Header list of 2ch0.pdb file
Complete list - y 2 2 Bytes
HEADER NUCLEAR PROTEIN 10-MAR-06 2CH0
TITLE SOLUTION STRUCTURE OF THE HUMAN MAN1 C-TERMINAL DOMAIN (RESIDUES 655-
TITLE 2 775)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INNER NUCLEAR MEMBRANE PROTEIN MAN1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 655-775;
COMPND 5 SYNONYM: LEM DOMAIN CONTAINING PROTEIN 3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS MAN1, WINGED HELIX MOTIF, DNA, NUCLEAR PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.CAPUTO,J.COUPRIE,I.DUBAND-GOULET,F.LIN,S.BRAUD,M.GONDRY,H.J.WORMAN,
AUTHOR 2 B.GILQUIN,S.ZINN-JUSTIN
REVDAT 4 02-MAY-18 2CH0 1 JRNL REMARK
REVDAT 3 24-FEB-09 2CH0 1 VERSN
REVDAT 2 20-DEC-06 2CH0 1 JRNL
REVDAT 1 16-MAY-06 2CH0 0
JRNL AUTH S.CAPUTO,J.COUPRIE,I.DUBAND-GOULET,E.KONDE,F.LIN,S.BRAUD,
JRNL AUTH 2 M.GONDRY,B.GILQUIN,H.J.WORMAN,S.ZINN-JUSTIN
JRNL TITL THE CARBOXYL-TERMINAL NUCLEOPLASMIC REGION OF MAN1 EXHIBITS
JRNL TITL 2 A DNA BINDING WINGED HELIX DOMAIN.
JRNL REF J. BIOL. CHEM. V. 281 18208 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16648637
JRNL DOI 10.1074/JBC.M601980200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON A TOTAL OF
REMARK 3 1811 NOE-DERIVED CONSTRAINTS, 169 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 2CH0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1290027997.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.0; 303.0; 303.0; 303.0;
REMARK 210 303.0
REMARK 210 PH : 6.0; 6.0; 6.0; 6.0; 6.0
REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE, 150MM NACL; 50
REMARK 210 MM PHOSPHATE, 150MM NACL; 50 MM
REMARK 210 PHOSPHATE, 150MM NACL; 50 MM
REMARK 210 PHOSPHATE, 150MM NACL; 50 MM
REMARK 210 PHOSPHATE, 150MM NACL
REMARK 210 PRESSURE : NULL; NULL; NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N HSQC-NOESY; 15N HSQC- NOESY;
REMARK 210 13C HSQC-NOESY; 13C HSQC- NOESY
REMARK 210 IN THE 13C AROMATIC REGION
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, NMRPIPE 2.0, FELIX
REMARK 210 2000.1, CNS 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 HH TYR A 18 OD1 ASN A 77 1.53
REMARK 500 O HIS A 49 HG SER A 53 1.53
REMARK 500 O PRO A 48 H ASP A 52 1.55
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 VAL A 27 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 PRO A 48 N - CA - CB ANGL. DEV. = 7.7 DEGREES
REMARK 500 2 TYR A 18 N - CA - C ANGL. DEV. = 19.6 DEGREES
REMARK 500 2 CYS A 35 CA - CB - SG ANGL. DEV. = 10.0 DEGREES
REMARK 500 2 GLN A 42 C - N - CA ANGL. DEV. = 16.9 DEGREES
REMARK 500 2 PRO A 43 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 PRO A 48 CB - CA - C ANGL. DEV. = 14.8 DEGREES
REMARK 500 2 PRO A 48 N - CA - CB ANGL. DEV. = 7.3 DEGREES
REMARK 500 2 TRP A 98 CB - CG - CD2 ANGL. DEV. = -23.1 DEGREES
REMARK 500 2 SER A 113 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 3 TYR A 18 N - CA - C ANGL. DEV. = 20.1 DEGREES
REMARK 500 3 CYS A 35 CA - CB - SG ANGL. DEV. = 15.7 DEGREES
REMARK 500 3 GLN A 42 C - N - CA ANGL. DEV. = 16.6 DEGREES
REMARK 500 3 PRO A 43 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 3 PRO A 48 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 3 LEU A 54 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 3 TRP A 98 CB - CG - CD2 ANGL. DEV. = -16.8 DEGREES
REMARK 500 4 VAL A 27 CA - CB - CG2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 4 CYS A 35 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 4 LYS A 39 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 4 PRO A 48 CB - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 4 PRO A 48 CA - C - N ANGL. DEV. = 13.3 DEGREES
REMARK 500 4 HIS A 49 N - CA - CB ANGL. DEV. = 12.8 DEGREES
REMARK 500 4 LEU A 54 CB - CG - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 5 MET A 20 CG - SD - CE ANGL. DEV. = 14.1 DEGREES
REMARK 500 5 VAL A 27 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 5 CYS A 35 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 5 GLN A 42 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 5 PRO A 43 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 5 MET A 45 CA - CB - CG ANGL. DEV. = 10.5 DEGREES
REMARK 500 5 LYS A 61 CB - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 6 PHE A 5 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 6 PHE A 5 CB - CG - CD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 6 GLN A 42 C - N - CA ANGL. DEV. = 18.5 DEGREES
REMARK 500 6 HIS A 49 CA - CB - CG ANGL. DEV. = 10.8 DEGREES
REMARK 500 6 MET A 63 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 6 TRP A 98 CB - CG - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 6 TRP A 98 CB - CG - CD1 ANGL. DEV. = -12.3 DEGREES
REMARK 500 7 VAL A 27 CA - CB - CG2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 7 GLN A 42 C - N - CA ANGL. DEV. = 18.6 DEGREES
REMARK 500 7 HIS A 49 CA - CB - CG ANGL. DEV. = 10.2 DEGREES
REMARK 500 7 ILE A 55 CA - CB - CG1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 7 TRP A 98 CB - CG - CD2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 7 TRP A 98 CB - CG - CD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 8 PHE A 5 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 8 PHE A 5 CB - CG - CD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 8 THR A 14 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 8 THR A 14 CA - CB - CG2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 8 TYR A 18 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 8 TYR A 18 CB - CG - CD1 ANGL. DEV. = 5.7 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 PHE A 5 -63.08 83.17
REMARK 500 1 ARG A 6 89.21 61.57
REMARK 500 1 TRP A 7 -155.26 -126.63
REMARK 500 1 GLN A 16 -31.77 133.68
REMARK 500 1 ASP A 19 -76.75 -24.77
REMARK 500 1 PRO A 48 -14.59 -49.40
REMARK 500 1 PRO A 57 -129.02 -85.81
REMARK 500 1 ASN A 77 -23.95 -142.04
REMARK 500 1 SER A 79 73.78 -157.03
REMARK 500 1 ARG A 80 35.32 -94.39
REMARK 500 1 SER A 102 161.48 82.04
REMARK 500 1 ALA A 103 -35.00 60.72
REMARK 500 1 LEU A 109 -153.53 -99.35
REMARK 500 1 PRO A 112 85.24 -62.98
REMARK 500 1 TRP A 116 -66.01 -12.62
REMARK 500 1 GLN A 119 -94.99 -81.74
REMARK 500 1 ALA A 120 -121.76 -128.62
REMARK 500 1 LEU A 123 -60.06 75.79
REMARK 500 1 ARG A 125 66.10 71.80
REMARK 500 1 LEU A 127 -161.77 -118.00
REMARK 500 1 ARG A 132 63.11 -69.50
REMARK 500 2 ARG A 6 44.94 -96.05
REMARK 500 2 TRP A 7 -95.51 -53.84
REMARK 500 2 ARG A 15 -126.45 22.27
REMARK 500 2 GLN A 16 23.66 -148.14
REMARK 500 2 ASP A 19 -128.93 -103.43
REMARK 500 2 LYS A 39 -39.89 -36.53
REMARK 500 2 ASP A 40 85.58 -151.32
REMARK 500 2 PRO A 48 -14.70 -49.15
REMARK 500 2 PRO A 57 -115.31 -89.72
REMARK 500 2 ASN A 77 -124.79 -120.83
REMARK 500 2 ARG A 80 -46.11 61.61
REMARK 500 2 ALA A 103 -69.68 74.57
REMARK 500 2 CYS A 105 -62.36 74.72
REMARK 500 2 ASP A 106 -38.95 -152.25
REMARK 500 2 ILE A 108 137.78 85.82
REMARK 500 2 PRO A 112 -80.02 -79.43
REMARK 500 2 SER A 113 -49.98 140.35
REMARK 500 2 TRP A 116 -81.39 54.06
REMARK 500 2 PHE A 121 -52.37 -168.12
REMARK 500 2 LEU A 123 -51.09 75.42
REMARK 500 2 ASP A 124 47.68 -71.51
REMARK 500 2 GLU A 128 138.63 86.15
REMARK 500 2 HIS A 131 84.26 80.07
REMARK 500 3 PRO A 3 -152.31 -78.84
REMARK 500 3 ARG A 15 58.31 -58.80
REMARK 500 3 GLN A 16 -20.35 57.50
REMARK 500 3 ASP A 19 -139.23 -91.93
REMARK 500 3 LYS A 39 -37.73 -29.30
REMARK 500 3 ASP A 40 84.26 -152.42
REMARK 500
REMARK 500 THIS ENTRY HAS 407 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 42 PRO A 43 4 -143.50
REMARK 500 GLN A 42 PRO A 43 11 -141.83
REMARK 500 GLN A 42 PRO A 43 12 -143.30
REMARK 500 LYS A 39 ASP A 40 13 -102.35
REMARK 500 GLN A 42 PRO A 43 20 -140.33
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 HIS A 31 0.13 SIDE CHAIN
REMARK 500 7 HIS A 31 0.11 SIDE CHAIN
REMARK 500 8 TYR A 18 0.12 SIDE CHAIN
REMARK 500 8 HIS A 49 0.17 SIDE CHAIN
REMARK 500 9 TYR A 18 0.09 SIDE CHAIN
REMARK 500 9 TYR A 44 0.08 SIDE CHAIN
REMARK 500 9 HIS A 49 0.12 SIDE CHAIN
REMARK 500 10 TYR A 44 0.07 SIDE CHAIN
REMARK 500 10 HIS A 49 0.13 SIDE CHAIN
REMARK 500 11 TYR A 18 0.10 SIDE CHAIN
REMARK 500 11 HIS A 31 0.12 SIDE CHAIN
REMARK 500 11 TYR A 44 0.07 SIDE CHAIN
REMARK 500 12 TYR A 18 0.08 SIDE CHAIN
REMARK 500 12 TYR A 44 0.07 SIDE CHAIN
REMARK 500 13 TYR A 18 0.07 SIDE CHAIN
REMARK 500 13 HIS A 49 0.12 SIDE CHAIN
REMARK 500 16 HIS A 49 0.10 SIDE CHAIN
REMARK 500 18 TYR A 44 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6919 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 BECAUSE OF THE CLONING STRATEGY, THE PEPTIDE
REMARK 999 RESULTING FROM THE CLEAVAGE COMPRISES ADDITIONAL RESIDUES
REMARK 999 FROM 1 TO 5, MAN1 RESIDUES FROM 6 TO 126 AND AGAIN
REMARK 999 ADDITIONAL RESIDUES FROM 127 TO 133.
DBREF 2CH0 A 1 5 PDB 2CH0 2CH0 1 5
DBREF 2CH0 A 6 126 UNP Q9Y2U8 MAN1_HUMAN 655 775
DBREF 2CH0 A 127 133 PDB 2CH0 2CH0 127 133
SEQRES 1 A 133 GLY SER PRO GLU PHE ARG TRP THR LYS GLU GLU GLU GLU
SEQRES 2 A 133 THR ARG GLN MET TYR ASP MET VAL VAL LYS ILE ILE ASP
SEQRES 3 A 133 VAL LEU ARG SER HIS ASN GLU ALA CYS GLN GLU ASN LYS
SEQRES 4 A 133 ASP LEU GLN PRO TYR MET PRO ILE PRO HIS VAL ARG ASP
SEQRES 5 A 133 SER LEU ILE GLN PRO HIS ASP ARG LYS LYS MET LYS LYS
SEQRES 6 A 133 VAL TRP ASP ARG ALA VAL ASP PHE LEU ALA ALA ASN GLU
SEQRES 7 A 133 SER ARG VAL ARG THR GLU THR ARG ARG ILE GLY GLY ALA
SEQRES 8 A 133 ASP PHE LEU VAL TRP ARG TRP ILE GLN PRO SER ALA SER
SEQRES 9 A 133 CYS ASP LYS ILE LEU VAL ILE PRO SER LYS VAL TRP GLN
SEQRES 10 A 133 GLY GLN ALA PHE HIS LEU ASP ARG ARG LEU GLU ARG PRO
SEQRES 11 A 133 HIS ARG ASP
HELIX 1 1 MET A 17 GLU A 37 1 21
HELIX 2 2 ILE A 47 LEU A 54 1 8
HELIX 3 3 HIS A 58 ALA A 76 1 19
SHEET 1 AA 2 VAL A 81 ILE A 88 0
SHEET 2 AA 2 ASP A 92 ILE A 99 -1 O ASP A 92 N ILE A 88
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 - y 2 2 Bytes