Header list of 1aab.pdb file
Complete list - v 3 2 Bytes
HEADER DNA-BINDING 28-OCT-95 1AAB TITLE NMR STRUCTURE OF RAT HMG1 HMGA FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIGH MOBILITY GROUP PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FRAGMENT A (RESIDUES 1 - 83); COMPND 5 SYNONYM: HMGA DNA-BINDING HMG-BOX DOMAIN A OF RAT HMG1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 STRAIN: SPRAGUE-DAWLEY; SOURCE 6 TISSUE: LIVER; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: DE3; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-HMGACS KEYWDS HMG-BOX, DNA-BINDING EXPDTA SOLUTION NMR NUMMDL 33 AUTHOR C.H.HARDMAN,R.W.BROADHURST,A.R.C.RAINE,K.D.GRASSER,J.O.THOMAS, AUTHOR 2 E.D.LAUE REVDAT 3 03-NOV-21 1AAB 1 REMARK SEQADV REVDAT 2 24-FEB-09 1AAB 1 VERSN REVDAT 1 08-MAR-96 1AAB 0 JRNL AUTH C.H.HARDMAN,R.W.BROADHURST,A.R.RAINE,K.D.GRASSER,J.O.THOMAS, JRNL AUTH 2 E.D.LAUE JRNL TITL STRUCTURE OF THE A-DOMAIN OF HMG1 AND ITS INTERACTION WITH JRNL TITL 2 DNA AS STUDIED BY HETERONUCLEAR THREE- AND FOUR-DIMENSIONAL JRNL TITL 3 NMR SPECTROSCOPY. JRNL REF BIOCHEMISTRY V. 34 16596 1995 JRNL REFN ISSN 0006-2960 JRNL PMID 8527432 JRNL DOI 10.1021/BI00051A007 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.W.BROADHURST,C.H.HARDMAN,J.O.THOMAS,E.D.LAUE REMARK 1 TITL BACKBONE DYNAMICS OF THE A DOMAIN OF HMG1 AS STUDIED BY 15N REMARK 1 TITL 2 NMR SPECTROSCOPY REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1AAB 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_1000170588. 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 : 33 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: 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 H SER A 38 H GLU A 39 1.35 REMARK 500 REMARK 500 REMARK: NULL 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 1 HIS A 26 CG HIS A 26 ND1 -0.122 REMARK 500 1 HIS A 30 CG HIS A 30 ND1 -0.122 REMARK 500 1 TRP A 48 CG TRP A 48 CD2 -0.121 REMARK 500 2 HIS A 26 CG HIS A 26 ND1 -0.120 REMARK 500 2 HIS A 30 CG HIS A 30 ND1 -0.122 REMARK 500 2 TRP A 48 CG TRP A 48 CD2 -0.120 REMARK 500 3 HIS A 26 CG HIS A 26 ND1 -0.115 REMARK 500 3 HIS A 30 CG HIS A 30 ND1 -0.122 REMARK 500 3 TRP A 48 CG TRP A 48 CD2 -0.124 REMARK 500 4 HIS A 26 CG HIS A 26 ND1 -0.118 REMARK 500 4 HIS A 30 CG HIS A 30 ND1 -0.120 REMARK 500 4 TRP A 48 CG TRP A 48 CD2 -0.120 REMARK 500 5 HIS A 26 CG HIS A 26 ND1 -0.119 REMARK 500 5 HIS A 30 CG HIS A 30 ND1 -0.119 REMARK 500 5 TRP A 48 CG TRP A 48 CD2 -0.122 REMARK 500 6 HIS A 26 CG HIS A 26 ND1 -0.117 REMARK 500 6 HIS A 30 CG HIS A 30 ND1 -0.122 REMARK 500 6 TRP A 48 CG TRP A 48 CD2 -0.121 REMARK 500 7 HIS A 26 CG HIS A 26 ND1 -0.120 REMARK 500 7 HIS A 30 CG HIS A 30 ND1 -0.121 REMARK 500 7 TRP A 48 CG TRP A 48 CD2 -0.124 REMARK 500 8 HIS A 26 CG HIS A 26 ND1 -0.121 REMARK 500 8 HIS A 30 CG HIS A 30 ND1 -0.121 REMARK 500 8 TRP A 48 CG TRP A 48 CD2 -0.119 REMARK 500 9 HIS A 26 CG HIS A 26 ND1 -0.125 REMARK 500 9 HIS A 30 CG HIS A 30 ND1 -0.119 REMARK 500 9 TRP A 48 CG TRP A 48 CD2 -0.119 REMARK 500 10 HIS A 26 CG HIS A 26 ND1 -0.123 REMARK 500 10 HIS A 30 CG HIS A 30 ND1 -0.120 REMARK 500 10 TRP A 48 CG TRP A 48 CD2 -0.116 REMARK 500 11 HIS A 26 CG HIS A 26 ND1 -0.121 REMARK 500 11 HIS A 30 CG HIS A 30 ND1 -0.121 REMARK 500 11 TRP A 48 CG TRP A 48 CD2 -0.123 REMARK 500 12 HIS A 26 CG HIS A 26 ND1 -0.119 REMARK 500 12 HIS A 30 CG HIS A 30 ND1 -0.120 REMARK 500 12 TRP A 48 CG TRP A 48 CD2 -0.119 REMARK 500 13 HIS A 26 CG HIS A 26 ND1 -0.123 REMARK 500 13 HIS A 30 CG HIS A 30 ND1 -0.121 REMARK 500 13 TRP A 48 CG TRP A 48 CD2 -0.120 REMARK 500 14 HIS A 26 CG HIS A 26 ND1 -0.124 REMARK 500 14 HIS A 30 CG HIS A 30 ND1 -0.119 REMARK 500 14 TRP A 48 CG TRP A 48 CD2 -0.120 REMARK 500 15 HIS A 26 CG HIS A 26 ND1 -0.119 REMARK 500 15 HIS A 30 CG HIS A 30 ND1 -0.117 REMARK 500 15 TRP A 48 CG TRP A 48 CD2 -0.119 REMARK 500 16 HIS A 26 CG HIS A 26 ND1 -0.124 REMARK 500 16 HIS A 30 CG HIS A 30 ND1 -0.120 REMARK 500 16 TRP A 48 CG TRP A 48 CD2 -0.117 REMARK 500 17 HIS A 26 CG HIS A 26 ND1 -0.123 REMARK 500 17 HIS A 30 CG HIS A 30 ND1 -0.120 REMARK 500 REMARK 500 THIS ENTRY HAS 99 BOND DEVIATIONS. 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 48 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 1 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 1 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES REMARK 500 1 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 2 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 2 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES REMARK 500 2 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 3 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES REMARK 500 3 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 3 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES REMARK 500 3 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 4 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 4 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES REMARK 500 4 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES REMARK 500 4 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 5 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES REMARK 500 5 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES REMARK 500 5 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 6 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 6 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES REMARK 500 6 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES REMARK 500 7 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 7 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 7 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.0 DEGREES REMARK 500 7 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 8 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES REMARK 500 8 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 9 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES REMARK 500 9 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES REMARK 500 9 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 10 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 10 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 10 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES REMARK 500 10 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 11 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 11 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES REMARK 500 11 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES REMARK 500 11 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 12 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 12 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES REMARK 500 12 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES REMARK 500 12 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES REMARK 500 13 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES REMARK 500 13 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES REMARK 500 13 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 14 TRP A 48 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES REMARK 500 14 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 14 TRP A 48 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES REMARK 500 14 TRP A 48 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 15 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 111 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 LYS A 2 55.78 -148.13 REMARK 500 1 LYS A 6 -1.70 53.48 REMARK 500 1 PRO A 8 -171.99 -61.84 REMARK 500 1 ARG A 9 38.82 -152.08 REMARK 500 1 LYS A 11 124.59 -37.55 REMARK 500 1 LYS A 29 46.45 -163.66 REMARK 500 1 HIS A 30 68.75 -151.80 REMARK 500 1 SER A 34 -12.05 64.03 REMARK 500 1 VAL A 35 84.84 45.89 REMARK 500 1 SER A 38 6.95 -169.34 REMARK 500 1 GLU A 39 -22.15 -150.32 REMARK 500 1 LYS A 49 -14.16 -49.54 REMARK 500 1 MET A 51 174.14 -56.25 REMARK 500 1 THR A 76 -6.99 -146.71 REMARK 500 1 TYR A 77 -94.32 -70.96 REMARK 500 1 ILE A 78 95.08 47.38 REMARK 500 1 PRO A 80 -158.47 -66.22 REMARK 500 1 LYS A 81 41.24 -79.38 REMARK 500 2 PRO A 5 -84.85 -60.49 REMARK 500 2 LYS A 11 104.54 -50.66 REMARK 500 2 SER A 34 -5.56 65.51 REMARK 500 2 VAL A 35 87.21 47.96 REMARK 500 2 PHE A 37 -20.80 71.14 REMARK 500 2 GLU A 39 63.27 -151.34 REMARK 500 2 PHE A 40 -52.93 -157.11 REMARK 500 2 LYS A 49 -15.96 -49.21 REMARK 500 2 MET A 51 172.43 -55.88 REMARK 500 2 TYR A 77 -100.29 -76.96 REMARK 500 2 ILE A 78 94.07 46.51 REMARK 500 2 PRO A 80 -162.35 -65.06 REMARK 500 2 LYS A 81 81.73 -67.63 REMARK 500 3 PRO A 5 103.47 -57.80 REMARK 500 3 LYS A 6 44.98 39.19 REMARK 500 3 LYS A 11 36.04 38.70 REMARK 500 3 LYS A 27 9.55 -69.17 REMARK 500 3 LYS A 28 -32.63 -136.19 REMARK 500 3 SER A 34 -5.16 61.36 REMARK 500 3 VAL A 35 87.12 47.37 REMARK 500 3 SER A 38 9.77 -153.57 REMARK 500 3 GLU A 39 -24.58 -152.06 REMARK 500 3 LYS A 49 -18.43 -48.50 REMARK 500 3 MET A 51 174.61 -56.04 REMARK 500 3 TYR A 77 -90.88 -77.83 REMARK 500 3 ILE A 78 93.21 49.45 REMARK 500 3 PRO A 80 -156.76 -74.76 REMARK 500 3 LYS A 81 92.02 -55.97 REMARK 500 4 LYS A 2 -149.81 -73.20 REMARK 500 4 ASP A 4 75.36 -155.73 REMARK 500 4 PRO A 8 88.18 -67.11 REMARK 500 4 LYS A 29 40.68 -157.95 REMARK 500 REMARK 500 THIS ENTRY HAS 524 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1AAB A 1 83 UNP P63159 HMG1_RAT 1 83 SEQADV 1AAB SER A 22 UNP P63159 CYS 22 ENGINEERED MUTATION SEQRES 1 A 83 GLY LYS GLY ASP PRO LYS LYS PRO ARG GLY LYS MET SER SEQRES 2 A 83 SER TYR ALA PHE PHE VAL GLN THR SER ARG GLU GLU HIS SEQRES 3 A 83 LYS LYS LYS HIS PRO ASP ALA SER VAL ASN PHE SER GLU SEQRES 4 A 83 PHE SER LYS LYS CYS SER GLU ARG TRP LYS THR MET SER SEQRES 5 A 83 ALA LYS GLU LYS GLY LYS PHE GLU ASP MET ALA LYS ALA SEQRES 6 A 83 ASP LYS ALA ARG TYR GLU ARG GLU MET LYS THR TYR ILE SEQRES 7 A 83 PRO PRO LYS GLY GLU HELIX 1 H1 SER A 14 LYS A 28 1 15 HELIX 2 H2 SER A 38 THR A 50 1 13 HELIX 3 H3 ALA A 53 MET A 74 1 22 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 3 2 Bytes