Header list of 1cis.pdb file
Complete list - v 29 2 Bytes
HEADER HYBRID PROTEIN 23-APR-93 1CIS TITLE CONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION. THE TITLE 2 THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID BETWEEN TITLE 3 CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN CARLSBERG COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYBRID PROTEIN FORMED FROM CHYMOTRYPSIN INHIBITOR-2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE, BACILLUS LICHENIFORMIS; SOURCE 3 ORGANISM_COMMON: BARLEY, DENITROBACILLUS LICHENIFORMIS; SOURCE 4 ORGANISM_TAXID: 4513, 1402; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HYBRID PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR P.OSMARK,P.SORENSEN,F.M.POULSEN REVDAT 4 29-NOV-17 1CIS 1 REMARK HELIX REVDAT 3 25-AUG-09 1CIS 1 SOURCE REVDAT 2 24-FEB-09 1CIS 1 VERSN REVDAT 1 31-OCT-93 1CIS 0 JRNL AUTH P.OSMARK,P.SORENSEN,F.M.POULSEN JRNL TITL CONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION: JRNL TITL 2 THE THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID JRNL TITL 3 BETWEEN CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN JRNL TITL 4 CARLSBERG. JRNL REF BIOCHEMISTRY V. 32 11007 1993 JRNL REFN ISSN 0006-2960 JRNL PMID 8218165 JRNL DOI 10.1021/BI00092A009 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.LUDVIGSEN,H.SHEN,M.KJAER,J.C.MADSEN,F.M.POULSEN REMARK 1 TITL REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF REMARK 1 TITL 2 BARLEY SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE REMARK 1 TITL 3 STRUCTURES IN CRYSTALS REMARK 1 REF J.MOL.BIOL. V. 222 621 1991 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.BODE,E.PAPAMOKOS,D.MUSIL REMARK 1 TITL THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX REMARK 1 TITL 2 FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE REMARK 1 TITL 3 INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS: STRUCTURAL REMARK 1 TITL 4 ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY REMARK 1 REF EUR.J.BIOCHEM. V. 166 673 1987 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CIS 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_1000172350. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 8 ARG A 64 CZ ARG A 64 NH2 -0.079 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 24 CG - CD1 - NE1 ANGL. DEV. = -7.9 DEGREES REMARK 500 1 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 1 ARG A 64 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES REMARK 500 1 ARG A 67 NH1 - CZ - NH2 ANGL. DEV. = 7.4 DEGREES REMARK 500 1 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES REMARK 500 1 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 1 ARG A 83 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES REMARK 500 2 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -7.8 DEGREES REMARK 500 2 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 2 TYR A 63 CA - CB - CG ANGL. DEV. = -11.8 DEGREES REMARK 500 2 ARG A 64 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 2 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 2 ARG A 69 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES REMARK 500 2 ASP A 73 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ARG A 83 NH1 - CZ - NH2 ANGL. DEV. = 9.4 DEGREES REMARK 500 2 ARG A 83 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES REMARK 500 2 ARG A 83 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES REMARK 500 3 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -8.1 DEGREES REMARK 500 3 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 3 TRP A 24 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES REMARK 500 3 GLU A 34 OE1 - CD - OE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 3 ARG A 64 CG - CD - NE ANGL. DEV. = -13.1 DEGREES REMARK 500 3 ARG A 67 NH1 - CZ - NH2 ANGL. DEV. = 10.1 DEGREES REMARK 500 3 ARG A 67 NE - CZ - NH1 ANGL. DEV. = -7.8 DEGREES REMARK 500 3 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES REMARK 500 3 ASP A 73 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -8.2 DEGREES REMARK 500 4 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 4 TRP A 24 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES REMARK 500 4 ARG A 64 NH1 - CZ - NH2 ANGL. DEV. = 8.7 DEGREES REMARK 500 4 ARG A 64 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES REMARK 500 4 ARG A 64 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES REMARK 500 4 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 4 ARG A 83 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 4 VAL A 84 CG1 - CB - CG2 ANGL. DEV. = -10.1 DEGREES REMARK 500 5 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -8.0 DEGREES REMARK 500 5 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 5 GLN A 47 N - CA - C ANGL. DEV. = -18.7 DEGREES REMARK 500 5 ARG A 64 NH1 - CZ - NH2 ANGL. DEV. = 7.2 DEGREES REMARK 500 5 ARG A 64 NE - CZ - NH2 ANGL. DEV. = -7.6 DEGREES REMARK 500 5 ARG A 67 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES REMARK 500 5 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 5 ASP A 73 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 5 ARG A 83 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES REMARK 500 6 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -7.6 DEGREES REMARK 500 6 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 6 TYR A 60 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 6 TYR A 60 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES REMARK 500 6 GLU A 62 OE1 - CD - OE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 6 ARG A 83 NH1 - CZ - NH2 ANGL. DEV. = 7.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 121 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 LEU A 51 -158.08 -155.32 REMARK 500 1 GLU A 52 -165.76 -105.64 REMARK 500 1 LYS A 53 -158.49 -31.44 REMARK 500 1 ALA A 55 77.91 -107.61 REMARK 500 1 ASP A 57 -67.04 -120.01 REMARK 500 1 ALA A 61 -171.15 -41.55 REMARK 500 1 GLU A 62 161.24 -40.73 REMARK 500 1 TYR A 63 161.66 -40.30 REMARK 500 1 ILE A 65 7.32 -63.31 REMARK 500 1 ASP A 76 41.61 27.96 REMARK 500 1 VAL A 84 -80.90 -48.20 REMARK 500 2 TRP A 24 69.19 -115.12 REMARK 500 2 GLU A 26 -31.37 -38.79 REMARK 500 2 GLU A 52 -160.15 -101.40 REMARK 500 2 GLN A 54 62.56 -54.34 REMARK 500 2 ALA A 55 55.53 -105.26 REMARK 500 2 ASN A 58 43.88 -85.89 REMARK 500 2 GLU A 62 -154.64 -104.46 REMARK 500 2 ASP A 73 -140.51 -94.31 REMARK 500 2 ASP A 76 38.45 29.87 REMARK 500 2 VAL A 81 103.13 -59.45 REMARK 500 3 TRP A 24 60.92 -117.66 REMARK 500 3 GLU A 26 -29.31 -34.52 REMARK 500 3 GLU A 52 -148.22 -89.73 REMARK 500 3 LYS A 53 -168.83 -62.60 REMARK 500 3 GLN A 54 47.74 -78.89 REMARK 500 3 TYR A 60 -165.45 -107.09 REMARK 500 3 GLU A 62 -155.01 -39.58 REMARK 500 3 TYR A 63 107.98 -46.95 REMARK 500 3 ARG A 64 73.80 -113.24 REMARK 500 3 ILE A 65 -22.74 -23.06 REMARK 500 3 VAL A 68 110.11 -162.77 REMARK 500 3 ASP A 73 -158.72 -109.16 REMARK 500 3 ASP A 76 36.30 25.98 REMARK 500 3 VAL A 81 102.91 -51.85 REMARK 500 3 VAL A 84 -70.34 -48.46 REMARK 500 4 GLU A 26 -35.19 -32.91 REMARK 500 4 GLU A 52 -96.90 -73.99 REMARK 500 4 GLN A 54 46.98 -83.23 REMARK 500 4 TYR A 60 -163.23 -106.99 REMARK 500 4 ALA A 61 -157.78 -80.15 REMARK 500 4 ILE A 65 1.87 -54.90 REMARK 500 4 ASP A 73 -149.19 -95.19 REMARK 500 4 ASP A 76 40.44 24.24 REMARK 500 4 VAL A 81 98.66 -64.62 REMARK 500 4 VAL A 84 -101.69 -66.17 REMARK 500 5 GLU A 26 -31.58 -31.49 REMARK 500 5 ALA A 46 124.70 -38.65 REMARK 500 5 GLU A 52 -153.98 -60.48 REMARK 500 5 LYS A 53 -163.77 -58.67 REMARK 500 REMARK 500 THIS ENTRY HAS 171 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 64 0.23 SIDE CHAIN REMARK 500 1 ARG A 67 0.30 SIDE CHAIN REMARK 500 1 ARG A 69 0.29 SIDE CHAIN REMARK 500 1 ARG A 83 0.28 SIDE CHAIN REMARK 500 2 ARG A 64 0.13 SIDE CHAIN REMARK 500 2 ARG A 67 0.24 SIDE CHAIN REMARK 500 2 ARG A 69 0.30 SIDE CHAIN REMARK 500 2 ARG A 83 0.20 SIDE CHAIN REMARK 500 3 ARG A 64 0.28 SIDE CHAIN REMARK 500 3 ARG A 67 0.30 SIDE CHAIN REMARK 500 3 ARG A 69 0.20 SIDE CHAIN REMARK 500 3 ARG A 83 0.17 SIDE CHAIN REMARK 500 4 ARG A 64 0.17 SIDE CHAIN REMARK 500 4 ARG A 67 0.27 SIDE CHAIN REMARK 500 4 ARG A 69 0.11 SIDE CHAIN REMARK 500 4 ARG A 83 0.32 SIDE CHAIN REMARK 500 5 ARG A 64 0.16 SIDE CHAIN REMARK 500 5 ARG A 67 0.19 SIDE CHAIN REMARK 500 5 ARG A 69 0.23 SIDE CHAIN REMARK 500 5 ARG A 83 0.28 SIDE CHAIN REMARK 500 6 ARG A 64 0.12 SIDE CHAIN REMARK 500 6 ARG A 67 0.28 SIDE CHAIN REMARK 500 6 ARG A 69 0.25 SIDE CHAIN REMARK 500 6 ARG A 83 0.28 SIDE CHAIN REMARK 500 7 ARG A 64 0.24 SIDE CHAIN REMARK 500 7 ARG A 67 0.26 SIDE CHAIN REMARK 500 7 ARG A 69 0.29 SIDE CHAIN REMARK 500 7 ARG A 83 0.25 SIDE CHAIN REMARK 500 8 ARG A 64 0.21 SIDE CHAIN REMARK 500 8 ARG A 67 0.18 SIDE CHAIN REMARK 500 8 ARG A 69 0.20 SIDE CHAIN REMARK 500 8 ARG A 83 0.28 SIDE CHAIN REMARK 500 9 ARG A 64 0.20 SIDE CHAIN REMARK 500 9 ARG A 67 0.22 SIDE CHAIN REMARK 500 9 ARG A 69 0.16 SIDE CHAIN REMARK 500 9 ARG A 83 0.24 SIDE CHAIN REMARK 500 10 ARG A 67 0.16 SIDE CHAIN REMARK 500 10 ARG A 69 0.30 SIDE CHAIN REMARK 500 10 ARG A 83 0.19 SIDE CHAIN REMARK 500 11 ARG A 64 0.19 SIDE CHAIN REMARK 500 11 ARG A 67 0.28 SIDE CHAIN REMARK 500 11 ARG A 69 0.15 SIDE CHAIN REMARK 500 11 ARG A 83 0.16 SIDE CHAIN REMARK 500 12 ARG A 64 0.23 SIDE CHAIN REMARK 500 12 ARG A 67 0.18 SIDE CHAIN REMARK 500 12 ARG A 69 0.30 SIDE CHAIN REMARK 500 12 ARG A 83 0.30 SIDE CHAIN REMARK 500 13 ARG A 64 0.12 SIDE CHAIN REMARK 500 13 ARG A 67 0.28 SIDE CHAIN REMARK 500 13 ARG A 69 0.20 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1CIS A 21 85 UNP P01053 ICI2_HORVU 21 83 SEQADV 1CIS GLU A 52 UNP P01053 INSERTION SEQADV 1CIS LYS A 53 UNP P01053 INSERTION SEQADV 1CIS GLN A 54 UNP P01053 PRO 52 CONFLICT SEQADV 1CIS ALA A 55 UNP P01053 VAL 53 CONFLICT SEQADV 1CIS VAL A 56 UNP P01053 GLY 54 CONFLICT SEQADV 1CIS ASP A 57 UNP P01053 THR 55 CONFLICT SEQADV 1CIS ASN A 58 UNP P01053 ILE 56 CONFLICT SEQADV 1CIS ALA A 59 UNP P01053 VAL 57 CONFLICT SEQADV 1CIS TYR A 60 UNP P01053 THR 58 CONFLICT SEQADV 1CIS ALA A 61 UNP P01053 MET 59 CONFLICT SEQADV 1CIS ALA A 71 UNP P01053 PHE 69 CONFLICT SEQRES 1 A 66 MET LYS THR GLU TRP PRO GLU LEU VAL GLY LYS SER VAL SEQRES 2 A 66 GLU GLU ALA LYS LYS VAL ILE LEU GLN ASP LYS PRO GLU SEQRES 3 A 66 ALA GLN ILE ILE VAL LEU GLU LYS GLN ALA VAL ASP ASN SEQRES 4 A 66 ALA TYR ALA GLU TYR ARG ILE ASP ARG VAL ARG LEU ALA SEQRES 5 A 66 VAL ASP LYS LEU ASP ASN ILE ALA GLN VAL PRO ARG VAL SEQRES 6 A 66 GLY HELIX 1 H1 SER A 31 LYS A 43 1 13 SHEET 1 S1A 4 THR A 22 PRO A 25 0 SHEET 2 S1A 4 PRO A 82 VAL A 84 -1 O PRO A 82 N TRP A 24 SHEET 3 S1A 4 ASP A 66 VAL A 72 -1 N ARG A 69 O ARG A 83 SHEET 4 S1A 4 GLN A 47 LEU A 51 1 O ILE A 49 N LEU A 70 SHEET 1 S1B 4 GLY A 29 SER A 31 0 SHEET 2 S1B 4 ASN A 77 GLN A 80 -1 N ILE A 78 O LYS A 30 SHEET 3 S1B 4 ASP A 66 ASP A 73 -1 N ASP A 73 O ASN A 77 SHEET 4 S1B 4 GLN A 47 LEU A 51 1 O ILE A 49 N LEU A 70 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 - v 29 2 Bytes