Header list of 1yus.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 14-FEB-05 1YUS
TITLE SOLUTION STRUCTURE OF APO-S100A13
CAVEAT 1YUS THERE ARE MANY CHIRALITY ERRORS IN CHAIN A AND B.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S100 CALCIUM BINDING PROTEIN A13;
COMPND 3 CHAIN: A, B;
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 GENE: S100A13;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21GOLD(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET21A;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21S100
KEYWDS S100A13, EF HAND CALCIUM-BINDING PROTEINS, COPPER(II), STRUCTURAL
KEYWDS 2 GENOMICS, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, METAL BINDING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,A.FANTONI,L.TENORI,M.S.VIEZZOLI,
AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1YUS 1 REMARK
REVDAT 2 24-FEB-09 1YUS 1 VERSN
REVDAT 1 18-OCT-05 1YUS 0
JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,A.FANTONI,L.TENORI,M.S.VIEZZOLI
JRNL TITL STRUCTURAL INTERPLAY BETWEEN CALCIUM(II) AND COPPER(II)
JRNL TITL 2 BINDING TO S100A13 PROTEIN
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 44 6341 2005
JRNL REFN ESSN 0570-0833
JRNL PMID 16145699
JRNL DOI 10.1002/ANIE.200500540
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 5.1, AMBER 6
REMARK 3 AUTHORS : GUNTERT ET AL. (DYANA), D.A. CASE ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YUS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031941.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : 20MM SODIUM ACETATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM 13C, 15N LABELED S100A13
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D TECHNIQUES
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: 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
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 2 LYS A 97 CG - CD - CE ANGL. DEV. = 22.2 DEGREES
REMARK 500 2 ARG B 78 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 4 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 GLU B 86 CA - CB - CG ANGL. DEV. = 17.6 DEGREES
REMARK 500 10 GLU B 8 CA - CB - CG ANGL. DEV. = 28.3 DEGREES
REMARK 500 12 LYS A 89 CB - CG - CD ANGL. DEV. = 16.0 DEGREES
REMARK 500 12 ALA B 2 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 12 GLU B 4 CB - CA - C ANGL. DEV. = 13.9 DEGREES
REMARK 500 13 THR A 19 CA - C - O ANGL. DEV. = -35.4 DEGREES
REMARK 500 13 THR A 19 CA - C - N ANGL. DEV. = -30.7 DEGREES
REMARK 500 13 THR A 19 O - C - N ANGL. DEV. = 48.5 DEGREES
REMARK 500 14 LYS A 98 CA - CB - CG ANGL. DEV. = 21.9 DEGREES
REMARK 500 15 ALA B 2 CA - C - O ANGL. DEV. = -34.3 DEGREES
REMARK 500 15 ALA B 2 CA - C - N ANGL. DEV. = 50.0 DEGREES
REMARK 500 15 ALA B 2 O - C - N ANGL. DEV. = -41.0 DEGREES
REMARK 500 17 ARG A 29 CB - CG - CD ANGL. DEV. = 19.3 DEGREES
REMARK 500 17 LEU B 6 CB - CG - CD2 ANGL. DEV. = 11.9 DEGREES
REMARK 500 18 ARG B 25 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 21 ARG A 88 CB - CG - CD ANGL. DEV. = 20.7 DEGREES
REMARK 500 22 MET B 1 CB - CA - C ANGL. DEV. = 15.2 DEGREES
REMARK 500 22 GLU B 10 CB - CA - C ANGL. DEV. = 22.9 DEGREES
REMARK 500 22 VAL B 17 CB - CA - C ANGL. DEV. = 15.0 DEGREES
REMARK 500 24 ARG B 29 NE - CZ - NH2 ANGL. DEV. = -3.3 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 ALA A 3 63.13 -155.95
REMARK 500 1 ARG A 25 106.24 -48.83
REMARK 500 1 ASP A 31 59.71 75.92
REMARK 500 1 SER A 32 -145.02 -125.33
REMARK 500 1 LEU A 46 73.77 -105.90
REMARK 500 1 PRO A 47 31.41 -82.16
REMARK 500 1 LEU A 49 -61.92 -160.10
REMARK 500 1 ASP A 52 90.66 57.89
REMARK 500 1 ASN A 66 58.51 -145.70
REMARK 500 1 TRP A 77 -75.43 -49.52
REMARK 500 1 GLU A 86 -75.63 -60.26
REMARK 500 1 LYS A 90 -174.72 179.13
REMARK 500 1 LYS A 91 -64.89 64.17
REMARK 500 1 ASP A 92 56.51 -155.14
REMARK 500 1 ARG A 96 -64.68 74.98
REMARK 500 1 LYS A 97 -61.02 -164.87
REMARK 500 1 PRO B 5 65.36 -54.86
REMARK 500 1 PHE B 23 -58.04 -156.24
REMARK 500 1 LYS B 30 -105.81 -80.78
REMARK 500 1 ASP B 31 -73.78 -111.22
REMARK 500 1 SER B 32 -157.83 -126.08
REMARK 500 1 LEU B 46 65.20 -108.63
REMARK 500 1 PRO B 47 46.86 -83.18
REMARK 500 1 LEU B 49 -51.83 -147.50
REMARK 500 1 LEU B 50 61.14 62.47
REMARK 500 1 ASP B 52 84.08 57.47
REMARK 500 1 SER B 69 -176.84 -66.25
REMARK 500 1 LYS B 89 -33.76 -39.88
REMARK 500 1 LYS B 90 -81.11 70.17
REMARK 500 1 LYS B 91 -46.20 -164.85
REMARK 500 1 ARG B 96 74.24 61.65
REMARK 500 1 LYS B 97 -11.93 82.53
REMARK 500 2 ALA A 3 58.02 -156.70
REMARK 500 2 PHE A 23 -165.34 -164.88
REMARK 500 2 ARG A 25 155.67 59.67
REMARK 500 2 GLN A 26 64.14 -160.14
REMARK 500 2 ASP A 31 -62.78 -158.03
REMARK 500 2 LEU A 46 58.24 -102.46
REMARK 500 2 PRO A 47 43.89 -84.23
REMARK 500 2 HIS A 48 -80.29 -82.87
REMARK 500 2 ASP A 52 91.56 31.81
REMARK 500 2 TRP A 77 -73.08 -46.19
REMARK 500 2 GLU A 86 -81.47 -60.98
REMARK 500 2 LYS A 89 115.67 -38.95
REMARK 500 2 LYS A 91 -63.85 -162.42
REMARK 500 2 ARG A 96 -50.06 80.58
REMARK 500 2 LYS A 97 -58.54 -141.77
REMARK 500 2 ALA B 3 55.35 -95.13
REMARK 500 2 PRO B 5 44.50 -68.41
REMARK 500 2 ASP B 31 -63.90 -136.02
REMARK 500
REMARK 500 THIS ENTRY HAS 824 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 THR A 22 PHE A 23 1 -43.02
REMARK 500 PHE A 23 ALA A 24 1 114.57
REMARK 500 ALA B 3 GLU B 4 1 119.87
REMARK 500 THR A 22 PHE A 23 2 -84.78
REMARK 500 ALA A 24 ARG A 25 2 -146.39
REMARK 500 GLY B 28 ARG B 29 3 149.23
REMARK 500 GLU A 70 LEU A 71 4 149.93
REMARK 500 GLU A 70 LEU A 71 5 146.12
REMARK 500 ALA B 3 GLU B 4 5 108.23
REMARK 500 ALA B 3 GLU B 4 6 91.56
REMARK 500 ALA B 2 ALA B 3 7 -35.46
REMARK 500 GLU B 4 PRO B 5 7 -133.01
REMARK 500 MET B 1 ALA B 2 8 -123.14
REMARK 500 ALA B 3 GLU B 4 10 115.46
REMARK 500 GLU B 4 PRO B 5 11 -55.65
REMARK 500 ALA B 3 GLU B 4 12 -140.92
REMARK 500 LYS A 30 ASP A 31 13 -138.75
REMARK 500 ALA A 24 ARG A 25 15 88.86
REMARK 500 ARG A 25 GLN A 26 15 -147.70
REMARK 500 LYS B 97 LYS B 98 16 143.71
REMARK 500 PHE A 21 THR A 22 17 -147.16
REMARK 500 LYS A 91 ASP A 92 17 -148.57
REMARK 500 MET B 1 ALA B 2 17 89.45
REMARK 500 GLU B 4 PRO B 5 18 -92.83
REMARK 500 ALA B 3 GLU B 4 19 112.49
REMARK 500 SER A 34 VAL A 35 20 -148.86
REMARK 500 MET A 1 ALA A 2 21 136.42
REMARK 500 ALA B 3 GLU B 4 21 72.74
REMARK 500 LEU A 33 SER A 34 22 135.66
REMARK 500 ALA B 2 ALA B 3 22 -136.74
REMARK 500 ALA B 3 GLU B 4 23 86.90
REMARK 500 LYS A 51 ASP A 52 25 147.82
REMARK 500 LYS A 97 LYS A 98 25 149.39
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 B 78 0.09 SIDE CHAIN
REMARK 500 2 PHE A 73 0.09 SIDE CHAIN
REMARK 500 3 PHE A 20 0.08 SIDE CHAIN
REMARK 500 3 ARG A 29 0.11 SIDE CHAIN
REMARK 500 3 ARG B 96 0.08 SIDE CHAIN
REMARK 500 4 TYR A 76 0.13 SIDE CHAIN
REMARK 500 5 HIS B 48 0.08 SIDE CHAIN
REMARK 500 5 PHE B 73 0.10 SIDE CHAIN
REMARK 500 5 TYR B 76 0.07 SIDE CHAIN
REMARK 500 5 ARG B 96 0.11 SIDE CHAIN
REMARK 500 6 ARG A 25 0.09 SIDE CHAIN
REMARK 500 7 PHE A 73 0.10 SIDE CHAIN
REMARK 500 7 ARG B 29 0.08 SIDE CHAIN
REMARK 500 7 PHE B 73 0.20 SIDE CHAIN
REMARK 500 8 HIS A 48 0.12 SIDE CHAIN
REMARK 500 8 ARG A 96 0.17 SIDE CHAIN
REMARK 500 8 PHE B 20 0.09 SIDE CHAIN
REMARK 500 8 ARG B 78 0.08 SIDE CHAIN
REMARK 500 8 ARG B 88 0.11 SIDE CHAIN
REMARK 500 9 PHE A 38 0.08 SIDE CHAIN
REMARK 500 9 ARG B 29 0.17 SIDE CHAIN
REMARK 500 9 TYR B 76 0.09 SIDE CHAIN
REMARK 500 10 PHE A 73 0.10 SIDE CHAIN
REMARK 500 11 PHE A 23 0.09 SIDE CHAIN
REMARK 500 11 ARG A 78 0.11 SIDE CHAIN
REMARK 500 11 ARG B 96 0.10 SIDE CHAIN
REMARK 500 12 PHE A 38 0.10 SIDE CHAIN
REMARK 500 12 ARG A 96 0.08 SIDE CHAIN
REMARK 500 13 HIS A 48 0.09 SIDE CHAIN
REMARK 500 13 TYR A 76 0.09 SIDE CHAIN
REMARK 500 13 ARG A 96 0.09 SIDE CHAIN
REMARK 500 13 PHE B 38 0.09 SIDE CHAIN
REMARK 500 13 PHE B 73 0.16 SIDE CHAIN
REMARK 500 14 ARG A 29 0.12 SIDE CHAIN
REMARK 500 15 ARG A 78 0.11 SIDE CHAIN
REMARK 500 16 ARG A 96 0.17 SIDE CHAIN
REMARK 500 16 PHE B 20 0.10 SIDE CHAIN
REMARK 500 17 PHE A 73 0.12 SIDE CHAIN
REMARK 500 18 ARG A 96 0.13 SIDE CHAIN
REMARK 500 18 PHE B 21 0.13 SIDE CHAIN
REMARK 500 18 PHE B 23 0.12 SIDE CHAIN
REMARK 500 18 TYR B 76 0.11 SIDE CHAIN
REMARK 500 19 ARG A 29 0.10 SIDE CHAIN
REMARK 500 19 PHE B 21 0.08 SIDE CHAIN
REMARK 500 20 PHE A 73 0.10 SIDE CHAIN
REMARK 500 20 TYR A 76 0.12 SIDE CHAIN
REMARK 500 20 ARG A 96 0.16 SIDE CHAIN
REMARK 500 20 PHE B 21 0.10 SIDE CHAIN
REMARK 500 20 ARG B 25 0.11 SIDE CHAIN
REMARK 500 20 PHE B 73 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 70 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 15 ALA B 2 -166.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YUR RELATED DB: PDB
REMARK 900 APO-S100A13, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1YUT RELATED DB: PDB
REMARK 900 CALCIUM-S100A13, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1YUU RELATED DB: PDB
REMARK 900 CALCIUM-S100A13, 25 ENSEMBLE STRUCTURES
REMARK 900 RELATED ID: CIRMMP11 RELATED DB: TARGETDB
DBREF 1YUS A 1 98 UNP Q99584 S10AD_HUMAN 1 98
DBREF 1YUS B 1 98 UNP Q99584 S10AD_HUMAN 1 98
SEQRES 1 A 98 MET ALA ALA GLU PRO LEU THR GLU LEU GLU GLU SER ILE
SEQRES 2 A 98 GLU THR VAL VAL THR THR PHE PHE THR PHE ALA ARG GLN
SEQRES 3 A 98 GLU GLY ARG LYS ASP SER LEU SER VAL ASN GLU PHE LYS
SEQRES 4 A 98 GLU LEU VAL THR GLN GLN LEU PRO HIS LEU LEU LYS ASP
SEQRES 5 A 98 VAL GLY SER LEU ASP GLU LYS MET LYS SER LEU ASP VAL
SEQRES 6 A 98 ASN GLN ASP SER GLU LEU LYS PHE ASN GLU TYR TRP ARG
SEQRES 7 A 98 LEU ILE GLY GLU LEU ALA LYS GLU ILE ARG LYS LYS LYS
SEQRES 8 A 98 ASP LEU LYS ILE ARG LYS LYS
SEQRES 1 B 98 MET ALA ALA GLU PRO LEU THR GLU LEU GLU GLU SER ILE
SEQRES 2 B 98 GLU THR VAL VAL THR THR PHE PHE THR PHE ALA ARG GLN
SEQRES 3 B 98 GLU GLY ARG LYS ASP SER LEU SER VAL ASN GLU PHE LYS
SEQRES 4 B 98 GLU LEU VAL THR GLN GLN LEU PRO HIS LEU LEU LYS ASP
SEQRES 5 B 98 VAL GLY SER LEU ASP GLU LYS MET LYS SER LEU ASP VAL
SEQRES 6 B 98 ASN GLN ASP SER GLU LEU LYS PHE ASN GLU TYR TRP ARG
SEQRES 7 B 98 LEU ILE GLY GLU LEU ALA LYS GLU ILE ARG LYS LYS LYS
SEQRES 8 B 98 ASP LEU LYS ILE ARG LYS LYS
HELIX 1 1 THR A 7 PHE A 20 1 14
HELIX 2 2 SER A 34 LEU A 46 1 13
HELIX 3 3 GLY A 54 GLN A 67 1 14
HELIX 4 4 LYS A 72 ILE A 87 1 16
HELIX 5 5 THR B 7 PHE B 20 1 14
HELIX 6 6 SER B 34 LEU B 46 1 13
HELIX 7 7 VAL B 53 GLN B 67 1 15
HELIX 8 8 LYS B 72 ILE B 87 1 16
CISPEP 1 ASP A 31 SER A 32 1 -0.39
CISPEP 2 ALA B 2 ALA B 3 3 3.65
CISPEP 3 MET B 1 ALA B 2 4 -5.84
CISPEP 4 ALA B 3 GLU B 4 11 10.97
CISPEP 5 GLU B 4 PRO B 5 12 -19.60
CISPEP 6 MET B 1 ALA B 2 15 -20.41
CISPEP 7 ALA B 3 GLU B 4 16 27.31
CISPEP 8 THR A 22 PHE A 23 17 -13.62
CISPEP 9 PHE A 23 ALA A 24 17 6.01
CISPEP 10 ALA B 2 ALA B 3 17 5.61
CISPEP 11 MET B 1 ALA B 2 23 -26.99
CISPEP 12 MET B 1 ALA B 2 24 -26.35
CISPEP 13 ALA B 3 GLU B 4 24 28.34
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 2 2 Bytes