A 34 N ASN A 50
SSBOND 1 CYS A 12 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 16 CYS A 37 1555 1555 2.03
SSBOND 3 CYS A 23 CYS A 47 1555 1555 2.02
SSBOND 4 CYS A 27 CYS A 49 1555 1555 2.02
LINK C SER A 67 N NH2 A 68 1555 1555 1.37
CISPEP 1 PRO A 9 GLU A 10 1 4.61
CISPEP 2 PRO A 9 GLU A 10 2 12.35
CISPEP 3 PRO A 9 GLU A 10 3 -5.45
CISPEP 4 PRO A 9 GLU A 10 4 9.48
CISPEP 5 PRO A 9 GLU A 10 5 1.20
CISPEP 6 PRO A 9 GLU A 10 6 9.14
CISPEP 7 PRO A 9 GLU A 10 7 1.26
CISPEP 8 PRO A 9 GLU A 10 8 -7.64
CISPEP 9 PRO A 9 GLU A 10 9 5.78
CISPEP 10 PRO A 9 GLU A 10 10 1.94
CISPEP 11 PRO A 9 GLU A 10 11 -1.61
CISPEP 12 PRO A 9 GLU A 10 12 10.82
CISPEP 13 PRO A 9 GLU A 10 13 5.49
CISPEP 14 PRO A 9 GLU A 10 14 5.84
CISPEP 15 PRO A 9 GLU A 10 15 12.23
CISPEP 16 PRO A 9 GLU A 10 16 3.97
CISPEP 17 PRO A 9 GLU A 10 17 9.52
CISPEP 18 PRO A 9 GLU A 10 18 2.27
CISPEP 19 PRO A 9 GLU A 10 19 7.46
CISPEP 20 PRO A 9 GLU A 10 20 7.51
CISPEP 21 PRO A 9 GLU A 10 21 -3.69
CISPEP 22 PRO A 9 GLU A 10 22 7.40
CISPEP 23 PRO A 9 GLU A 10 23 -10.68
CISPEP 24 PRO A 9 GLU A 10 24 13.96
CISPEP 25 PRO A 9 GLU A 10 25 -1.06
CISPEP 26 PRO A 9 GLU A 10 26 11.77
CISPEP 27 PRO A 9 GLU A 10 27 -1.11
CISPEP 28 PRO A 9 GLU A 10 28 14.54
CISPEP 29 PRO A 9 GLU A 10 29 7.66
CISPEP 30 PRO A 9 GLU A 10 30 17.44
CISPEP 31 PRO A 9 GLU A 10 31 2.48
CISPEP 32 PRO A 9 GLU A 10 32 12.80
CISPEP 33 PRO A 9 GLU A 10 33 4.60
CISPEP 34 PRO A 9 GLU A 10 34 5.27
CISPEP 35 PRO A 9 GLU A 10 35 6.57
CISPEP 36 PRO A 9 GLU A 10 36 14.48
CISPEP 37 PRO A 9 GLU A 10 37 13.40
CISPEP 38 PRO A 9 GLU A 10 38 -1.20
CISPEP 39 PRO A 9 GLU A 10 39 12.81
CISPEP 40 PRO A 9 GLU A 10 40 20.23
CISPEP 41 PRO A 9 GLU A 10 41 2.54
CISPEP 42 PRO A 9 GLU A 10 42 7.18
SITE 1 AC1 2 GLN A 8 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 23 2 Bytes