Header list of 1xqq.pdb file
Complete list - ar 2 Bytes
HEADER SIGNALING PROTEIN 13-OCT-04 1XQQ
TITLE SIMULTANEOUS DETERMINATION OF PROTEIN STRUCTURE AND DYNAMICS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN;
COMPND 3 CHAIN: A;
COMPND 4 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: 562
KEYWDS SIGNALING PROTEIN, UBIQUITIN
EXPDTA SOLUTION NMR
NUMMDL 128
AUTHOR K.LINDORFF-LARSEN,R.B.BEST,M.A.DEPRISTO,M.VENDRUSCOLO,C.M.DOBSON
REVDAT 3 02-MAR-22 1XQQ 1 REMARK
REVDAT 2 24-FEB-09 1XQQ 1 VERSN
REVDAT 1 08-FEB-05 1XQQ 0
JRNL AUTH K.LINDORFF-LARSEN,R.B.BEST,M.A.DEPRISTO,C.M.DOBSON,
JRNL AUTH 2 M.VENDRUSCOLO
JRNL TITL SIMULTANEOUS DETERMINATION OF PROTEIN STRUCTURE AND DYNAMICS
JRNL REF NATURE V. 433 128 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 15650731
JRNL DOI 10.1038/NATURE03199
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CHARMM C30
REMARK 3 AUTHORS : B.R.BROOKS, R.E.BRUCCOLERI, B.D.OLAFSON,
REMARK 3 D.J.STATES, S.SWAMINATHAN, M.KARPLUS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DYNAMIC ENSEMBLE REFINEMENT USING
REMARK 3 PREVIOUSLY PUBLISHED NOE DERIVED DISTANCE RESTRAINTS AND 112
REMARK 3 EXPERIMENTALLY DETERMINED ORDER PARAMETERS AS INPUT TO ENSEMBLE
REMARK 3 SIMULATIONS.
REMARK 4
REMARK 4 1XQQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030656.
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 : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 128
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 128
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 OE1 GLU A 51 HE ARG A 54 1.59
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 MET A 1 CG - SD - CE ANGL. DEV. = -14.3 DEGREES
REMARK 500 1 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 1 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 ARG A 72 O - C - N ANGL. DEV. = -9.9 DEGREES
REMARK 500 2 MET A 1 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 2 ASP A 39 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 PHE A 45 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 PHE A 45 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 3 PHE A 4 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 LYS A 6 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 3 VAL A 26 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 3 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 PHE A 45 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 3 TYR A 59 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 THR A 66 N - CA - CB ANGL. DEV. = 12.3 DEGREES
REMARK 500 3 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 4 PHE A 4 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 THR A 14 CA - CB - CG2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 4 ILE A 30 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 4 ARG A 42 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 ASP A 58 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 4 TYR A 59 CB - CG - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 4 TYR A 59 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ARG A 74 NH1 - CZ - NH2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 4 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 5 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 5 ARG A 42 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 PHE A 45 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 5 TYR A 59 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 GLU A 64 CB - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 5 GLU A 64 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 5 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 6 THR A 9 N - CA - CB ANGL. DEV. = 14.8 DEGREES
REMARK 500 6 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 6 ILE A 30 O - C - N ANGL. DEV. = -10.9 DEGREES
REMARK 500 6 GLN A 49 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 6 ARG A 54 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 VAL A 5 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 7 ASP A 39 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 7 GLY A 47 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500 7 GLU A 64 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 7 ARG A 72 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 8 PHE A 45 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 8 ASP A 52 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 8 ARG A 72 NH1 - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 831 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 ALA A 46 -102.08 65.29
REMARK 500 1 ASN A 60 53.16 87.10
REMARK 500 1 LEU A 73 -139.50 -99.15
REMARK 500 2 THR A 9 -78.52 -79.97
REMARK 500 2 PHE A 45 -75.83 -95.57
REMARK 500 2 ALA A 46 -66.06 -105.61
REMARK 500 2 ARG A 74 -73.19 -101.99
REMARK 500 3 LYS A 33 -71.97 -63.67
REMARK 500 3 PHE A 45 -88.77 -90.88
REMARK 500 3 ALA A 46 -61.79 -103.98
REMARK 500 3 ASN A 60 54.02 72.77
REMARK 500 3 GLN A 62 -166.50 -102.94
REMARK 500 3 ARG A 74 -91.77 -167.44
REMARK 500 4 PHE A 45 -90.46 -85.61
REMARK 500 4 ASP A 52 -70.48 -37.06
REMARK 500 4 ASN A 60 29.83 81.23
REMARK 500 4 LEU A 71 -159.30 -82.33
REMARK 500 4 LEU A 73 -62.35 -102.73
REMARK 500 4 ARG A 74 -83.46 -144.32
REMARK 500 5 ALA A 46 -80.71 -136.44
REMARK 500 5 ASN A 60 29.53 92.49
REMARK 500 5 GLU A 64 42.80 75.43
REMARK 500 5 LEU A 73 -75.20 -83.72
REMARK 500 6 ALA A 46 -36.39 -135.58
REMARK 500 7 LYS A 33 -70.99 -87.42
REMARK 500 7 ALA A 46 -60.79 -130.54
REMARK 500 7 GLN A 62 -165.56 -105.60
REMARK 500 8 PHE A 45 -77.68 -111.68
REMARK 500 8 ASP A 52 -55.36 -28.20
REMARK 500 9 ALA A 46 -102.56 70.84
REMARK 500 9 ASN A 60 71.57 68.56
REMARK 500 9 GLN A 62 -166.39 -100.13
REMARK 500 10 ALA A 46 -84.85 65.65
REMARK 500 11 THR A 9 -78.55 -72.42
REMARK 500 11 ALA A 46 -91.65 68.86
REMARK 500 11 ARG A 72 -82.31 -68.86
REMARK 500 12 ALA A 46 -108.25 54.42
REMARK 500 12 ARG A 72 -87.80 -65.48
REMARK 500 13 ALA A 46 -75.83 54.08
REMARK 500 13 ARG A 72 -82.87 -90.38
REMARK 500 14 THR A 9 -72.95 -85.93
REMARK 500 14 LYS A 33 -82.53 -63.22
REMARK 500 14 ALA A 46 -98.33 58.58
REMARK 500 14 ASN A 60 61.03 66.44
REMARK 500 14 ARG A 72 -80.43 -86.93
REMARK 500 14 ARG A 74 -164.83 -73.67
REMARK 500 15 THR A 9 -70.20 -68.49
REMARK 500 15 ALA A 46 -95.84 44.10
REMARK 500 15 ASN A 60 45.03 72.34
REMARK 500 15 LEU A 73 -56.32 -143.54
REMARK 500
REMARK 500 THIS ENTRY HAS 365 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 GLY A 10 LYS A 11 13 147.13
REMARK 500 PRO A 37 PRO A 38 15 -148.07
REMARK 500 GLU A 51 ASP A 52 35 -147.41
REMARK 500 PRO A 37 PRO A 38 44 -149.65
REMARK 500 GLN A 41 ARG A 42 46 140.76
REMARK 500 LEU A 71 ARG A 72 57 148.58
REMARK 500 GLN A 40 GLN A 41 59 -145.26
REMARK 500 ARG A 72 LEU A 73 64 149.20
REMARK 500 GLU A 51 ASP A 52 66 -143.21
REMARK 500 PRO A 37 PRO A 38 84 -142.66
REMARK 500 LEU A 15 GLU A 16 86 148.91
REMARK 500 GLU A 51 ASP A 52 101 -149.30
REMARK 500 PRO A 37 PRO A 38 106 -148.17
REMARK 500 GLN A 2 ILE A 3 109 148.55
REMARK 500 GLU A 51 ASP A 52 118 -148.32
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 59 0.14 SIDE CHAIN
REMARK 500 1 ARG A 72 0.11 SIDE CHAIN
REMARK 500 1 ARG A 74 0.10 SIDE CHAIN
REMARK 500 2 ARG A 42 0.16 SIDE CHAIN
REMARK 500 3 ARG A 42 0.12 SIDE CHAIN
REMARK 500 4 ARG A 42 0.09 SIDE CHAIN
REMARK 500 5 ARG A 74 0.09 SIDE CHAIN
REMARK 500 6 ARG A 42 0.13 SIDE CHAIN
REMARK 500 7 ARG A 74 0.11 SIDE CHAIN
REMARK 500 8 ARG A 72 0.15 SIDE CHAIN
REMARK 500 10 ARG A 54 0.09 SIDE CHAIN
REMARK 500 11 ARG A 42 0.11 SIDE CHAIN
REMARK 500 11 TYR A 59 0.11 SIDE CHAIN
REMARK 500 11 ARG A 72 0.17 SIDE CHAIN
REMARK 500 12 ARG A 54 0.10 SIDE CHAIN
REMARK 500 12 TYR A 59 0.08 SIDE CHAIN
REMARK 500 12 ARG A 72 0.09 SIDE CHAIN
REMARK 500 13 ARG A 54 0.09 SIDE CHAIN
REMARK 500 13 TYR A 59 0.08 SIDE CHAIN
REMARK 500 13 ARG A 74 0.08 SIDE CHAIN
REMARK 500 15 ARG A 72 0.11 SIDE CHAIN
REMARK 500 16 TYR A 59 0.07 SIDE CHAIN
REMARK 500 16 ARG A 72 0.13 SIDE CHAIN
REMARK 500 18 ARG A 54 0.10 SIDE CHAIN
REMARK 500 18 TYR A 59 0.12 SIDE CHAIN
REMARK 500 18 ARG A 74 0.15 SIDE CHAIN
REMARK 500 19 ARG A 42 0.16 SIDE CHAIN
REMARK 500 21 PHE A 45 0.08 SIDE CHAIN
REMARK 500 21 ARG A 74 0.09 SIDE CHAIN
REMARK 500 22 ARG A 42 0.09 SIDE CHAIN
REMARK 500 22 ARG A 72 0.12 SIDE CHAIN
REMARK 500 23 ARG A 42 0.13 SIDE CHAIN
REMARK 500 23 TYR A 59 0.07 SIDE CHAIN
REMARK 500 25 PHE A 4 0.08 SIDE CHAIN
REMARK 500 25 TYR A 59 0.09 SIDE CHAIN
REMARK 500 26 ARG A 42 0.10 SIDE CHAIN
REMARK 500 27 ARG A 72 0.10 SIDE CHAIN
REMARK 500 28 ARG A 42 0.10 SIDE CHAIN
REMARK 500 28 ARG A 74 0.10 SIDE CHAIN
REMARK 500 29 ARG A 54 0.09 SIDE CHAIN
REMARK 500 29 ARG A 74 0.10 SIDE CHAIN
REMARK 500 30 ARG A 72 0.11 SIDE CHAIN
REMARK 500 31 ARG A 54 0.11 SIDE CHAIN
REMARK 500 32 ARG A 72 0.11 SIDE CHAIN
REMARK 500 33 ARG A 54 0.10 SIDE CHAIN
REMARK 500 33 ARG A 72 0.14 SIDE CHAIN
REMARK 500 33 ARG A 74 0.11 SIDE CHAIN
REMARK 500 34 ARG A 54 0.15 SIDE CHAIN
REMARK 500 34 HIS A 68 0.09 SIDE CHAIN
REMARK 500 34 ARG A 72 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 210 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D3Z RELATED DB: PDB
REMARK 900 RELATED ID: 1UBQ RELATED DB: PDB
DBREF 1XQQ A 1 76 GB 4506713 NP_002945 1 76
SEQRES 1 A 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 A 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 A 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 A 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 A 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 A 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HELIX 1 1 THR A 22 GLU A 34 1 13
HELIX 2 2 THR A 55 ASN A 60 1 6
SHEET 1 A 5 THR A 12 GLU A 16 0
SHEET 2 A 5 GLN A 2 LYS A 6 -1 N VAL A 5 O ILE A 13
SHEET 3 A 5 THR A 66 LEU A 71 1 O LEU A 69 N LYS A 6
SHEET 4 A 5 GLN A 41 PHE A 45 -1 N ILE A 44 O HIS A 68
SHEET 5 A 5 LYS A 48 GLN A 49 -1 O LYS A 48 N PHE A 45
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 - ar 2 Bytes