Header list of 1h5o.pdb file
Complete list - l 24 2 Bytes
HEADER TOXIN 23-MAY-01 1H5O TITLE SOLUTION STRUCTURE OF CROTAMINE, A NEUROTOXIN FROM CROTALUS TITLE 2 DURISSUS TERRIFICUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: MYOTOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CROTAMINE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CROTALUS DURISSUS TERRIFICUS; SOURCE 3 ORGANISM_COMMON: SOUTH AMERICAN RATTLESNAKE; SOURCE 4 ORGANISM_TAXID: 8732; SOURCE 5 OTHER_DETAILS: VENOM OF THE RATTLESNAKE CROTALUS DURISSUS SOURCE 6 TERRIFICUS KEYWDS TOXIN, SODIUM CHANNEL AFFECTING TOXIN, VENOM EXPDTA SOLUTION NMR NUMMDL 26 AUTHOR G.NICASTRO,L.FRANZONI,C.DE CHIARA,C.A.MANCIN,J.R.GIGLIO, AUTHOR 2 A.SPISNI REVDAT 4 24-JUL-13 1H5O 1 HEADER KEYWDS REMARK VERSN REVDAT 4 2 SCALE1 SCALE2 REVDAT 3 24-FEB-09 1H5O 1 VERSN REVDAT 2 21-FEB-06 1H5O 1 EXPDTA REVDAT 1 09-MAY-03 1H5O 0 JRNL AUTH G.NICASTRO,L.FRANZONI,C.DE CHIARA,A.C.A.MANCIN, JRNL AUTH 2 J.R.GIGLIO,A.SPISNI JRNL TITL SOLUTION STRUCTURE OF CROTAMINE, A NA+ CHANNEL JRNL TITL 2 AFFECTING TOXIN FROM CROTALUS DURISSUS TERRIFICUS JRNL TITL 3 VENOM JRNL REF EUR.J.BIOCHEM. V. 270 1969 2003 JRNL REFN ISSN 0014-2956 JRNL PMID 12709056 JRNL DOI 10.1046/J.1432-1033.2003.03563.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.C.MANCIN,A.M.SOARES,S.H.ANDRIAO-ESCARSO,V.M.FACA, REMARK 1 AUTH 2 L.J.GREENE,S.ZUCCOLOTTO,I.R.PELA,J.R.GIGLIO REMARK 1 TITL THE ANALGESIC ACTIVITY OF CROTAMINE,A NEUROTOXIN REMARK 1 TITL 2 FROM CROTALUS DURISSUS TERRIFICUS VENOM:A REMARK 1 TITL 3 BIOCHEMICAL AND PHARMACOLOGICAL STUDY REMARK 1 REF TOXICON V. 36 1927 1998 REMARK 1 REFN ISSN 0041-0101 REMARK 1 PMID 9839677 REMARK 1 DOI 10.1016/S0041-0101(98)00117-2 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SEE JRNL CITATION REMARK 4 REMARK 4 1H5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-NOV-02. REMARK 100 THE PDBE ID CODE IS EBI-8083. 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 : NULL REMARK 210 SAMPLE CONTENTS : 1MM CROTAMINE, REMARK 210 H2O/TFE (70/30) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY, NOESY, DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX600; DMX800 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : MSI DISCOVER REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT REMARK 210 VIOLATION, LEAST RESIDUAL REMARK 210 DEVIATIONS FROM IDEALIZED REMARK 210 GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR REMARK 210 1H-1H 2D NMR ON THE NATURAL TOXIN EXTRACTED FROM THE REMARK 210 SNAKE 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 400 REMARK 400 COMPOUND REMARK 400 EXTREMELY RAPID ACTING TOXIN THAT CAUSES MUSCLE NECROSIS. REMARK 400 DISABLES PREY BY CAUSING INSTANTANEOUS PARALYSIS OF HIND REMARK 400 LIMBS AND DEATH BY PARALYSIS OF THE DIAPHRAGM. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 H1 TYR A 1 - OD2 ASP A 29 1.53 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 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 1 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 1 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 1 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 2 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 2 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 2 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 2 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 3 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 3 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 3 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 3 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 4 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 4 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 4 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 4 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 4 TRP A 32 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES REMARK 500 5 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 5 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 5 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 6 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 6 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 6 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.0 DEGREES REMARK 500 6 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 7 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 7 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 7 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 7 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 7 TRP A 32 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES REMARK 500 8 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 8 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 8 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 8 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 9 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 9 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 9 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.0 DEGREES REMARK 500 9 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 10 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 10 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 10 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 10 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 11 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 11 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 11 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 11 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 12 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 12 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 12 HIS A 10 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 12 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 13 HIS A 5 CE1 - NE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 108 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 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 SER A 23 98.27 -162.53 REMARK 500 2 SER A 23 74.64 -163.74 REMARK 500 2 MET A 28 -74.52 -98.48 REMARK 500 2 CYS A 30 -103.00 -129.97 REMARK 500 3 LYS A 2 -71.92 -173.81 REMARK 500 3 SER A 22 56.73 -92.58 REMARK 500 3 MET A 28 -111.02 -82.17 REMARK 500 4 PRO A 13 173.49 -58.05 REMARK 500 4 SER A 22 52.62 -93.45 REMARK 500 4 SER A 23 77.88 -150.23 REMARK 500 4 MET A 28 -76.26 -84.50 REMARK 500 4 CYS A 30 -157.78 -114.10 REMARK 500 5 SER A 22 58.91 -90.50 REMARK 500 5 SER A 23 83.20 -162.48 REMARK 500 5 MET A 28 -113.63 -90.19 REMARK 500 5 ASP A 29 68.64 -110.62 REMARK 500 5 CYS A 30 -88.68 -142.26 REMARK 500 6 LYS A 2 -78.26 -87.19 REMARK 500 6 ASP A 29 57.65 -151.72 REMARK 500 6 CYS A 30 -105.36 -123.32 REMARK 500 7 SER A 22 59.43 -90.06 REMARK 500 7 SER A 23 85.75 -161.27 REMARK 500 7 MET A 28 -77.52 -89.50 REMARK 500 7 ASP A 29 43.85 -145.86 REMARK 500 7 CYS A 30 -151.21 -134.11 REMARK 500 8 LYS A 2 -69.84 -132.32 REMARK 500 8 SER A 22 50.46 -96.93 REMARK 500 8 SER A 23 78.53 -152.11 REMARK 500 8 MET A 28 -121.40 -89.34 REMARK 500 8 ASP A 29 48.51 -95.54 REMARK 500 8 CYS A 30 -93.39 -131.53 REMARK 500 9 LYS A 2 -80.32 -90.44 REMARK 500 9 SER A 22 48.90 -85.60 REMARK 500 9 SER A 23 72.51 -167.81 REMARK 500 9 MET A 28 -86.37 -86.01 REMARK 500 9 ASP A 29 50.60 -140.72 REMARK 500 9 CYS A 30 -90.92 -98.98 REMARK 500 10 LYS A 2 -71.73 -95.17 REMARK 500 10 SER A 23 71.01 -165.99 REMARK 500 10 MET A 28 -95.39 -117.98 REMARK 500 10 CYS A 30 -77.80 -144.85 REMARK 500 11 LYS A 2 -72.29 -91.65 REMARK 500 11 SER A 23 50.02 -100.42 REMARK 500 11 MET A 28 -79.61 -71.18 REMARK 500 11 ASP A 29 52.95 -111.05 REMARK 500 11 ARG A 31 -165.78 -79.96 REMARK 500 12 MET A 28 -108.66 -84.88 REMARK 500 12 ASP A 29 66.80 -108.23 REMARK 500 13 LYS A 2 -86.71 -82.87 REMARK 500 13 MET A 28 -93.18 -117.91 REMARK 500 13 CYS A 30 -88.93 -123.28 REMARK 500 14 SER A 22 49.44 -87.62 REMARK 500 14 SER A 23 51.40 -150.91 REMARK 500 14 MET A 28 -118.81 -96.92 REMARK 500 15 LYS A 2 -58.15 -156.07 REMARK 500 15 PRO A 21 48.52 -93.90 REMARK 500 15 MET A 28 -116.01 -108.36 REMARK 500 15 ASP A 29 53.51 -91.11 REMARK 500 16 LYS A 2 -62.10 -99.41 REMARK 500 16 MET A 28 -106.30 -122.44 REMARK 500 16 ASP A 29 50.67 -95.40 REMARK 500 16 CYS A 30 -89.20 -157.47 REMARK 500 17 GLU A 15 -27.74 -150.19 REMARK 500 17 SER A 23 47.40 -94.61 REMARK 500 17 MET A 28 -112.01 -93.04 REMARK 500 17 CYS A 30 -83.24 -111.35 REMARK 500 17 LYS A 38 74.88 -104.55 REMARK 500 18 LYS A 16 -106.49 -90.25 REMARK 500 18 MET A 28 -81.24 -90.20 REMARK 500 18 ASP A 29 57.84 -148.06 REMARK 500 18 CYS A 30 -102.15 -135.13 REMARK 500 19 SER A 22 45.27 -102.80 REMARK 500 19 SER A 23 63.73 -160.55 REMARK 500 19 MET A 28 -85.28 -78.72 REMARK 500 20 LYS A 2 -66.41 -95.01 REMARK 500 20 SER A 22 58.69 -92.98 REMARK 500 20 SER A 23 88.19 -164.20 REMARK 500 20 MET A 28 -121.10 -107.45 REMARK 500 20 ASP A 29 66.05 -100.24 REMARK 500 20 CYS A 30 -142.25 -146.55 REMARK 500 21 LYS A 2 -66.01 -90.47 REMARK 500 21 PRO A 21 52.27 -93.19 REMARK 500 21 MET A 28 -76.36 -95.58 REMARK 500 21 ASP A 29 58.74 -153.41 REMARK 500 21 CYS A 30 -71.23 -141.45 REMARK 500 22 LYS A 2 -69.76 -174.27 REMARK 500 22 PRO A 21 55.63 -94.58 REMARK 500 22 MET A 28 -115.97 -95.34 REMARK 500 23 LYS A 2 -70.16 -135.16 REMARK 500 23 SER A 23 80.73 -162.44 REMARK 500 23 MET A 28 -108.65 -86.98 REMARK 500 23 ASP A 29 50.61 -103.53 REMARK 500 24 LYS A 2 -137.68 -142.21 REMARK 500 24 GLU A 15 -35.84 -154.23 REMARK 500 24 MET A 28 -71.52 -83.37 REMARK 500 25 LYS A 2 -64.12 -107.97 REMARK 500 25 LYS A 14 45.90 -85.12 REMARK 500 25 GLU A 15 -29.02 -145.41 REMARK 500 25 SER A 22 59.26 -94.70 REMARK 500 25 SER A 23 69.16 -166.18 REMARK 500 25 MET A 28 -95.95 -119.42 REMARK 500 25 ASP A 29 53.71 -107.79 REMARK 500 26 LYS A 2 -71.65 -88.49 REMARK 500 26 GLU A 15 -32.20 -169.29 REMARK 500 26 SER A 22 -66.35 -140.05 REMARK 500 26 MET A 28 -120.39 -99.43 REMARK 500 26 ASP A 29 40.77 -103.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. DBREF 1H5O A 1 42 UNP P01475 MYXC_CRODU 1 42 SEQRES 1 A 42 TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO SEQRES 2 A 42 LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY SEQRES 3 A 42 LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS SEQRES 4 A 42 GLY SER GLY HELIX 1 1 GLN A 3 LYS A 7 1 5 SHEET 1 AA 3 GLY A 9 PHE A 12 0 SHEET 2 AA 3 LYS A 35 LYS A 38 -1 N LYS A 35 O PHE A 12 SHEET 3 AA 3 ASP A 24 PHE A 25 -1 N CYS A 36 O PHE A 25 SSBOND 1 CYS A 4 CYS A 36 1555 1555 2.00 SSBOND 2 CYS A 11 CYS A 30 1555 1555 2.00 SSBOND 3 CYS A 18 CYS A 37 1555 1555 2.00 CISPEP 1 LEU A 19 PRO A 20 1 7.69 CISPEP 2 LEU A 19 PRO A 20 2 0.73 CISPEP 3 LEU A 19 PRO A 20 3 1.29 CISPEP 4 LEU A 19 PRO A 20 4 5.03 CISPEP 5 LEU A 19 PRO A 20 5 2.97 CISPEP 6 LEU A 19 PRO A 20 6 7.71 CISPEP 7 LEU A 19 PRO A 20 7 8.67 CISPEP 8 LEU A 19 PRO A 20 8 5.05 CISPEP 9 LEU A 19 PRO A 20 9 9.17 CISPEP 10 LEU A 19 PRO A 20 10 5.72 CISPEP 11 LEU A 19 PRO A 20 11 4.70 CISPEP 12 LEU A 19 PRO A 20 12 8.83 CISPEP 13 LEU A 19 PRO A 20 13 7.47 CISPEP 14 LEU A 19 PRO A 20 14 5.39 CISPEP 15 LEU A 19 PRO A 20 15 10.10 CISPEP 16 LEU A 19 PRO A 20 16 5.49 CISPEP 17 LEU A 19 PRO A 20 17 8.21 CISPEP 18 LEU A 19 PRO A 20 18 6.96 CISPEP 19 LEU A 19 PRO A 20 19 7.72 CISPEP 20 LEU A 19 PRO A 20 20 9.31 CISPEP 21 LEU A 19 PRO A 20 21 8.88 CISPEP 22 LEU A 19 PRO A 20 22 6.09 CISPEP 23 LEU A 19 PRO A 20 23 9.87 CISPEP 24 LEU A 19 PRO A 20 24 6.07 CISPEP 25 LEU A 19 PRO A 20 25 2.64 CISPEP 26 LEU A 19 PRO A 20 26 4.43 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 - l 24 2 Bytes