Header list of 1f5y.pdb file
Complete list - b 16 2 Bytes
HEADER LIPID BINDING PROTEIN 18-JUN-00 1F5Y TITLE NMR STRUCTURE OF A CONCATEMER OF THE FIRST AND SECOND LIGAND-BINDING TITLE 2 MODULES OF THE HUMAN LDL RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIGAND-BINDING MODULES 1-2; COMPND 5 SYNONYM: LDL RECEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: LIGAND-BINDING MODULE CONCATEMER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 ORGAN: LIVER; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX-2T, GST-FUSION PROTEIN KEYWDS BETA HAIRPIN, 3-10 HELIX, CALCIUM BINDING, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.D.KURNIAWAN,A.R.ATKINS,I.M.BRERETON,P.A.KROON,R.SMITH REVDAT 3 16-FEB-22 1F5Y 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1F5Y 1 VERSN REVDAT 1 30-AUG-00 1F5Y 0 JRNL AUTH N.D.KURNIAWAN,A.R.ATKINS,S.BIERI,C.J.BROWN,I.M.BRERETON, JRNL AUTH 2 P.A.KROON,R.SMITH JRNL TITL NMR STRUCTURE OF A CONCATEMER OF THE FIRST AND SECOND JRNL TITL 2 LIGAND-BINDING MODULES OF THE HUMAN LOW-DENSITY LIPOPROTEIN JRNL TITL 3 RECEPTOR. JRNL REF PROTEIN SCI. V. 9 1282 2000 JRNL REFN ISSN 0961-8368 JRNL PMID 10933493 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.R.ATKINS,I.M.BRERETON,P.A.KROON,H.T.LEE,R.SMITH REMARK 1 TITL CALCIUM IS ESSENTIAL FOR THE STRUCTURAL INTEGRITY OF THE REMARK 1 TITL 2 CYSTEINE-RICH, LIGAND-BINDING REPEAT OF THE LOW-DENSITY REMARK 1 TITL 3 LIPOPROTEIN RECEPTOR REMARK 1 REF BIOCHEMISTRY V. 37 1662 1998 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI972529N REMARK 1 REFERENCE 2 REMARK 1 AUTH S.BIERI,A.R.ATKINS,H.T.LEE,D.J.WINZOR,R.SMITH,P.A.KROON REMARK 1 TITL FOLDING, CALCIUM BINDING, AND STRUCTURAL CHARACTERIZATION OF REMARK 1 TITL 2 A CONCATEMER OF THE FIRST AND SECOND LIGAND-BINDING MODULES REMARK 1 TITL 3 OF THE LOW-DENSITY LIPOPROTEIN RECEPTOR REMARK 1 REF BIOCHEMISTRY V. 37 10994 1998 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI980452C REMARK 1 REFERENCE 3 REMARK 1 AUTH N.L.DALY,M.J.SCANLON,J.T.DJORDJEVIC,P.A.KROON,R.SMITH REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF A CYSTEINE-RICH REPEAT FROM REMARK 1 TITL 2 THE LOW-DENSITY LIPOPROTEIN RECEPTOR REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 92 6334 1995 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 4 REMARK 1 AUTH N.L.DALY,J.T.DJORDJEVIC,P.A.KROON,R.SMITH REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE SECOND CYSTEINE-RICH REMARK 1 TITL 2 REPEAT FROM THE HUMAN LOW-DENSITY LIPOPROTEIN RECEPTOR REMARK 1 REF BIOCHEMISTRY V. 34 14474 1995 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2, X-PLOR 3.85 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 NMR INPUTS: NOE TOTAL 889: 286 INTRA, 273 SEQUENTIAL, 184 MEDIUM, REMARK 3 146 LONG RANGE; REMARK 3 OTHERS: 32 DIHEDRAL RESTRAINTS, 13 H-BONDS, 12 CALCIUM COORDINATION REMARK 4 REMARK 4 1F5Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-00. REMARK 100 THE DEPOSITION ID IS D_1000011283. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 0.045 REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 1 MM LB1-2, 15 MM CACL2, PH 5.5; REMARK 210 1 MM LB1-2, 15 MM CACL2, PH 5.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-TOCSY; DQF-COSY; 2D NOESY; E REMARK 210 -COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.4, DYANA 1.5, MOLMOL 2.6 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (DYANA) REMARK 210 FOLLOWED BY SIMULATED ANNEALING REMARK 210 AND MOLECULAR DYNAMICS (X-PLOR) REMARK 210 FOR CALCIUM COORDINATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES 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 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 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 1 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 1 CYS A 27 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 1 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 2 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES REMARK 500 2 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 2 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 3 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES REMARK 500 3 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES REMARK 500 3 CYS A 27 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 3 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 3 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 4 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 4 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES REMARK 500 4 CYS A 49 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 4 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES REMARK 500 4 TRP A 68 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES REMARK 500 5 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 5 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES REMARK 500 5 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 5 TRP A 68 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES REMARK 500 5 ASP A 71 CB - CG - OD1 ANGL. DEV. = -9.2 DEGREES REMARK 500 6 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 6 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES REMARK 500 6 CYS A 27 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 6 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 6 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES REMARK 500 7 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 7 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES REMARK 500 7 CYS A 44 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 7 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES REMARK 500 7 TRP A 68 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES REMARK 500 7 ASP A 71 CB - CG - OD1 ANGL. DEV. = -9.4 DEGREES REMARK 500 8 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES REMARK 500 8 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 7.7 DEGREES REMARK 500 8 CYS A 27 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 8 TRP A 68 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES REMARK 500 8 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES REMARK 500 8 TRP A 68 NE1 - CE2 - CZ2 ANGL. DEV. = 7.3 DEGREES REMARK 500 8 ASP A 71 CB - CG - OD1 ANGL. DEV. = -9.5 DEGREES REMARK 500 8 CYS A 76 CA - CB - SG ANGL. DEV. = 12.0 DEGREES REMARK 500 9 CYS A 15 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 9 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.1 DEGREES REMARK 500 9 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES REMARK 500 9 CYS A 27 CA - CB - SG ANGL. DEV. = 9.6 DEGREES REMARK 500 9 CYS A 44 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 9 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 9 TRP A 68 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES REMARK 500 9 TRP A 68 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES REMARK 500 10 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 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 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 2 -48.98 -143.90 REMARK 500 1 VAL A 4 163.36 44.91 REMARK 500 1 GLU A 9 42.41 -148.75 REMARK 500 1 ARG A 10 -118.35 -136.74 REMARK 500 1 ASP A 35 -55.51 -130.46 REMARK 500 1 SER A 40 38.04 -87.97 REMARK 500 1 GLN A 41 18.49 52.44 REMARK 500 1 THR A 43 46.26 -155.34 REMARK 500 1 SER A 46 -166.66 -101.17 REMARK 500 1 VAL A 47 58.94 34.12 REMARK 500 1 THR A 48 83.82 56.42 REMARK 500 1 LYS A 50 90.41 -161.89 REMARK 500 1 SER A 51 45.13 -167.56 REMARK 500 1 SER A 80 7.90 -62.38 REMARK 500 1 GLU A 82 -51.88 -158.90 REMARK 500 2 SER A 2 -48.22 -140.85 REMARK 500 2 ALA A 3 31.55 -86.54 REMARK 500 2 ARG A 7 -158.80 -98.08 REMARK 500 2 GLU A 9 43.94 -147.63 REMARK 500 2 ARG A 10 -119.92 -140.68 REMARK 500 2 ASP A 35 -56.56 -129.14 REMARK 500 2 SER A 40 32.74 -92.25 REMARK 500 2 THR A 43 40.69 -145.48 REMARK 500 2 LEU A 45 29.82 -78.26 REMARK 500 2 SER A 46 -102.14 -135.50 REMARK 500 2 THR A 48 56.56 33.49 REMARK 500 2 LYS A 50 77.57 -166.25 REMARK 500 2 SER A 51 41.90 -153.49 REMARK 500 2 PHE A 67 -9.73 -56.12 REMARK 500 2 CYS A 70 39.33 38.32 REMARK 500 2 GLU A 82 -62.20 -131.72 REMARK 500 3 ALA A 3 116.34 63.89 REMARK 500 3 VAL A 4 154.91 -46.63 REMARK 500 3 GLU A 9 43.73 -149.26 REMARK 500 3 ARG A 10 -118.84 -138.01 REMARK 500 3 ASP A 35 -54.52 -130.20 REMARK 500 3 SER A 40 41.51 -89.23 REMARK 500 3 GLN A 41 27.43 46.71 REMARK 500 3 THR A 43 22.00 -152.73 REMARK 500 3 SER A 46 -86.32 -126.87 REMARK 500 3 LYS A 50 73.41 -168.38 REMARK 500 3 SER A 51 44.40 -150.80 REMARK 500 3 ASN A 61 64.40 -109.83 REMARK 500 3 GLN A 66 -35.54 -25.81 REMARK 500 3 SER A 80 31.90 -77.98 REMARK 500 3 GLU A 82 -60.21 -131.52 REMARK 500 4 ASP A 6 -164.97 -74.39 REMARK 500 4 GLU A 9 43.56 -147.82 REMARK 500 4 ARG A 10 -117.14 -139.04 REMARK 500 4 ASP A 35 -53.61 -132.50 REMARK 500 REMARK 500 THIS ENTRY HAS 291 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 86 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TRP A 25 O REMARK 620 2 CYS A 27 N 81.9 REMARK 620 3 ASP A 28 OD1 69.3 103.3 REMARK 620 4 SER A 30 O 116.1 146.5 62.5 REMARK 620 5 GLU A 32 OE1 59.4 141.3 66.2 64.1 REMARK 620 6 ASP A 38 O 114.0 58.8 159.6 126.0 133.6 REMARK 620 7 ASP A 38 OD1 103.3 130.4 124.9 75.3 64.1 74.9 REMARK 620 8 GLU A 39 OE1 136.8 86.6 73.3 60.7 121.8 94.4 115.6 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 87 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TRP A 68 O REMARK 620 2 ASP A 71 OD2 91.1 REMARK 620 3 GLN A 73 O 155.2 95.5 REMARK 620 4 ASP A 75 OD2 135.4 113.3 62.4 REMARK 620 5 ASP A 81 OD2 84.0 169.5 92.8 65.3 REMARK 620 6 GLU A 82 OE1 97.9 129.7 59.9 94.0 60.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 86 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 87 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LDR RELATED DB: PDB REMARK 900 NMR STRUCTURE OF LB2 REMARK 900 RELATED ID: 1LDL RELATED DB: PDB REMARK 900 NMR STRUCTURE OF LB1 REMARK 900 RELATED ID: 1AJJ RELATED DB: PDB REMARK 900 X-RAY STRUCTURE OF LB5 DBREF 1F5Y A 3 85 UNP P01130 LDLR_HUMAN 22 104 SEQADV 1F5Y GLY A 1 UNP P01130 CLONING ARTIFACT SEQADV 1F5Y SER A 2 UNP P01130 CLONING ARTIFACT SEQRES 1 A 85 GLY SER ALA VAL GLY ASP ARG CYS GLU ARG ASN GLU PHE SEQRES 2 A 85 GLN CYS GLN ASP GLY LYS CYS ILE SER TYR LYS TRP VAL SEQRES 3 A 85 CYS ASP GLY SER ALA GLU CYS GLN ASP GLY SER ASP GLU SEQRES 4 A 85 SER GLN GLU THR CYS LEU SER VAL THR CYS LYS SER GLY SEQRES 5 A 85 ASP PHE SER CYS GLY GLY ARG VAL ASN ARG CYS ILE PRO SEQRES 6 A 85 GLN PHE TRP ARG CYS ASP GLY GLN VAL ASP CYS ASP ASN SEQRES 7 A 85 GLY SER ASP GLU GLN GLY CYS HET CA A 86 1 HET CA A 87 1 HETNAM CA CALCIUM ION FORMUL 2 CA 2(CA 2+) HELIX 1 1 TYR A 23 TRP A 25 5 3 HELIX 2 2 GLN A 66 TRP A 68 5 3 SHEET 1 A 2 PHE A 13 GLN A 14 0 SHEET 2 A 2 CYS A 20 ILE A 21 -1 N ILE A 21 O PHE A 13 SHEET 1 B 2 PHE A 54 SER A 55 0 SHEET 2 B 2 CYS A 63 ILE A 64 -1 O ILE A 64 N PHE A 54 SSBOND 1 CYS A 8 CYS A 20 1555 1555 2.02 SSBOND 2 CYS A 15 CYS A 33 1555 1555 2.02 SSBOND 3 CYS A 27 CYS A 44 1555 1555 2.02 SSBOND 4 CYS A 49 CYS A 63 1555 1555 2.02 SSBOND 5 CYS A 56 CYS A 76 1555 1555 2.02 SSBOND 6 CYS A 70 CYS A 85 1555 1555 2.02 LINK O TRP A 25 CA CA A 86 1555 1555 2.67 LINK N CYS A 27 CA CA A 86 1555 1555 2.90 LINK OD1 ASP A 28 CA CA A 86 1555 1555 2.66 LINK O SER A 30 CA CA A 86 1555 1555 2.62 LINK OE1 GLU A 32 CA CA A 86 1555 1555 2.67 LINK O ASP A 38 CA CA A 86 1555 1555 3.09 LINK OD1 ASP A 38 CA CA A 86 1555 1555 2.68 LINK OE1 GLU A 39 CA CA A 86 1555 1555 2.70 LINK O TRP A 68 CA CA A 87 1555 1555 2.66 LINK OD2 ASP A 71 CA CA A 87 1555 1555 2.72 LINK O GLN A 73 CA CA A 87 1555 1555 2.65 LINK OD2 ASP A 75 CA CA A 87 1555 1555 2.66 LINK OD2 ASP A 81 CA CA A 87 1555 1555 2.72 LINK OE1 GLU A 82 CA CA A 87 1555 1555 2.66 SITE 1 AC1 8 TRP A 25 VAL A 26 CYS A 27 ASP A 28 SITE 2 AC1 8 SER A 30 GLU A 32 ASP A 38 GLU A 39 SITE 1 AC2 6 TRP A 68 ASP A 71 GLN A 73 ASP A 75 SITE 2 AC2 6 ASP A 81 GLU A 82 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