Header list of 1mx7.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 01-OCT-02 1MX7
TITLE TWO HOMOLOGOUS RAT CELLULAR RETINOL-BINDING PROTEINS DIFFER IN LOCAL
TITLE 2 STRUCTURE AND FLEXIBILITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR RETINOL-BINDING PROTEIN I, APO;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: RBP1 OR RBP-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMON CRBP I
KEYWDS BETA-BARREL, HELIX-TURN-HELIX, VITAMIN A, RETINOL-BINDING, TRANSPORT,
KEYWDS 2 LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR J.LU,D.P.CISTOLA,E.LI
REVDAT 4 23-FEB-22 1MX7 1 REMARK
REVDAT 3 24-FEB-09 1MX7 1 VERSN
REVDAT 2 02-DEC-03 1MX7 1 DBREF
REVDAT 1 29-JUL-03 1MX7 0
JRNL AUTH J.LU,D.P.CISTOLA,E.LI
JRNL TITL TWO HOMOLOGOUS RAT CELLULAR RETINOL-BINDING PROTEINS DIFFER
JRNL TITL 2 IN LOCAL CONFORMATIONAL FLEXIBILITY.
JRNL REF J.MOL.BIOL. V. 330 799 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12850148
JRNL DOI 10.1016/S0022-2836(03)00629-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.LU,C.L.LIN,C.TANG,J.W.PONDER,J.L.KAO,D.P.CISTOLA,E.LI
REMARK 1 TITL BINDING OF RETINOL INDUCES CHANGES IN RAT CELLULAR
REMARK 1 TITL 2 RETINOL-BINDING PROTEIN II CONFORMATION AND BACKBONE
REMARK 1 TITL 3 DYNAMICS
REMARK 1 REF J.MOL.BIOL. V. 300 619 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.3883
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.LU,C.L.LIN,C.TANG,J.W.PONDER,J.L.F.KAO,D.P.CISTOLA,E.LI
REMARK 1 TITL THE STRUCTURE AND DYNAMICS OF RAT APO-CELLULAR
REMARK 1 TITL 2 RETINOL-BINDING PROTEIN II IN SOLUTION: COMPARISON WITH THE
REMARK 1 TITL 3 X-RAY STRUCTURE
REMARK 1 REF J.MOL.BIOL. V. 286 1179 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1999.2544
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.W.COWAN,M.E.NEWCOMER,T.A.JONES
REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC
REMARK 1 TITL 2 TRANSPORT PROTEINS. REFINEMENT OF P2 MYELIN PROTEIN AND THE
REMARK 1 TITL 3 STRUCTURE DETERMINATION AND REFINEMENT OF CELLULAR
REMARK 1 TITL 4 RETINOL-BINDING PROTEIN IN COMPLEX WITH ALL-TRANS-RETINOL
REMARK 1 REF J.MOL.BIOL. V. 230 1225 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1993.1238
REMARK 1 REFERENCE 4
REMARK 1 AUTH N.S.WINTER,J.M.BRATT,L.J.BANASZAK
REMARK 1 TITL CRYSTAL STRUCTURES OF HOLO AND APO-CELLULAR RETINOL-BINDING
REMARK 1 TITL 2 PROTEIN II
REMARK 1 REF J.MOL.BIOL. V. 230 1247 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1993.1239
REMARK 1 REFERENCE 5
REMARK 1 AUTH L.FRANZONI,C.LUCKE,C.PEREZ,D.CAVAZZINI,M.RADEMACHER,
REMARK 1 AUTH 2 C.LUDWIG,A.SPISNI,G.L.ROSSI,H.RUTERJANS
REMARK 1 TITL STRUCTURE AND BACKBONE DYNAMICS OF APO- AND HOLO-CELLULAR
REMARK 1 TITL 2 RETINAL-BINDING PROTEIN IN SOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 277 21983 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M201994200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, TINKER 3.3
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), PONDER, J.W. (TINKER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MX7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017272.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7.4; 6.5
REMARK 210 IONIC STRENGTH : 0.34; 0.34
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0MM LIGAND FREE CELLULAR
REMARK 210 RETINOL-BINDING PROTEIN I U-[99%
REMARK 210 15N, 99% 13C]; 20MM PHOSPHATE
REMARK 210 BUFFER, 50MM POTASSIUM CHLORIDE,
REMARK 210 0.05% SUDIUM AZIDE, 5MM BETA-
REMARK 210 MECAPTOETHANOL-D6; 95% H2O, 5%
REMARK 210 D2O; 1.0MM LIGAND FREE CELLULAR
REMARK 210 RETINOL-BINDING PROTEIN I U-[99%
REMARK 210 15N, 80% 2H]; 20MM PHOSPHATE
REMARK 210 BUFFER, 50MM POTASSIUM CHLORIDE,
REMARK 210 0.05% SUDIUM AZIDE, 5MM BETA-
REMARK 210 MECAPTOETHANOL-D6; 95% H2O, 5%
REMARK 210 D2O; 1.0MM LIGAND FREE CELLULAR
REMARK 210 RETINOL-BINDING PROTEIN I U-[99%
REMARK 210 15N]; 20MM PHOSPHATE BUFFER,
REMARK 210 50MM POTASSIUM CHLORIDE, 0.05%
REMARK 210 SUDIUM AZIDE, 5MM BETA-
REMARK 210 MECAPTOETHANOL-D6; 95% H2O, 5%
REMARK 210 D2O; 1.0MM LIGAND FREE CELLULAR
REMARK 210 RETINOL-BINDING PROTEIN I U-[99%
REMARK 210 15N, 99% 13C]; 20MM PHOSPHATE
REMARK 210 BUFFER, 50MM POTASSIUM CHLORIDE,
REMARK 210 0.05% SUDIUM AZIDE, 5MM BETA-
REMARK 210 MECAPTOETHANOL-D6; 99.5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1, FELIX 2000, TINKER 3.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: TRIPLE RESONANCE EXPERIMENTS FOR
REMARK 210 THE 1H, 15N AND 13C RESONANCE
REMARK 210 ASSIGNMENTS INCLUDED THE FOLLOWING:
REMARK 210 HNCO
REMARK 210 CBCACONNH
REMARK 210 HNCACB
REMARK 210 CBCACOCAHA
REMARK 210 HCCH-TOCSY
REMARK 210 15N-RESOLVED TOCSY-HSQC
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 PHE A 64 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 3 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 PRO A 1 N - CA - CB ANGL. DEV. = 8.4 DEGREES
REMARK 500 5 TYR A 60 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 5 TYR A 60 CB - CG - CD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 5 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 PRO A 1 CA - N - CD ANGL. DEV. = -9.1 DEGREES
REMARK 500 7 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 7 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 8 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 8 ARG A 120 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 9 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 TRP A 8 CD1 - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 10 TRP A 8 CE2 - CD2 - CG ANGL. DEV. = 5.2 DEGREES
REMARK 500 10 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 10 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 10 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 11 ASP A 89 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 11 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 12 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 12 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 12 ARG A 120 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 13 TYR A 7 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 13 TRP A 8 CB - CG - CD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 15 PHE A 16 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 15 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 15 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 15 TYR A 60 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 15 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 16 PRO A 1 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 16 TRP A 8 CG - CD2 - CE3 ANGL. DEV. = 6.0 DEGREES
REMARK 500 16 ARG A 30 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 16 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 16 TRP A 88 CG - CD2 - CE3 ANGL. DEV. = 6.2 DEGREES
REMARK 500 16 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 16 HIS A 134 CE1 - NE2 - CD2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 18 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 18 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 19 PRO A 1 N - CA - CB ANGL. DEV. = 7.7 DEGREES
REMARK 500 19 PHE A 16 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 19 ASP A 45 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 19 TRP A 88 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 20 PHE A 16 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 20 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 20 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 ASP A 3 89.46 25.62
REMARK 500 1 ASN A 5 104.77 -49.05
REMARK 500 1 ASN A 13 104.97 177.43
REMARK 500 1 ASN A 15 34.33 34.03
REMARK 500 1 ARG A 58 91.87 36.64
REMARK 500 1 TYR A 60 78.13 -102.01
REMARK 500 1 ASP A 78 34.34 28.50
REMARK 500 1 ASP A 79 81.13 -4.56
REMARK 500 1 ASP A 91 49.77 -97.99
REMARK 500 1 GLU A 100 -171.68 -64.96
REMARK 500 1 LYS A 101 162.49 74.97
REMARK 500 1 TRP A 109 157.53 176.99
REMARK 500 1 GLU A 111 58.99 -111.12
REMARK 500 1 ALA A 121 103.69 -169.34
REMARK 500 1 LYS A 132 109.88 -56.26
REMARK 500 1 VAL A 133 50.58 -103.42
REMARK 500 2 VAL A 2 -156.42 -111.08
REMARK 500 2 PHE A 4 -52.49 -20.52
REMARK 500 2 GLU A 14 -57.26 -124.13
REMARK 500 2 ASN A 15 51.07 -112.40
REMARK 500 2 ASP A 24 61.74 61.67
REMARK 500 2 VAL A 25 -150.11 -88.33
REMARK 500 2 PHE A 57 -135.07 -87.00
REMARK 500 2 GLU A 69 150.61 65.85
REMARK 500 2 ASP A 73 62.66 -150.02
REMARK 500 2 ASP A 78 -11.00 83.24
REMARK 500 2 ASP A 79 100.26 50.45
REMARK 500 2 GLU A 100 -176.12 58.72
REMARK 500 2 LYS A 101 175.58 60.81
REMARK 500 2 THR A 107 88.98 -153.54
REMARK 500 2 GLU A 111 71.85 -101.50
REMARK 500 2 HIS A 116 68.03 -115.18
REMARK 500 2 ALA A 121 116.60 -177.58
REMARK 500 3 VAL A 2 67.21 -106.21
REMARK 500 3 PHE A 4 -43.32 63.21
REMARK 500 3 ASN A 5 106.39 -40.25
REMARK 500 3 LEU A 11 -63.88 -126.12
REMARK 500 3 ASN A 15 16.47 54.85
REMARK 500 3 ASP A 45 -146.81 -145.40
REMARK 500 3 SER A 55 -139.88 -122.82
REMARK 500 3 THR A 56 -38.36 -139.10
REMARK 500 3 PHE A 57 -81.16 -54.76
REMARK 500 3 ASN A 59 85.31 56.83
REMARK 500 3 ASP A 73 -60.48 75.83
REMARK 500 3 ILE A 77 20.49 92.02
REMARK 500 3 ASP A 78 -33.84 143.32
REMARK 500 3 LYS A 81 118.74 88.56
REMARK 500 3 MET A 83 71.75 -119.09
REMARK 500 3 ASP A 91 25.88 -145.66
REMARK 500 3 LYS A 92 -157.11 -153.03
REMARK 500
REMARK 500 THIS ENTRY HAS 402 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MX8 RELATED DB: PDB
REMARK 900 SAME PROTEIN, COMPLEXED WITH RETINOL
DBREF 1MX7 A 1 134 UNP P02696 RET1_RAT 2 135
SEQRES 1 A 134 PRO VAL ASP PHE ASN GLY TYR TRP LYS MET LEU SER ASN
SEQRES 2 A 134 GLU ASN PHE GLU GLU TYR LEU ARG ALA LEU ASP VAL ASN
SEQRES 3 A 134 VAL ALA LEU ARG LYS ILE ALA ASN LEU LEU LYS PRO ASP
SEQRES 4 A 134 LYS GLU ILE VAL GLN ASP GLY ASP HIS MET ILE ILE ARG
SEQRES 5 A 134 THR LEU SER THR PHE ARG ASN TYR ILE MET ASP PHE GLN
SEQRES 6 A 134 VAL GLY LYS GLU PHE GLU GLU ASP LEU THR GLY ILE ASP
SEQRES 7 A 134 ASP ARG LYS CYS MET THR THR VAL SER TRP ASP GLY ASP
SEQRES 8 A 134 LYS LEU GLN CYS VAL GLN LYS GLY GLU LYS GLU GLY ARG
SEQRES 9 A 134 GLY TRP THR GLN TRP ILE GLU GLY ASP GLU LEU HIS LEU
SEQRES 10 A 134 GLU MET ARG ALA GLU GLY VAL THR CYS LYS GLN VAL PHE
SEQRES 11 A 134 LYS LYS VAL HIS
HELIX 1 A1 PHE A 16 ALA A 22 1 7
HELIX 2 A2 VAL A 27 ILE A 32 1 6
SHEET 1 B1 4 TYR A 7 GLU A 14 0
SHEET 2 B1 4 PRO A 38 ASP A 45 -1 N LYS A 40 O TRP A 8
SHEET 3 B1 4 HIS A 48 SER A 55 -1 O ILE A 50 N VAL A 43
SHEET 4 B1 4 ASN A 59 GLN A 65 -1 N PHE A 64 O MET A 49
SHEET 1 B2 6 LYS A 68 ASP A 73 0
SHEET 2 B2 6 CYS A 82 ASP A 89 -1 N THR A 84 O PHE A 70
SHEET 3 B2 6 LYS A 92 GLN A 97 -1 N GLN A 94 O SER A 87
SHEET 4 B2 6 ARG A 104 GLU A 111 -1 N GLN A 108 O LEU A 93
SHEET 5 B2 6 GLU A 114 ARG A 120 -1 N GLU A 118 O THR A 107
SHEET 6 B2 6 VAL A 124 LYS A 131 -1 N GLN A 128 O LEU A 117
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 23 2 Bytes