Header list of 2cnp.pdb file
Complete list - r 9 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 07-JAN-99 2CNP TITLE HIGH RESOLUTION SOLUTION STRUCTURE OF APO RABBIT CALCYCLIN, NMR, 22 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALCYCLIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: 2A9, CACY, S100A6, PRA; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_COMMON: RABBIT; SOURCE 4 ORGANISM_TAXID: 9986; SOURCE 5 ORGAN: LUNG; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET 1120 KEYWDS CALCIUM-BINDING PROTEIN, EF-HAND, S-100 PROTEIN, SIGNAL TRANSDUCTION EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR L.MALER,B.C.M.POTTS,W.J.CHAZIN REVDAT 3 09-MAR-22 2CNP 1 REMARK REVDAT 2 24-FEB-09 2CNP 1 VERSN REVDAT 1 22-JUL-99 2CNP 0 JRNL AUTH L.MALER,B.C.POTTS,W.J.CHAZIN JRNL TITL HIGH RESOLUTION SOLUTION STRUCTURE OF APO CALCYCLIN AND JRNL TITL 2 STRUCTURAL VARIATIONS IN THE S100 FAMILY OF CALCIUM-BINDING JRNL TITL 3 PROTEINS. JRNL REF J.BIOMOL.NMR V. 13 233 1999 JRNL REFN ISSN 0925-2738 JRNL PMID 10212984 JRNL DOI 10.1023/A:1008315517955 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.C.POTTS,G.CARLSTROM,K.OKAZAKI,H.HIDAKA,W.J.CHAZIN REMARK 1 TITL 1H NMR ASSIGNMENTS OF APO CALCYCLIN AND COMPARATIVE REMARK 1 TITL 2 STRUCTURAL ANALYSIS WITH CALBINDIN D9K AND S100 BETA REMARK 1 REF PROTEIN SCI. V. 5 2162 1996 REMARK 1 REFN ISSN 0961-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.C.POTTS,J.SMITH,M.AKKE,T.J.MACKE,K.OKAZAKI,H.HIDAKA, REMARK 1 AUTH 2 D.A.CASE,W.J.CHAZIN REMARK 1 TITL THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD REMARK 1 TITL 2 FOR S100 CA(2+)-BINDING PROTEINS REMARK 1 REF NAT.STRUCT.BIOL. V. 2 790 1995 REMARK 1 REFN ISSN 1072-8368 REMARK 1 REFERENCE 3 REMARK 1 AUTH B.C.POTTS,J.SMITH,M.AKKE,T.J.MACKE,K.OKAZAKI,H.HIDAKA, REMARK 1 AUTH 2 D.A.CASE,W.J.CHAZIN REMARK 1 TITL ERRATUM. THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL REMARK 1 TITL 2 HOMODIMERIC FOLD FOR S100 CA(2+)-BINDING PROTEINS REMARK 1 REF NAT.STRUCT.BIOL. V. 2 912 1995 REMARK 1 REFN ISSN 1072-8368 REMARK 1 REFERENCE 4 REMARK 1 AUTH H.TOKUMITSU,R.KOBAYASHI,H.HIDAKA REMARK 1 TITL A CALCIUM-BINDING PROTEIN FROM RABBIT LUNG CYTOSOL REMARK 1 TITL 2 IDENTIFIED AS THE PRODUCT OF GROWTH-REGULATED GENE (2A9) AND REMARK 1 TITL 3 ITS BINDING PROTEINS REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 288 202 1991 REMARK 1 REFN ISSN 0003-9861 REMARK 1 REFERENCE 5 REMARK 1 AUTH H.TOKUMITSU,R.KOBAYASHI,H.HIDAKA REMARK 1 TITL A CALCIUM-BINDING PROTEIN FROM RABBIT LUNG CYTOSOL REMARK 1 TITL 2 IDENTIFIED AS THE PRODUCT OF GROWTH-REGULATED GENE (2A9) AND REMARK 1 TITL 3 ITS BINDING PROTEINS REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 291 401 1995 REMARK 1 REFN ISSN 0003-9861 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED USING REMARK 3 DIANA, FOLLOWED BY RESTRAINED MOLECULAR DYNAMICS ANNEALING REMARK 3 EMPLOYING THE FULL AMBER 4.1 FORCE FIELD TO CREATE MONOMER REMARK 3 STRUCTURES. THE DIMER WAS CREATED BY DOCKING TWO COPIES OF A REMARK 3 MONOMER AND FURTHER ANNEALING, ALL USING RESTRAINED MOLECULAR REMARK 3 DYNAMICS. REMARK 4 REMARK 4 2CNP 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_1000177936. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D/4D NOESY; SEE MANUSCRIPT. REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AMX; DMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA, AMBER 4.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY VARIABLE REMARK 210 TARGET FUNCTION ALGORITHM, REMARK 210 FOLLOWED BY RESTRAINED MOLECULAR REMARK 210 DYNAMICS SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 112 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : DEFINED THE MINIMAL NUMBER OF REMARK 210 CONFORMERS NEEDED TO REPRESENT REMARK 210 THE SRUCTURE. THE MEMBERS OF THE REMARK 210 ENSEMBLE WERE CHOSEN BASED ON A REMARK 210 COMBINATION OF LEAST RESTRAINT REMARK 210 VIOLATION ENERGY AND MOLECULAR REMARK 210 ENERGIES. REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: CHEMICAL SHIFT ASSIGNMENTS WERE MADE BASED ON TRIPLE REMARK 210 -RESONANCE EXPERIMENTS. DISTANCE CONTRAINTS WERE GENERATED FROM REMARK 210 2D HOMONUCLEAR NOESY, 3D 13C-NOESY-HSQC, 4D 13C/13C-NOESY-HMQC- REMARK 210 NOESY, 2D AND 3D 13C-SELECT, 13C-FILTERED NOESY. TORSION ANGLE REMARK 210 CONSTRAINTS WERE GENERATED FROM HACAHB-COSY, HNHA, HSQC AND REMARK 210 NOESY EXPERIMENTS. 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 TYR B 84 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 2 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 2 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 3 TYR B 84 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 4 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 4 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 5 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 5 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 6 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 7 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 7 TYR B 84 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 9 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 10 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 11 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 13 TYR B 84 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 14 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 14 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 16 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 17 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 18 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 19 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 19 TYR B 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 20 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 21 TYR B 84 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES 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 26 5.02 -66.31 REMARK 500 1 LYS A 31 -64.64 -18.61 REMARK 500 1 LYS A 47 92.69 -33.15 REMARK 500 1 GLN A 49 -78.00 61.94 REMARK 500 1 ASP A 50 -47.30 -168.11 REMARK 500 1 LYS A 64 -72.98 48.19 REMARK 500 1 ASP A 65 26.90 -143.37 REMARK 500 1 LYS B 26 12.18 -69.34 REMARK 500 1 LYS B 31 -68.86 -19.52 REMARK 500 1 ILE B 44 -65.08 -92.68 REMARK 500 1 SER B 46 75.74 -67.30 REMARK 500 1 LYS B 47 93.28 -39.62 REMARK 500 1 LYS B 64 -80.98 62.69 REMARK 500 1 ASP B 65 36.80 -153.49 REMARK 500 2 LYS A 26 8.62 -69.62 REMARK 500 2 LEU A 42 61.93 -117.02 REMARK 500 2 THR A 43 -72.73 -34.89 REMARK 500 2 ILE A 44 -67.22 64.44 REMARK 500 2 SER A 46 74.81 -68.14 REMARK 500 2 LYS A 47 92.67 -34.69 REMARK 500 2 LEU A 48 109.77 -59.78 REMARK 500 2 GLN A 49 -77.36 63.12 REMARK 500 2 ASP A 50 -47.43 -167.93 REMARK 500 2 ASN A 63 37.33 -93.05 REMARK 500 2 TYR B 19 -60.89 -101.96 REMARK 500 2 ILE B 44 76.94 -105.61 REMARK 500 2 SER B 46 80.40 -66.96 REMARK 500 2 LYS B 47 92.94 -46.95 REMARK 500 2 ASP B 50 -51.16 -19.96 REMARK 500 2 ALA B 51 -60.97 -29.84 REMARK 500 2 LYS B 64 -87.56 61.84 REMARK 500 2 ASP B 65 41.07 -150.82 REMARK 500 3 LEU A 42 60.57 -110.70 REMARK 500 3 ILE A 44 -64.13 61.40 REMARK 500 3 SER A 46 74.88 -68.13 REMARK 500 3 LYS A 47 93.75 -44.21 REMARK 500 3 ALA A 51 -54.89 -29.27 REMARK 500 3 LYS A 64 -72.82 62.44 REMARK 500 3 SER B 46 79.32 -66.05 REMARK 500 3 LYS B 47 93.15 -42.40 REMARK 500 3 ALA B 51 -59.69 -29.84 REMARK 500 4 LEU A 37 -75.26 -48.41 REMARK 500 4 LEU A 42 62.25 -119.28 REMARK 500 4 THR A 43 53.47 -69.23 REMARK 500 4 LEU A 48 77.48 -66.81 REMARK 500 4 GLN A 49 151.01 83.09 REMARK 500 4 ALA A 51 -60.39 -29.84 REMARK 500 4 ASP A 65 -2.60 69.41 REMARK 500 4 SER B 3 150.43 -45.71 REMARK 500 4 LYS B 22 -44.94 -146.47 REMARK 500 REMARK 500 THIS ENTRY HAS 300 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 TYR A 84 0.12 SIDE CHAIN REMARK 500 1 TYR B 84 0.14 SIDE CHAIN REMARK 500 2 HIS A 27 0.08 SIDE CHAIN REMARK 500 2 TYR A 84 0.13 SIDE CHAIN REMARK 500 2 TYR B 84 0.08 SIDE CHAIN REMARK 500 3 ARG A 62 0.11 SIDE CHAIN REMARK 500 3 TYR A 84 0.11 SIDE CHAIN REMARK 500 3 TYR B 84 0.09 SIDE CHAIN REMARK 500 4 TYR A 73 0.07 SIDE CHAIN REMARK 500 4 TYR A 84 0.10 SIDE CHAIN REMARK 500 4 TYR B 84 0.10 SIDE CHAIN REMARK 500 5 PHE A 76 0.07 SIDE CHAIN REMARK 500 5 TYR A 84 0.11 SIDE CHAIN REMARK 500 5 TYR B 84 0.10 SIDE CHAIN REMARK 500 6 TYR A 84 0.11 SIDE CHAIN REMARK 500 6 TYR B 19 0.09 SIDE CHAIN REMARK 500 6 TYR B 84 0.12 SIDE CHAIN REMARK 500 7 TYR A 84 0.13 SIDE CHAIN REMARK 500 7 TYR B 84 0.12 SIDE CHAIN REMARK 500 8 TYR A 84 0.09 SIDE CHAIN REMARK 500 8 TYR B 84 0.08 SIDE CHAIN REMARK 500 9 PHE A 76 0.08 SIDE CHAIN REMARK 500 9 TYR A 84 0.09 SIDE CHAIN REMARK 500 9 TYR B 84 0.10 SIDE CHAIN REMARK 500 10 TYR A 84 0.09 SIDE CHAIN REMARK 500 11 TYR A 84 0.11 SIDE CHAIN REMARK 500 11 TYR B 84 0.10 SIDE CHAIN REMARK 500 12 PHE A 76 0.10 SIDE CHAIN REMARK 500 12 TYR A 84 0.09 SIDE CHAIN REMARK 500 12 TYR B 84 0.06 SIDE CHAIN REMARK 500 13 TYR A 19 0.09 SIDE CHAIN REMARK 500 13 TYR A 84 0.07 SIDE CHAIN REMARK 500 13 TYR B 84 0.11 SIDE CHAIN REMARK 500 14 TYR A 84 0.10 SIDE CHAIN REMARK 500 14 TYR B 84 0.06 SIDE CHAIN REMARK 500 15 TYR A 84 0.09 SIDE CHAIN REMARK 500 15 TYR B 84 0.10 SIDE CHAIN REMARK 500 16 PHE A 76 0.09 SIDE CHAIN REMARK 500 16 TYR A 84 0.14 SIDE CHAIN REMARK 500 16 TYR B 84 0.09 SIDE CHAIN REMARK 500 17 TYR A 84 0.07 SIDE CHAIN REMARK 500 17 TYR B 84 0.09 SIDE CHAIN REMARK 500 18 TYR A 84 0.07 SIDE CHAIN REMARK 500 18 TYR B 84 0.10 SIDE CHAIN REMARK 500 19 TYR A 84 0.11 SIDE CHAIN REMARK 500 19 TYR B 19 0.10 SIDE CHAIN REMARK 500 20 PHE A 76 0.09 SIDE CHAIN REMARK 500 20 TYR A 84 0.12 SIDE CHAIN REMARK 500 20 TYR B 19 0.09 SIDE CHAIN REMARK 500 21 TYR A 84 0.08 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 53 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: L1A REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CALCIUM-BINDING LOOP 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: L1B REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CALCIUM-BINDING LOOP 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: L2A REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CALCIUM-BINDING LOOP 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: L2B REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CALCIUM-BINDING LOOP 2 DBREF 2CNP A 1 90 UNP P30801 S10A6_RABIT 1 90 DBREF 2CNP B 1 90 UNP P30801 S10A6_RABIT 1 90 SEQRES 1 A 90 MET ALA SER PRO LEU ASP GLN ALA ILE GLY LEU LEU ILE SEQRES 2 A 90 GLY ILE PHE HIS LYS TYR SER GLY LYS GLU GLY ASP LYS SEQRES 3 A 90 HIS THR LEU SER LYS LYS GLU LEU LYS GLU LEU ILE GLN SEQRES 4 A 90 LYS GLU LEU THR ILE GLY SER LYS LEU GLN ASP ALA GLU SEQRES 5 A 90 ILE VAL LYS LEU MET ASP ASP LEU ASP ARG ASN LYS ASP SEQRES 6 A 90 GLN GLU VAL ASN PHE GLN GLU TYR ILE THR PHE LEU GLY SEQRES 7 A 90 ALA LEU ALA MET ILE TYR ASN GLU ALA LEU LYS GLY SEQRES 1 B 90 MET ALA SER PRO LEU ASP GLN ALA ILE GLY LEU LEU ILE SEQRES 2 B 90 GLY ILE PHE HIS LYS TYR SER GLY LYS GLU GLY ASP LYS SEQRES 3 B 90 HIS THR LEU SER LYS LYS GLU LEU LYS GLU LEU ILE GLN SEQRES 4 B 90 LYS GLU LEU THR ILE GLY SER LYS LEU GLN ASP ALA GLU SEQRES 5 B 90 ILE VAL LYS LEU MET ASP ASP LEU ASP ARG ASN LYS ASP SEQRES 6 B 90 GLN GLU VAL ASN PHE GLN GLU TYR ILE THR PHE LEU GLY SEQRES 7 B 90 ALA LEU ALA MET ILE TYR ASN GLU ALA LEU LYS GLY HELIX 1 H1A SER A 3 LYS A 18 9 16 HELIX 2 H2A LYS A 31 LEU A 42 9 12 HELIX 3 H3A ASP A 50 ASN A 63 9 14 HELIX 4 H4A ASN A 69 ASN A 85 9 17 HELIX 5 H1B SER B 3 LYS B 18 9 16 HELIX 6 H2B LYS B 31 LEU B 42 9 12 HELIX 7 H3B ASP B 50 ASN B 63 9 14 HELIX 8 H4B ASN B 69 ASN B 85 9 17 SHEET 1 SA 2 THR A 28 SER A 30 0 SHEET 2 SA 2 GLU A 67 ASN A 69 -1 N VAL A 68 O LEU A 29 SHEET 1 SB 2 THR B 28 SER B 30 0 SHEET 2 SB 2 GLU B 67 ASN B 69 -1 N VAL B 68 O LEU B 29 SITE 1 L1A 14 SER A 20 GLY A 21 LYS A 22 GLU A 23 SITE 2 L1A 14 GLY A 24 ASP A 25 LYS A 26 HIS A 27 SITE 3 L1A 14 THR A 28 LEU A 29 SER A 30 LYS A 31 SITE 4 L1A 14 LYS A 32 GLU A 33 SITE 1 L1B 14 SER B 20 GLY B 21 LYS B 22 GLU B 23 SITE 2 L1B 14 GLY B 24 ASP B 25 LYS B 26 HIS B 27 SITE 3 L1B 14 THR B 28 LEU B 29 SER B 30 LYS B 31 SITE 4 L1B 14 LYS B 32 GLU B 33 SITE 1 L2A 12 ASP A 61 ARG A 62 ASN A 63 LYS A 64 SITE 2 L2A 12 ASP A 65 GLN A 66 GLU A 67 VAL A 68 SITE 3 L2A 12 ASN A 69 PHE A 70 GLN A 71 GLU A 72 SITE 1 L2B 12 ASP B 61 ARG B 62 ASN B 63 LYS B 64 SITE 2 L2B 12 ASP B 65 GLN B 66 GLU B 67 VAL B 68 SITE 3 L2B 12 ASN B 69 PHE B 70 GLN B 71 GLU B 72 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 - r 9 2 Bytes