Header list of 2cxj.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 30-JUN-05 2CXJ
TITLE 3D SOLUTION STRUCTURE OF S100A13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S100 CALCIUM-BINDING PROTEIN A13;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100A13;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLYS
KEYWDS S100A13, SOLUTION, FGF, NON-CLASSICAL SECRETION, CALCIUM, METAL
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.VAITHIYALINGAM,T.K.S.KUMAR,C.YU
REVDAT 3 09-MAR-22 2CXJ 1 REMARK
REVDAT 2 24-FEB-09 2CXJ 1 VERSN
REVDAT 1 30-JUN-06 2CXJ 0
JRNL AUTH S.VAITHIYALINGAM,T.K.S.KUMAR,C.YU
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF S100A13
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (CNS), A.T. BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CXJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000024737.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 25MM TRIS-HCL, 0.3MM CALCIUM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : PROTEIN (S100A13)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, SPARKY 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D & 3D HOMO-
REMARK 210 AND HETERONUCLEAR 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 O LEU A 41 H GLN A 45 1.54
REMARK 500 O LEU B 41 H GLN B 45 1.58
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 GLU A 4 -90.14 -73.76
REMARK 500 1 THR A 5 -155.15 -88.19
REMARK 500 1 THR A 19 -88.98 -86.57
REMARK 500 1 ARG A 29 162.00 -42.70
REMARK 500 1 LYS A 30 51.49 -98.36
REMARK 500 1 ASN A 34 -117.43 -117.72
REMARK 500 1 ILE A 35 28.46 -143.15
REMARK 500 1 LEU A 41 -91.35 -76.46
REMARK 500 1 ALA A 42 -37.90 -38.66
REMARK 500 1 LEU A 46 -70.72 -42.93
REMARK 500 1 LEU A 49 -79.91 -82.09
REMARK 500 1 LEU A 50 49.26 -86.18
REMARK 500 1 LYS A 51 152.56 -39.46
REMARK 500 1 VAL A 53 84.38 100.66
REMARK 500 1 THR A 62 -28.77 -38.84
REMARK 500 1 VAL A 65 -77.78 -55.87
REMARK 500 1 ASN A 66 49.35 -82.84
REMARK 500 1 ASP A 68 37.96 -88.47
REMARK 500 1 PHE A 73 -97.79 -97.19
REMARK 500 1 GLU A 75 24.23 -62.60
REMARK 500 1 ARG A 88 -73.19 -43.05
REMARK 500 1 ILE A 95 60.94 -66.09
REMARK 500 1 GLU B 4 -89.34 -73.43
REMARK 500 1 THR B 5 -155.16 -89.06
REMARK 500 1 THR B 19 -90.77 -86.07
REMARK 500 1 ARG B 29 161.84 -41.95
REMARK 500 1 LYS B 30 51.79 -98.35
REMARK 500 1 ASN B 34 -117.90 -115.71
REMARK 500 1 ILE B 35 27.26 -142.27
REMARK 500 1 LEU B 41 -88.01 -81.24
REMARK 500 1 LEU B 46 -72.16 -42.00
REMARK 500 1 HIS B 48 -164.17 -100.72
REMARK 500 1 LEU B 49 -80.31 -82.72
REMARK 500 1 LEU B 50 49.15 -86.88
REMARK 500 1 LYS B 51 157.62 -39.15
REMARK 500 1 VAL B 53 75.98 101.45
REMARK 500 1 VAL B 65 -73.73 -55.24
REMARK 500 1 ASN B 66 35.71 -83.95
REMARK 500 1 ASP B 68 36.74 -87.35
REMARK 500 1 PHE B 73 -94.23 -97.81
REMARK 500 1 GLU B 75 25.75 -63.35
REMARK 500 1 ARG B 88 -73.06 -42.04
REMARK 500 1 ILE B 95 62.92 -64.53
REMARK 500 2 GLU A 4 -87.49 -65.53
REMARK 500 2 THR A 5 -160.32 -78.23
REMARK 500 2 THR A 19 -91.96 -88.00
REMARK 500 2 ARG A 29 165.14 -42.02
REMARK 500 2 ASN A 34 -166.56 -118.64
REMARK 500 2 LEU A 41 -93.62 -73.53
REMARK 500 2 ALA A 42 -34.25 -37.98
REMARK 500
REMARK 500 THIS ENTRY HAS 756 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2CXJ A 1 98 UNP P97352 S10AD_MOUSE 1 98
DBREF 2CXJ B 1 98 UNP P97352 S10AD_MOUSE 1 98
SEQRES 1 A 98 MET ALA ALA GLU THR LEU THR GLU LEU GLU ALA ALA ILE
SEQRES 2 A 98 GLU THR VAL VAL SER THR PHE PHE THR PHE ALA GLY ARG
SEQRES 3 A 98 GLU GLY ARG LYS GLY SER LEU ASN ILE ASN GLU PHE LYS
SEQRES 4 A 98 GLU LEU ALA THR GLN GLN LEU PRO HIS LEU LEU LYS ASP
SEQRES 5 A 98 VAL GLY SER LEU ASP GLU LYS MET LYS THR LEU ASP VAL
SEQRES 6 A 98 ASN GLN ASP SER GLU LEU ARG PHE SER GLU TYR TRP ARG
SEQRES 7 A 98 LEU ILE GLY GLU LEU ALA LYS GLU VAL ARG LYS GLU LYS
SEQRES 8 A 98 ALA LEU GLY ILE ARG LYS LYS
SEQRES 1 B 98 MET ALA ALA GLU THR LEU THR GLU LEU GLU ALA ALA ILE
SEQRES 2 B 98 GLU THR VAL VAL SER THR PHE PHE THR PHE ALA GLY ARG
SEQRES 3 B 98 GLU GLY ARG LYS GLY SER LEU ASN ILE ASN GLU PHE LYS
SEQRES 4 B 98 GLU LEU ALA THR GLN GLN LEU PRO HIS LEU LEU LYS ASP
SEQRES 5 B 98 VAL GLY SER LEU ASP GLU LYS MET LYS THR LEU ASP VAL
SEQRES 6 B 98 ASN GLN ASP SER GLU LEU ARG PHE SER GLU TYR TRP ARG
SEQRES 7 B 98 LEU ILE GLY GLU LEU ALA LYS GLU VAL ARG LYS GLU LYS
SEQRES 8 B 98 ALA LEU GLY ILE ARG LYS LYS
HELIX 1 1 LEU A 9 PHE A 20 1 12
HELIX 2 2 PHE A 21 GLU A 27 5 7
HELIX 3 3 ASN A 36 LYS A 39 5 4
HELIX 4 4 GLU A 40 LEU A 46 1 7
HELIX 5 5 SER A 55 ASN A 66 1 12
HELIX 6 6 TYR A 76 GLY A 81 1 6
HELIX 7 7 GLY A 81 GLY A 94 1 14
HELIX 8 8 LEU B 9 THR B 19 1 11
HELIX 9 9 PHE B 20 GLU B 27 5 8
HELIX 10 10 ASN B 36 LYS B 39 5 4
HELIX 11 11 GLU B 40 LEU B 46 1 7
HELIX 12 12 SER B 55 ASN B 66 1 12
HELIX 13 13 TYR B 76 GLY B 81 1 6
HELIX 14 14 GLY B 81 GLY B 94 1 14
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 9 2 Bytes