Header list of 2u1a.pdb file
Complete list - v 3 2 Bytes
HEADER NUCLEAR PROTEIN 26-MAR-97 2U1A
TITLE RNA BINDING DOMAIN 2 OF HUMAN U1A PROTEIN, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA BINDING DOMAIN 2, RBD2;
COMPND 5 SYNONYM: U1 SNRNP A PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PHA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511145;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: MG1655;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIA;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PAV105;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: 1603 TAC2
KEYWDS RNA BINDING DOMAIN, NUCLEAR PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.LU,K.B.HALL
REVDAT 3 03-NOV-21 2U1A 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2U1A 1 VERSN
REVDAT 1 26-SEP-97 2U1A 0
JRNL AUTH J.LU,K.B.HALL
JRNL TITL TERTIARY STRUCTURE OF RBD2 AND BACKBONE DYNAMICS OF RBD1 AND
JRNL TITL 2 RBD2 OF THE HUMAN U1A PROTEIN DETERMINED BY NMR
JRNL TITL 3 SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 36 10393 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9265619
JRNL DOI 10.1021/BI9709811
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TINKER
REMARK 3 AUTHORS : PONDER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISTANCE GEOMETRY WAS PERFORMED USING
REMARK 3 5%-PAIRWISE METRIZATION AND A GAUSSIAN TRIAL DISTRIBUTION FOR
REMARK 3 THE SELECTION OF DISTANCES USING THE PROGRAM DISTGEOM, A
REMARK 3 COMPONENT OF THE TINKER MOLECULAR MODELING PACKAGE. EMBEDDED
REMARK 3 STRUCTURES WERE REFINED VERSUS A PENALTY FUNCTION BASED SOLELY
REMARK 3 ON THE EXPERIMENTAL RESTRAINTS AND LOCAL COVALENT GEOMETRY (BOND
REMARK 3 LENGTHS, ANGLES, CHIRALITY) OBTAINED FROM A EXTENDED MODEL
REMARK 3 GENERATED BY QUANTA; NO ENERGY-BASED TERMS WERE INCLUDED.
REMARK 3 DETAILS OF THE CALCULATIONS AND STRUCTURAL STATISTICS ARE GIVEN
REMARK 3 IN THE JRNL RECORDS ABOVE.
REMARK 4
REMARK 4 2U1A 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_1000178715.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N EDITED NOESYHMQC; 13C EDITED
REMARK 210 NOESYHSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TINKER
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST ERROR FUNCTION
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 O ILE A 75 H ASN A 78 1.54
REMARK 500 O ILE A 75 H ASN A 79 1.59
REMARK 500 N THR A 76 O ASN A 79 2.13
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 PRO A 12 N - CA - CB ANGL. DEV. = 7.0 DEGREES
REMARK 500 1 LEU A 18 N - CA - CB ANGL. DEV. = 12.0 DEGREES
REMARK 500 1 PRO A 47 N - CA - CB ANGL. DEV. = 7.3 DEGREES
REMARK 500 1 THR A 76 CA - CB - CG2 ANGL. DEV. = -11.4 DEGREES
REMARK 500 2 PHE A 57 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 PHE A 85 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 4 PRO A 22 CA - N - CD ANGL. DEV. = -10.9 DEGREES
REMARK 500 4 HIS A 50 CB - CG - CD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 ALA A 53 N - CA - CB ANGL. DEV. = -9.0 DEGREES
REMARK 500 4 PHE A 57 CB - CG - CD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 PRO A 22 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 5 PRO A 47 N - CD - CG ANGL. DEV. = -9.9 DEGREES
REMARK 500 5 PHE A 57 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 6 PRO A 22 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 6 PRO A 22 CA - N - CD ANGL. DEV. = -10.7 DEGREES
REMARK 500 7 GLY A 48 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 7 PHE A 57 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 7 LYS A 82 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 8 PHE A 40 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 8 GLY A 48 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 8 PHE A 57 CB - CG - CD1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 9 PHE A 54 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 9 PHE A 57 CB - CG - CD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 9 LYS A 82 O - C - N ANGL. DEV. = 10.1 DEGREES
REMARK 500 10 ILE A 75 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 10 THR A 76 CA - CB - CG2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 10 ASN A 79 O - C - N ANGL. DEV. = -12.7 DEGREES
REMARK 500 11 PHE A 37 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 11 PHE A 57 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 12 PRO A 22 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 12 PRO A 38 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 12 PRO A 38 CA - N - CD ANGL. DEV. = -9.0 DEGREES
REMARK 500 12 PRO A 47 CA - N - CD ANGL. DEV. = -9.4 DEGREES
REMARK 500 12 PHE A 57 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 12 LYS A 82 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 13 PRO A 12 CA - N - CD ANGL. DEV. = -10.8 DEGREES
REMARK 500 13 PRO A 12 N - CD - CG ANGL. DEV. = 8.6 DEGREES
REMARK 500 13 PRO A 22 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 13 PRO A 22 N - CA - CB ANGL. DEV. = -7.4 DEGREES
REMARK 500 13 PHE A 40 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 13 PRO A 47 N - CA - CB ANGL. DEV. = 7.8 DEGREES
REMARK 500 14 PRO A 11 N - CA - CB ANGL. DEV. = -7.4 DEGREES
REMARK 500 14 PHE A 37 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 14 PRO A 47 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 14 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 15 PRO A 11 N - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 15 PHE A 40 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 16 HIS A 14 CB - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 16 PRO A 47 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 16 PRO A 47 CA - N - CD ANGL. DEV. = -9.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 67 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 2 80.33 49.98
REMARK 500 1 SER A 8 140.62 70.59
REMARK 500 1 GLU A 9 -34.43 -135.33
REMARK 500 1 LEU A 18 -179.44 173.88
REMARK 500 1 ASN A 20 34.64 110.31
REMARK 500 1 PRO A 22 -156.94 -112.69
REMARK 500 1 GLU A 23 52.20 90.33
REMARK 500 1 GLN A 36 -36.83 -34.29
REMARK 500 1 PHE A 40 94.83 -40.59
REMARK 500 1 VAL A 46 -20.67 -162.19
REMARK 500 1 PRO A 47 -169.63 -63.19
REMARK 500 1 ARG A 49 -79.43 -46.25
REMARK 500 1 ASP A 58 -49.67 -8.08
REMARK 500 1 GLN A 71 40.72 -68.52
REMARK 500 1 PHE A 73 90.45 -66.77
REMARK 500 1 LYS A 74 48.18 -42.74
REMARK 500 1 GLN A 77 -16.77 -47.17
REMARK 500 1 ASN A 78 -49.79 -137.56
REMARK 500 1 PHE A 85 157.31 -39.86
REMARK 500 1 ALA A 86 49.02 -79.99
REMARK 500 2 ALA A 2 78.32 -157.78
REMARK 500 2 ALA A 4 -141.20 -134.18
REMARK 500 2 GLN A 5 -52.08 -174.00
REMARK 500 2 LEU A 7 -74.49 -72.50
REMARK 500 2 SER A 8 -161.94 -113.44
REMARK 500 2 ASN A 10 -66.21 -167.58
REMARK 500 2 PRO A 11 132.35 -31.50
REMARK 500 2 HIS A 14 5.09 145.06
REMARK 500 2 LEU A 18 -179.48 178.17
REMARK 500 2 ASN A 20 35.51 117.69
REMARK 500 2 PRO A 22 -171.76 -69.65
REMARK 500 2 GLN A 36 -41.06 -28.21
REMARK 500 2 PHE A 40 106.16 -47.96
REMARK 500 2 LEU A 45 89.95 -164.95
REMARK 500 2 VAL A 46 -26.86 -161.08
REMARK 500 2 PRO A 47 -165.12 -63.58
REMARK 500 2 ARG A 49 -87.36 -56.62
REMARK 500 2 ASP A 58 -38.58 -24.67
REMARK 500 2 GLN A 71 88.55 -58.53
REMARK 500 2 LYS A 74 80.36 -52.33
REMARK 500 2 THR A 76 -35.23 -130.93
REMARK 500 2 GLN A 77 -40.50 132.36
REMARK 500 2 PHE A 85 -95.32 -18.55
REMARK 500 2 ALA A 86 -22.97 171.49
REMARK 500 2 LYS A 87 -78.97 -125.69
REMARK 500 3 LEU A 7 -145.62 61.64
REMARK 500 3 SER A 8 156.83 70.31
REMARK 500 3 GLU A 9 79.50 -152.68
REMARK 500 3 PRO A 12 85.62 -63.83
REMARK 500 3 LEU A 18 -179.47 170.43
REMARK 500
REMARK 500 THIS ENTRY HAS 418 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 ARG A 44 0.27 SIDE CHAIN
REMARK 500 1 ARG A 49 0.26 SIDE CHAIN
REMARK 500 1 ARG A 67 0.32 SIDE CHAIN
REMARK 500 2 ARG A 44 0.25 SIDE CHAIN
REMARK 500 2 ARG A 49 0.25 SIDE CHAIN
REMARK 500 2 ARG A 67 0.31 SIDE CHAIN
REMARK 500 3 ARG A 44 0.26 SIDE CHAIN
REMARK 500 3 ARG A 49 0.24 SIDE CHAIN
REMARK 500 3 ARG A 67 0.31 SIDE CHAIN
REMARK 500 4 ARG A 44 0.26 SIDE CHAIN
REMARK 500 4 ARG A 49 0.26 SIDE CHAIN
REMARK 500 4 ARG A 67 0.32 SIDE CHAIN
REMARK 500 5 ARG A 44 0.26 SIDE CHAIN
REMARK 500 5 ARG A 49 0.24 SIDE CHAIN
REMARK 500 5 ARG A 67 0.30 SIDE CHAIN
REMARK 500 6 ARG A 44 0.26 SIDE CHAIN
REMARK 500 6 ARG A 49 0.25 SIDE CHAIN
REMARK 500 6 ARG A 67 0.31 SIDE CHAIN
REMARK 500 7 ARG A 44 0.26 SIDE CHAIN
REMARK 500 7 ARG A 49 0.25 SIDE CHAIN
REMARK 500 7 ARG A 67 0.32 SIDE CHAIN
REMARK 500 8 ARG A 44 0.26 SIDE CHAIN
REMARK 500 8 ARG A 49 0.26 SIDE CHAIN
REMARK 500 8 ARG A 67 0.31 SIDE CHAIN
REMARK 500 9 ARG A 44 0.26 SIDE CHAIN
REMARK 500 9 ARG A 49 0.26 SIDE CHAIN
REMARK 500 9 ARG A 67 0.31 SIDE CHAIN
REMARK 500 10 ARG A 44 0.27 SIDE CHAIN
REMARK 500 10 ARG A 49 0.25 SIDE CHAIN
REMARK 500 10 ARG A 67 0.31 SIDE CHAIN
REMARK 500 11 ARG A 44 0.26 SIDE CHAIN
REMARK 500 11 ARG A 49 0.26 SIDE CHAIN
REMARK 500 11 ARG A 67 0.32 SIDE CHAIN
REMARK 500 12 ARG A 44 0.26 SIDE CHAIN
REMARK 500 12 ARG A 49 0.25 SIDE CHAIN
REMARK 500 12 ARG A 67 0.31 SIDE CHAIN
REMARK 500 13 ARG A 44 0.27 SIDE CHAIN
REMARK 500 13 ARG A 49 0.25 SIDE CHAIN
REMARK 500 13 ARG A 67 0.31 SIDE CHAIN
REMARK 500 14 ARG A 44 0.26 SIDE CHAIN
REMARK 500 14 ARG A 49 0.25 SIDE CHAIN
REMARK 500 14 ARG A 67 0.30 SIDE CHAIN
REMARK 500 15 ARG A 44 0.26 SIDE CHAIN
REMARK 500 15 ARG A 49 0.25 SIDE CHAIN
REMARK 500 15 ARG A 67 0.31 SIDE CHAIN
REMARK 500 16 ARG A 44 0.26 SIDE CHAIN
REMARK 500 16 ARG A 49 0.25 SIDE CHAIN
REMARK 500 16 ARG A 67 0.31 SIDE CHAIN
REMARK 500 17 ARG A 44 0.26 SIDE CHAIN
REMARK 500 17 ARG A 49 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2U1A A 1 88 UNP P09012 SNRPA_HUMAN 195 282
SEQADV 2U1A ALA A 2 UNP P09012 PRO 196 ENGINEERED MUTATION
SEQRES 1 A 88 MET ALA PRO ALA GLN PRO LEU SER GLU ASN PRO PRO ASN
SEQRES 2 A 88 HIS ILE LEU PHE LEU THR ASN LEU PRO GLU GLU THR ASN
SEQRES 3 A 88 GLU LEU MET LEU SER MET LEU PHE ASN GLN PHE PRO GLY
SEQRES 4 A 88 PHE LYS GLU VAL ARG LEU VAL PRO GLY ARG HIS ASP ILE
SEQRES 5 A 88 ALA PHE VAL GLU PHE ASP ASN GLU VAL GLN ALA GLY ALA
SEQRES 6 A 88 ALA ARG ASP ALA LEU GLN GLY PHE LYS ILE THR GLN ASN
SEQRES 7 A 88 ASN ALA MET LYS ILE SER PHE ALA LYS LYS
HELIX 1 1 GLU A 27 ASN A 35 1 9
HELIX 2 2 GLU A 60 ALA A 69 1 10
HELIX 3 3 LYS A 74 GLN A 77 5 4
SHEET 1 A 4 LYS A 82 PHE A 85 0
SHEET 2 A 4 ILE A 15 THR A 19 -1 N THR A 19 O LYS A 82
SHEET 3 A 4 ILE A 52 PHE A 57 -1 N VAL A 55 O LEU A 16
SHEET 4 A 4 PHE A 40 ARG A 44 -1 N ARG A 44 O PHE A 54
CISPEP 1 PRO A 11 PRO A 12 1 0.17
CISPEP 2 PRO A 11 PRO A 12 2 0.67
CISPEP 3 PRO A 11 PRO A 12 5 0.25
CISPEP 4 GLN A 5 PRO A 6 6 0.06
CISPEP 5 GLN A 5 PRO A 6 9 0.00
CISPEP 6 PRO A 11 PRO A 12 9 -0.03
CISPEP 7 GLN A 5 PRO A 6 10 -0.02
CISPEP 8 GLN A 5 PRO A 6 12 0.02
CISPEP 9 GLN A 5 PRO A 6 13 0.04
CISPEP 10 PRO A 11 PRO A 12 13 0.60
CISPEP 11 ALA A 2 PRO A 3 14 0.02
CISPEP 12 ALA A 2 PRO A 3 16 0.07
CISPEP 13 GLN A 5 PRO A 6 17 0.22
CISPEP 14 PRO A 11 PRO A 12 19 0.04
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