Header list of 1r3b.pdb file
Complete list - r 2 2 Bytes
HEADER CELL CYCLE 01-OCT-03 1R3B
TITLE SOLUTION STRUCTURE OF XENOPUS LAEVIS MOB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (33-216);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: MOB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS LEFT-HANDED FOUR-HELIX BUNDLE, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.PONCHON,C.DUMAS,A.V.KAJAVA,D.FESQUET,A.PADILLA
REVDAT 3 02-MAR-22 1R3B 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1R3B 1 VERSN
REVDAT 1 28-SEP-04 1R3B 0
JRNL AUTH L.PONCHON,C.DUMAS,A.V.KAJAVA,D.FESQUET,A.PADILLA
JRNL TITL NMR SOLUTION STRUCTURE OF MOB1, A MITOTIC EXIT NETWORK
JRNL TITL 2 PROTEIN AND ITS INTERACTION WITH AN NDR KINASE PEPTIDE
JRNL REF J.MOL.BIOL. V. 337 167 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15001360
JRNL DOI 10.1016/J.JMB.2004.01.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GIFA 4.0, CNS 1.0
REMARK 3 AUTHORS : DELSUC (GIFA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DYANA STRUCTURES WERE ENERGY MINIMIZED
REMARK 3 IN CNS
REMARK 4
REMARK 4 1R3B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020384.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : 500MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM MOB1 U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D TOCSY; HNCO;
REMARK 210 HNCACB; HNCOCA; CBCACONH;
REMARK 210 HNCACO; 3D HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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
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 LEU A 46 147.48 -33.80
REMARK 500 1 GLU A 48 -73.12 66.95
REMARK 500 1 GLU A 80 159.02 68.53
REMARK 500 1 THR A 82 90.00 -49.81
REMARK 500 1 CYS A 83 23.16 -162.49
REMARK 500 1 SER A 84 15.19 59.44
REMARK 500 1 VAL A 85 126.57 59.35
REMARK 500 1 ALA A 97 -65.99 69.51
REMARK 500 1 ASN A 101 80.92 60.88
REMARK 500 1 LYS A 103 89.01 -156.89
REMARK 500 1 GLU A 128 87.43 -54.49
REMARK 500 1 THR A 129 -43.71 -164.42
REMARK 500 1 SER A 133 -52.87 -160.90
REMARK 500 1 LYS A 141 -53.76 177.87
REMARK 500 1 HIS A 165 73.44 -158.07
REMARK 500 1 GLN A 173 -76.61 64.55
REMARK 500 1 ASP A 196 -179.86 -179.14
REMARK 500 1 ARG A 197 167.26 63.06
REMARK 500 1 LEU A 203 -46.74 -145.49
REMARK 500 2 CYS A 83 154.15 66.65
REMARK 500 2 SER A 84 -57.15 -164.29
REMARK 500 2 TYR A 94 117.98 -171.09
REMARK 500 2 HIS A 95 10.81 -158.38
REMARK 500 2 TRP A 96 81.19 37.78
REMARK 500 2 THR A 100 -66.03 -143.55
REMARK 500 2 ILE A 102 85.92 33.54
REMARK 500 2 LYS A 103 -72.96 65.93
REMARK 500 2 SER A 133 -169.60 -67.28
REMARK 500 2 PHE A 139 -86.40 26.00
REMARK 500 2 PRO A 140 40.24 -100.02
REMARK 500 2 ASN A 142 34.45 -179.42
REMARK 500 2 HIS A 165 67.32 -110.96
REMARK 500 2 GLN A 173 -79.07 -167.23
REMARK 500 2 ARG A 197 -3.88 -147.26
REMARK 500 2 PRO A 202 64.12 -68.31
REMARK 500 2 LEU A 203 -42.45 -167.26
REMARK 500 2 SER A 212 103.03 55.36
REMARK 500 2 LYS A 213 -66.36 -176.40
REMARK 500 2 ASP A 214 108.91 60.11
REMARK 500 3 HIS A 20 -49.79 -131.02
REMARK 500 3 SER A 24 -61.24 -98.59
REMARK 500 3 SER A 25 -48.71 -147.58
REMARK 500 3 ARG A 30 166.22 61.11
REMARK 500 3 ALA A 33 128.06 63.54
REMARK 500 3 THR A 34 -45.40 -154.47
REMARK 500 3 LEU A 35 154.02 64.35
REMARK 500 3 LEU A 46 102.66 -34.07
REMARK 500 3 GLU A 48 122.08 63.07
REMARK 500 3 CYS A 78 -171.94 -69.67
REMARK 500 3 THR A 82 -67.50 68.24
REMARK 500
REMARK 500 THIS ENTRY HAS 443 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 10 ARG A 153 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R3B A 33 215 UNP Q7T1M9 Q7T1M9_XENLA 33 215
SEQADV 1R3B MET A 14 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B GLY A 15 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B SER A 16 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B SER A 17 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B HIS A 18 UNP Q7T1M9 EXPRESSION TAG
SEQADV 1R3B HIS A 19 UNP Q7T1M9 EXPRESSION TAG
SEQADV 1R3B HIS A 20 UNP Q7T1M9 EXPRESSION TAG
SEQADV 1R3B HIS A 21 UNP Q7T1M9 EXPRESSION TAG
SEQADV 1R3B HIS A 22 UNP Q7T1M9 EXPRESSION TAG
SEQADV 1R3B HIS A 23 UNP Q7T1M9 EXPRESSION TAG
SEQADV 1R3B SER A 24 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B SER A 25 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B GLY A 26 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B VAL A 28 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B PRO A 29 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B ARG A 30 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B GLY A 31 UNP Q7T1M9 CLONING ARTIFACT
SEQADV 1R3B SER A 32 UNP Q7T1M9 CLONING ARTIFACT
SEQRES 1 A 202 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 202 LEU VAL PRO ARG GLY SER ALA THR LEU GLY SER GLY ASN
SEQRES 3 A 202 LEU ARG GLN ALA VAL MET LEU PRO GLU GLY GLU ASP LEU
SEQRES 4 A 202 ASN GLU TRP ILE ALA VAL ASN THR VAL ASP PHE PHE ASN
SEQRES 5 A 202 GLN ILE ASN MET LEU TYR GLY THR ILE THR GLU PHE CYS
SEQRES 6 A 202 THR GLU SER THR CYS SER VAL MET SER ALA GLY PRO ARG
SEQRES 7 A 202 TYR GLU TYR HIS TRP ALA ASP GLY THR ASN ILE LYS LYS
SEQRES 8 A 202 PRO ILE LYS CYS SER ALA PRO LYS TYR ILE ASP TYR LEU
SEQRES 9 A 202 MET THR TRP VAL GLN ASP GLN LEU ASP ASP GLU THR LEU
SEQRES 10 A 202 PHE PRO SER LYS ILE GLY VAL PRO PHE PRO LYS ASN PHE
SEQRES 11 A 202 MET SER VAL ALA LYS THR ILE LEU LYS ARG LEU PHE ARG
SEQRES 12 A 202 VAL TYR ALA HIS ILE TYR HIS GLN HIS PHE ASP ALA VAL
SEQRES 13 A 202 MET GLN LEU GLN GLU GLU ALA HIS LEU ASN THR SER PHE
SEQRES 14 A 202 LYS HIS PHE ILE PHE PHE VAL GLN GLU PHE ASN LEU ILE
SEQRES 15 A 202 ASP ARG ARG GLU LEU ALA PRO LEU GLN GLU LEU ILE GLU
SEQRES 16 A 202 LYS LEU GLY SER LYS ASP ARG
HELIX 1 1 ASN A 39 MET A 45 1 7
HELIX 2 2 ASP A 51 THR A 75 1 25
HELIX 3 3 GLU A 76 CYS A 78 5 3
HELIX 4 4 SER A 109 ASP A 126 1 18
HELIX 5 5 LYS A 141 GLN A 164 1 24
HELIX 6 6 HIS A 165 LEU A 172 1 8
HELIX 7 7 GLU A 175 ASN A 193 1 19
HELIX 8 8 ARG A 197 ALA A 201 5 5
HELIX 9 9 LEU A 203 GLY A 211 1 9
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