Header list of 1yuu.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 14-FEB-05 1YUU
TITLE SOLUTION STRUCTURE OF CALCIUM-S100A13
CAVEAT 1YUU 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 1YUU 1 REMARK LINK
REVDAT 2 24-FEB-09 1YUU 1 VERSN
REVDAT 1 18-OCT-05 1YUU 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 1.5, 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 1YUU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031943.
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 : 19
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 1 LEU A 93 C - N - CA ANGL. DEV. = 18.1 DEGREES
REMARK 500 1 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 2 LYS A 91 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 2 MET B 1 CA - CB - CG ANGL. DEV. = 17.5 DEGREES
REMARK 500 3 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 3 ARG A 88 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 4 ARG A 88 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 4 MET B 1 CA - CB - CG ANGL. DEV. = 10.3 DEGREES
REMARK 500 4 ASN B 36 C - N - CA ANGL. DEV. = 19.6 DEGREES
REMARK 500 5 ARG A 78 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 5 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 6 TRP A 77 CZ3 - CH2 - CZ2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 6 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 7 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 8 ARG A 88 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 8 ASP B 68 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 8 ARG B 88 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 ARG B 88 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 MET B 1 CA - CB - CG ANGL. DEV. = 21.9 DEGREES
REMARK 500 9 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 9 ASP B 52 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 10 ARG A 78 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 11 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 11 GLU B 4 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 12 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 12 LYS A 91 C - N - CA ANGL. DEV. = 19.3 DEGREES
REMARK 500 12 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 12 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 13 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 14 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 14 MET B 1 CA - CB - CG ANGL. DEV. = 18.9 DEGREES
REMARK 500 15 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 15 TRP A 77 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 15 LYS A 89 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 16 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 16 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 16 ARG B 88 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 17 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 17 ARG B 96 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 18 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 20 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 20 ASP B 68 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 21 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 22 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 22 ASP B 52 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 23 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 23 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 24 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 24 TRP A 77 CZ3 - CH2 - CZ2 ANGL. DEV. = -7.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 53 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 3 71.47 100.71
REMARK 500 1 ARG A 29 103.25 66.13
REMARK 500 1 LYS A 30 64.71 -62.92
REMARK 500 1 ASP A 31 -30.08 -177.20
REMARK 500 1 GLN A 45 -127.64 -98.00
REMARK 500 1 LEU A 46 59.56 29.70
REMARK 500 1 LEU A 49 -97.20 -64.84
REMARK 500 1 LYS A 91 -81.87 -158.53
REMARK 500 1 ASP A 92 -35.81 137.21
REMARK 500 1 LEU A 93 -153.13 161.51
REMARK 500 1 ARG A 96 -113.49 -79.00
REMARK 500 1 LYS A 97 132.64 -176.78
REMARK 500 1 ALA B 2 134.74 61.05
REMARK 500 1 ALA B 3 92.48 79.27
REMARK 500 1 ARG B 29 73.12 49.15
REMARK 500 1 LYS B 30 49.78 -78.89
REMARK 500 1 ASP B 31 -48.94 -161.03
REMARK 500 1 ASN B 36 57.25 -158.53
REMARK 500 1 GLU B 37 -57.60 -176.29
REMARK 500 1 VAL B 65 -19.95 -36.95
REMARK 500 1 GLN B 67 -29.56 82.43
REMARK 500 1 ASP B 68 109.16 -50.80
REMARK 500 1 SER B 69 66.93 -66.85
REMARK 500 1 ASN B 74 50.73 -167.37
REMARK 500 1 GLU B 75 -60.69 -93.21
REMARK 500 1 LYS B 91 49.77 73.93
REMARK 500 1 LYS B 97 136.14 -178.16
REMARK 500 2 ALA A 3 99.11 100.09
REMARK 500 2 GLU A 27 75.75 -106.05
REMARK 500 2 ARG A 29 100.38 28.72
REMARK 500 2 LYS A 30 65.06 -69.38
REMARK 500 2 ASP A 31 -45.08 -169.31
REMARK 500 2 LEU A 46 29.13 -155.04
REMARK 500 2 ASP A 52 74.05 61.21
REMARK 500 2 SER A 69 16.56 99.92
REMARK 500 2 LYS A 90 -34.51 -37.73
REMARK 500 2 LYS A 91 61.53 -158.44
REMARK 500 2 ASP A 92 -111.12 7.57
REMARK 500 2 ARG A 96 -68.27 -149.46
REMARK 500 2 LYS A 97 138.24 177.01
REMARK 500 2 ALA B 2 167.42 86.94
REMARK 500 2 ALA B 3 100.24 101.66
REMARK 500 2 GLU B 4 -78.15 -132.43
REMARK 500 2 THR B 7 -154.35 -73.98
REMARK 500 2 GLU B 27 -74.87 -91.72
REMARK 500 2 ARG B 29 102.93 36.25
REMARK 500 2 LYS B 30 34.82 -72.11
REMARK 500 2 ASP B 31 -50.82 -147.80
REMARK 500 2 GLU B 37 -52.49 -155.03
REMARK 500 2 LEU B 49 -62.82 -18.84
REMARK 500
REMARK 500 THIS ENTRY HAS 814 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 ALA B 2 ALA B 3 1 112.84
REMARK 500 GLN B 45 LEU B 46 1 -136.43
REMARK 500 LEU B 46 PRO B 47 1 -36.21
REMARK 500 PHE B 73 ASN B 74 1 111.91
REMARK 500 ASN B 74 GLU B 75 1 140.71
REMARK 500 LYS B 90 LYS B 91 1 -143.10
REMARK 500 LYS B 97 LYS B 98 1 148.05
REMARK 500 ARG B 25 GLN B 26 2 -143.14
REMARK 500 GLY B 28 ARG B 29 2 142.39
REMARK 500 LEU B 46 PRO B 47 2 -126.35
REMARK 500 ASP B 64 VAL B 65 2 -137.85
REMARK 500 PHE B 73 ASN B 74 2 112.80
REMARK 500 ASN B 74 GLU B 75 2 142.23
REMARK 500 GLY B 28 ARG B 29 3 139.12
REMARK 500 ASN B 36 GLU B 37 3 144.50
REMARK 500 GLN B 45 LEU B 46 3 -143.16
REMARK 500 LEU B 46 PRO B 47 3 -145.15
REMARK 500 ASP B 64 VAL B 65 3 -130.87
REMARK 500 PHE B 73 ASN B 74 3 109.69
REMARK 500 LYS A 91 ASP A 92 4 147.53
REMARK 500 ALA B 2 ALA B 3 4 124.10
REMARK 500 ALA B 3 GLU B 4 4 131.31
REMARK 500 GLU B 4 PRO B 5 4 -147.19
REMARK 500 PRO B 5 LEU B 6 4 -149.42
REMARK 500 GLY B 28 ARG B 29 4 136.77
REMARK 500 ASP B 64 VAL B 65 4 -131.01
REMARK 500 PHE B 73 ASN B 74 4 125.76
REMARK 500 ASN B 74 GLU B 75 4 131.49
REMARK 500 LYS B 97 LYS B 98 4 148.82
REMARK 500 MET A 1 ALA A 2 5 149.45
REMARK 500 LYS A 94 ILE A 95 5 147.49
REMARK 500 LYS A 97 LYS A 98 5 128.51
REMARK 500 ALA B 2 ALA B 3 5 143.62
REMARK 500 LEU B 9 GLU B 10 5 138.40
REMARK 500 VAL B 35 ASN B 36 5 130.52
REMARK 500 LEU B 46 PRO B 47 5 -147.64
REMARK 500 ASP B 64 VAL B 65 5 -141.09
REMARK 500 PHE B 73 ASN B 74 5 126.58
REMARK 500 LYS A 91 ASP A 92 6 -147.23
REMARK 500 ILE A 95 ARG A 96 6 -144.90
REMARK 500 LYS A 97 LYS A 98 6 127.86
REMARK 500 ARG B 25 GLN B 26 6 -126.57
REMARK 500 VAL B 35 ASN B 36 6 143.91
REMARK 500 LEU B 46 PRO B 47 6 -78.21
REMARK 500 ASP B 64 VAL B 65 6 -134.95
REMARK 500 PHE B 73 ASN B 74 6 102.12
REMARK 500 LYS B 91 ASP B 92 6 -140.34
REMARK 500 LYS A 97 LYS A 98 7 -141.61
REMARK 500 GLY B 28 ARG B 29 7 131.89
REMARK 500 SER B 32 LEU B 33 7 147.09
REMARK 500
REMARK 500 THIS ENTRY HAS 204 NON CIS, NON-TRANS OMEGA 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 PHE A 21 0.10 SIDE CHAIN
REMARK 500 2 PHE A 23 0.11 SIDE CHAIN
REMARK 500 2 ARG A 25 0.09 SIDE CHAIN
REMARK 500 2 PHE B 20 0.10 SIDE CHAIN
REMARK 500 2 TYR B 76 0.10 SIDE CHAIN
REMARK 500 2 ARG B 78 0.09 SIDE CHAIN
REMARK 500 2 ARG B 88 0.08 SIDE CHAIN
REMARK 500 3 PHE A 21 0.12 SIDE CHAIN
REMARK 500 3 PHE A 73 0.10 SIDE CHAIN
REMARK 500 3 ARG A 78 0.14 SIDE CHAIN
REMARK 500 3 ARG A 88 0.11 SIDE CHAIN
REMARK 500 3 PHE B 20 0.08 SIDE CHAIN
REMARK 500 3 TYR B 76 0.09 SIDE CHAIN
REMARK 500 4 ARG A 88 0.10 SIDE CHAIN
REMARK 500 4 ARG B 78 0.09 SIDE CHAIN
REMARK 500 5 PHE B 38 0.09 SIDE CHAIN
REMARK 500 5 ARG B 78 0.12 SIDE CHAIN
REMARK 500 6 TYR A 76 0.08 SIDE CHAIN
REMARK 500 6 PHE B 21 0.13 SIDE CHAIN
REMARK 500 6 PHE B 38 0.08 SIDE CHAIN
REMARK 500 6 PHE B 73 0.09 SIDE CHAIN
REMARK 500 6 ARG B 78 0.08 SIDE CHAIN
REMARK 500 7 TYR A 76 0.07 SIDE CHAIN
REMARK 500 7 PHE B 21 0.08 SIDE CHAIN
REMARK 500 7 PHE B 38 0.07 SIDE CHAIN
REMARK 500 8 TYR A 76 0.07 SIDE CHAIN
REMARK 500 8 ARG A 88 0.10 SIDE CHAIN
REMARK 500 8 ARG B 29 0.09 SIDE CHAIN
REMARK 500 8 TYR B 76 0.13 SIDE CHAIN
REMARK 500 8 ARG B 88 0.10 SIDE CHAIN
REMARK 500 9 PHE B 23 0.08 SIDE CHAIN
REMARK 500 9 PHE B 38 0.14 SIDE CHAIN
REMARK 500 9 TYR B 76 0.10 SIDE CHAIN
REMARK 500 9 ARG B 78 0.09 SIDE CHAIN
REMARK 500 10 PHE A 38 0.11 SIDE CHAIN
REMARK 500 10 PHE A 73 0.10 SIDE CHAIN
REMARK 500 10 ARG A 88 0.09 SIDE CHAIN
REMARK 500 11 ARG A 25 0.08 SIDE CHAIN
REMARK 500 11 ARG B 29 0.18 SIDE CHAIN
REMARK 500 11 PHE B 38 0.09 SIDE CHAIN
REMARK 500 11 TYR B 76 0.10 SIDE CHAIN
REMARK 500 12 TYR A 76 0.12 SIDE CHAIN
REMARK 500 12 ARG A 88 0.13 SIDE CHAIN
REMARK 500 12 ARG A 96 0.14 SIDE CHAIN
REMARK 500 12 PHE B 38 0.08 SIDE CHAIN
REMARK 500 12 HIS B 48 0.09 SIDE CHAIN
REMARK 500 13 PHE A 38 0.12 SIDE CHAIN
REMARK 500 13 ARG A 78 0.14 SIDE CHAIN
REMARK 500 13 TYR B 76 0.10 SIDE CHAIN
REMARK 500 14 PHE A 21 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 97 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 7 VAL B 35 15.31
REMARK 500 10 VAL B 35 13.82
REMARK 500 16 VAL B 35 10.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 197 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 24 O
REMARK 620 2 GLU A 27 O 82.4
REMARK 620 3 GLY A 28 O 110.5 68.7
REMARK 620 4 ARG A 29 O 61.2 97.0 61.7
REMARK 620 5 SER A 32 O 92.6 165.3 100.5 68.5
REMARK 620 6 GLU A 37 OE1 113.9 111.3 135.2 150.7 83.4
REMARK 620 7 GLU A 37 OE2 72.0 71.7 139.4 133.1 120.1 55.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 198 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD1
REMARK 620 2 ASN A 66 OD1 81.3
REMARK 620 3 ASP A 68 OD1 87.4 88.9
REMARK 620 4 ASP A 68 OD2 131.9 70.2 55.1
REMARK 620 5 GLU A 70 O 82.3 156.5 73.7 109.9
REMARK 620 6 GLU A 75 OE1 94.0 127.7 143.2 134.1 70.1
REMARK 620 7 GLU A 75 OE2 92.0 73.6 162.3 114.7 123.8 54.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 199 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 24 O
REMARK 620 2 GLY B 28 O 83.4
REMARK 620 3 ARG B 29 O 68.8 73.9
REMARK 620 4 SER B 32 O 112.9 131.9 71.5
REMARK 620 5 GLU B 37 OE1 119.0 122.6 161.2 89.8
REMARK 620 6 GLU B 37 OE2 78.7 82.8 141.6 143.0 55.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 200 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 64 OD1
REMARK 620 2 ASP B 64 O 62.1
REMARK 620 3 ASP B 68 OD1 133.3 87.0
REMARK 620 4 ASP B 68 OD2 140.6 141.1 54.4
REMARK 620 5 ASP B 68 O 71.9 93.4 76.4 74.9
REMARK 620 6 GLU B 70 O 77.4 138.4 130.9 77.6 82.1
REMARK 620 7 GLU B 75 OE1 103.4 106.2 119.1 97.7 155.0 73.0
REMARK 620 8 GLU B 75 OE2 94.7 54.9 94.2 124.6 147.7 124.5 55.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YUR RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO-S100A13 (MINIMIZED MEAN STRUCTURE)
REMARK 900 RELATED ID: 1YUS RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO-S100A13
REMARK 900 RELATED ID: 1YUT RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-S100A13 (MINIMIZED MEAN STRUCTURE)
REMARK 900 RELATED ID: CIRMMP11 RELATED DB: TARGETDB
DBREF 1YUU A 1 98 UNP Q99584 S10AD_HUMAN 1 98
DBREF 1YUU 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
HET CA A 197 1
HET CA A 198 1
HET CA B 199 1
HET CA B 200 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 1 THR A 7 GLN A 26 1 20
HELIX 2 2 SER A 34 GLN A 45 1 12
HELIX 3 3 SER A 55 ASP A 64 1 10
HELIX 4 4 PHE A 73 ILE A 87 1 15
HELIX 5 5 THR B 7 ARG B 25 1 19
HELIX 6 6 GLU B 37 GLN B 45 1 9
HELIX 7 7 SER B 55 ASP B 64 1 10
HELIX 8 8 TYR B 76 ILE B 87 1 12
SHEET 1 A 2 SER A 32 LEU A 33 0
SHEET 2 A 2 LEU A 71 LYS A 72 -1 O LEU A 71 N LEU A 33
LINK O ALA A 24 CA CA A 197 1555 1555 2.30
LINK O GLU A 27 CA CA A 197 1555 1555 2.34
LINK O GLY A 28 CA CA A 197 1555 1555 2.36
LINK O ARG A 29 CA CA A 197 1555 1555 3.00
LINK O SER A 32 CA CA A 197 1555 1555 2.33
LINK OE1 GLU A 37 CA CA A 197 1555 1555 2.27
LINK OE2 GLU A 37 CA CA A 197 1555 1555 2.30
LINK OD1 ASP A 64 CA CA A 198 1555 1555 2.19
LINK OD1 ASN A 66 CA CA A 198 1555 1555 2.47
LINK OD1 ASP A 68 CA CA A 198 1555 1555 2.28
LINK OD2 ASP A 68 CA CA A 198 1555 1555 2.31
LINK O GLU A 70 CA CA A 198 1555 1555 2.34
LINK OE1 GLU A 75 CA CA A 198 1555 1555 2.32
LINK OE2 GLU A 75 CA CA A 198 1555 1555 2.33
LINK O ALA B 24 CA CA B 199 1555 1555 2.33
LINK O GLY B 28 CA CA B 199 1555 1555 2.28
LINK O ARG B 29 CA CA B 199 1555 1555 2.43
LINK O SER B 32 CA CA B 199 1555 1555 2.33
LINK OE1 GLU B 37 CA CA B 199 1555 1555 2.27
LINK OE2 GLU B 37 CA CA B 199 1555 1555 2.28
LINK OD1 ASP B 64 CA CA B 200 1555 1555 2.22
LINK O ASP B 64 CA CA B 200 1555 1555 3.27
LINK OD1 ASP B 68 CA CA B 200 1555 1555 2.31
LINK OD2 ASP B 68 CA CA B 200 1555 1555 2.34
LINK O ASP B 68 CA CA B 200 1555 1555 2.36
LINK O GLU B 70 CA CA B 200 1555 1555 2.33
LINK OE1 GLU B 75 CA CA B 200 1555 1555 2.30
LINK OE2 GLU B 75 CA CA B 200 1555 1555 2.31
CISPEP 1 ASP A 92 LEU A 93 1 -15.79
CISPEP 2 GLU B 27 GLY B 28 1 7.57
CISPEP 3 VAL B 35 ASN B 36 2 9.89
CISPEP 4 LEU B 46 PRO B 47 4 -25.07
CISPEP 5 GLU B 10 GLU B 11 5 19.72
CISPEP 6 GLU B 27 GLY B 28 5 18.11
CISPEP 7 ARG A 96 LYS A 97 9 -1.66
CISPEP 8 LYS A 89 LYS A 90 12 -21.12
CISPEP 9 LYS A 90 LYS A 91 12 -13.54
CISPEP 10 ALA B 2 ALA B 3 12 27.45
CISPEP 11 LYS A 97 LYS A 98 13 4.02
CISPEP 12 ALA B 2 ALA B 3 18 11.84
CISPEP 13 GLU B 27 GLY B 28 18 -4.52
CISPEP 14 GLY B 28 ARG B 29 22 27.35
CISPEP 15 GLU B 27 GLY B 28 23 9.58
SITE 1 AC1 6 ALA A 24 GLU A 27 GLY A 28 ARG A 29
SITE 2 AC1 6 SER A 32 GLU A 37
SITE 1 AC2 5 ASP A 64 ASN A 66 ASP A 68 GLU A 70
SITE 2 AC2 5 GLU A 75
SITE 1 AC3 5 ALA B 24 GLY B 28 ARG B 29 SER B 32
SITE 2 AC3 5 GLU B 37
SITE 1 AC4 4 ASP B 64 ASP B 68 GLU B 70 GLU B 75
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