Header list of 1ysm.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 08-FEB-05 1YSM
TITLE NMR STRUCTURE OF N-TERMINAL DOMAIN (RESIDUES 1-77) OF SIAH-INTERACTING
TITLE 2 PROTEIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCYCLIN-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: CACYBP, SIAH-INTERACTING PROTEIN, SIP;
COMPND 6 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 GENE: CACYBP, SIP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS HELIX-TURN-HELIX, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.BHATTACHARYA,Y.T.LEE,W.MICHOWSKI,B.JASTRZEBSKA,A.FILIPEK,
AUTHOR 2 J.KUZNICKI,W.J.CHAZIN
REVDAT 3 02-MAR-22 1YSM 1 REMARK
REVDAT 2 24-FEB-09 1YSM 1 VERSN
REVDAT 1 26-JUL-05 1YSM 0
JRNL AUTH S.BHATTACHARYA,Y.T.LEE,W.MICHOWSKI,B.JASTRZEBSKA,A.FILIPEK,
JRNL AUTH 2 J.KUZNICKI,W.J.CHAZIN
JRNL TITL THE MODULAR STRUCTURE OF SIP FACILITATES ITS ROLE IN
JRNL TITL 2 STABILIZING MULTIPROTEIN ASSEMBLIES.
JRNL REF BIOCHEMISTRY V. 44 9462 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15996101
JRNL DOI 10.1021/BI0502689
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, D. A. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YSM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031884.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20 MM NAPI, 50 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM 15N/13C-ENRICHED SIP(1-77),
REMARK 210 20 MM NAPI, 50 MM NACL; 1 MM 15N-
REMARK 210 ENRICHED SIP(1-77), 20 MM NAPI,
REMARK 210 50 MM NACL; 1 MM U-SIP(1-77), 20
REMARK 210 MM NAPI, 50 MM NACL; 1 MM 13C-
REMARK 210 ENRICHED SIP(1-77), 20 MM NAPI,
REMARK 210 50 MM NACL; 1 MM 10% 13C-
REMARK 210 ENRICHED SIP(1-77), 20 MM NAPI,
REMARK 210 50 MM NACL; 1 MM U-SIP(1-77), 20
REMARK 210 MM NAPI, 50 MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; HNHB; 3D-
REMARK 210 HACAHB-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, SANE 1.0, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING RESTRAINED MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY, LEAST RESTRAINT
REMARK 210 VIOLATIONS AND LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: STEREOSPECIFIC METHYL GROUP ASSIGNMENTS WERE MADE WITH 10%
REMARK 210 13C-ENRICHED SIP(1-77) SAMPLE.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 56
REMARK 465 ASP A 57
REMARK 465 ASN A 58
REMARK 465 GLU A 59
REMARK 465 LYS A 60
REMARK 465 PRO A 61
REMARK 465 ALA A 62
REMARK 465 ALA A 63
REMARK 465 VAL A 64
REMARK 465 VAL A 65
REMARK 465 ALA A 66
REMARK 465 PRO A 67
REMARK 465 LEU A 68
REMARK 465 THR A 69
REMARK 465 THR A 70
REMARK 465 GLY A 71
REMARK 465 TYR A 72
REMARK 465 THR A 73
REMARK 465 VAL A 74
REMARK 465 LYS A 75
REMARK 465 ILE A 76
REMARK 465 SER A 77
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 18 ARG A 26 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 LYS A 25 -37.37 63.10
REMARK 500 1 ARG A 26 -38.11 -33.66
REMARK 500 1 LYS A 49 -83.78 -84.13
REMARK 500 1 SER A 50 28.80 43.16
REMARK 500 2 THR A 23 12.06 -65.72
REMARK 500 2 LYS A 25 -43.54 70.70
REMARK 500 2 GLN A 47 64.91 -160.11
REMARK 500 3 THR A 23 37.89 -65.57
REMARK 500 3 LYS A 49 -130.47 86.44
REMARK 500 3 GLN A 51 -71.89 63.02
REMARK 500 3 LYS A 52 -69.67 60.23
REMARK 500 4 LYS A 21 -70.71 -73.63
REMARK 500 4 THR A 23 42.77 -73.01
REMARK 500 5 THR A 23 45.16 -72.43
REMARK 500 5 GLN A 48 -69.81 59.14
REMARK 500 5 SER A 50 47.86 -76.18
REMARK 500 6 SER A 22 48.44 -82.89
REMARK 500 6 THR A 23 26.87 -71.66
REMARK 500 6 LYS A 25 -40.12 -172.02
REMARK 500 6 MET A 46 -72.69 -69.94
REMARK 500 6 SER A 50 -37.99 66.56
REMARK 500 7 THR A 23 42.80 -68.55
REMARK 500 7 MET A 46 -70.46 -63.01
REMARK 500 7 GLN A 48 -34.10 67.76
REMARK 500 8 THR A 23 38.44 -67.39
REMARK 500 8 MET A 46 -70.96 -91.03
REMARK 500 8 SER A 50 -80.88 60.03
REMARK 500 8 LYS A 53 83.43 62.70
REMARK 500 9 THR A 23 38.93 -72.61
REMARK 500 9 SER A 50 45.80 -76.60
REMARK 500 10 SER A 22 47.51 -74.90
REMARK 500 10 LYS A 25 -48.39 73.15
REMARK 500 10 ARG A 26 -7.84 -57.90
REMARK 500 10 GLN A 48 -80.26 55.96
REMARK 500 10 LYS A 49 -57.92 64.19
REMARK 500 10 LYS A 52 45.67 -76.82
REMARK 500 10 LYS A 53 146.45 177.12
REMARK 500 11 THR A 23 -55.03 71.66
REMARK 500 11 LYS A 25 -35.08 73.50
REMARK 500 11 GLN A 48 41.10 -75.07
REMARK 500 11 GLN A 51 -51.37 -145.09
REMARK 500 12 LYS A 21 -72.59 -79.64
REMARK 500 12 THR A 23 38.21 -76.59
REMARK 500 12 GLN A 51 -45.33 72.77
REMARK 500 12 LYS A 52 -68.10 -122.60
REMARK 500 13 THR A 23 -32.22 70.18
REMARK 500 13 ARG A 24 150.17 -44.11
REMARK 500 13 LYS A 25 4.54 -60.78
REMARK 500 13 GLN A 48 105.20 -57.03
REMARK 500 13 LYS A 52 79.34 -67.67
REMARK 500
REMARK 500 THIS ENTRY HAS 77 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 26 0.08 SIDE CHAIN
REMARK 500 2 ARG A 24 0.10 SIDE CHAIN
REMARK 500 5 ARG A 26 0.11 SIDE CHAIN
REMARK 500 6 ARG A 24 0.13 SIDE CHAIN
REMARK 500 8 ARG A 28 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YSM A 1 77 UNP Q9CXW3 CYBP_MOUSE 1 77
SEQRES 1 A 77 MET ALA SER VAL LEU GLU GLU LEU GLN LYS ASP LEU GLU
SEQRES 2 A 77 GLU VAL LYS VAL LEU LEU GLU LYS SER THR ARG LYS ARG
SEQRES 3 A 77 LEU ARG ASP THR LEU THR SER GLU LYS SER LYS ILE GLU
SEQRES 4 A 77 THR GLU LEU LYS ASN LYS MET GLN GLN LYS SER GLN LYS
SEQRES 5 A 77 LYS PRO GLU LEU ASP ASN GLU LYS PRO ALA ALA VAL VAL
SEQRES 6 A 77 ALA PRO LEU THR THR GLY TYR THR VAL LYS ILE SER
HELIX 1 1 MET A 1 SER A 22 1 22
HELIX 2 2 ARG A 26 GLN A 48 1 23
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