Header list of 1s62.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN TRANSPORT 22-JAN-04 1S62
TITLE SOLUTION STRUCTURE OF THE ESCHERICHIA COLI TOLA C-TERMINAL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 325-421);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: TOLA, CIM, EXCC, LKY, B0739;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K12 SUBSTR. W3110;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 316407;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: W3110;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTOLAIII3
KEYWDS TOL G3P INTERACTION, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR C.DEPREZ,L.BLANCHARD,J.-P.SIMORRE,M.GAVIOLI,F.GUERLESQUIN,
AUTHOR 2 C.LAZDUNSKI,R.LLOUBES,D.MARION
REVDAT 4 02-MAR-22 1S62 1 REMARK SEQADV
REVDAT 3 28-APR-09 1S62 1 REMARK
REVDAT 2 24-FEB-09 1S62 1 VERSN
REVDAT 1 15-FEB-05 1S62 0
JRNL AUTH C.DEPREZ,R.LLOUBES,M.GAVIOLI,D.MARION,F.GUERLESQUIN,
JRNL AUTH 2 L.BLANCHARD
JRNL TITL SOLUTION STRUCTURE OF THE E.COLI TOLA C-TERMINAL DOMAIN
JRNL TITL 2 REVEALS CONFORMATIONAL CHANGES UPON BINDING TO THE PHAGE G3P
JRNL TITL 3 N-TERMINAL DOMAIN.
JRNL REF J.MOL.BIOL. V. 346 1047 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15701516
JRNL DOI 10.1016/J.JMB.2004.12.028
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, TALOS
REMARK 3 AUTHORS : VARIAN (VNMR), CORNILESCU (TALOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S62 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021412.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300
REMARK 210 PH : 6.8; 6.8; 6.8
REMARK 210 IONIC STRENGTH : 100MN NACL, 50MM NAPO4; 50MN
REMARK 210 NACL, 50MM NAPO4; 500MN NACL,
REMARK 210 50MM NAPO4
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM U-15N, 100MN NACL, 50MM
REMARK 210 NAPO4, 90% H2O, 10% D2O; 0.5MM U-
REMARK 210 15N,13C, 50MN NACL, 50MM NAPO4,
REMARK 210 COMPLETE PROTEASE INHIBITOR
REMARK 210 (BOEHRINGER), 90% H2O, 10% D2O;
REMARK 210 0.7MM U-15N, 500MN NACL, 50MM
REMARK 210 NAPO4, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, ARIA 1.0, TALOS
REMARK 210 METHOD USED : 2 STEP SIMULATED ANNEALING
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: NOE MIXING TIME OF 0.08 S, TRIPLE-RESONANCE PROBE
REMARK 210 INCLUDING SHIELDED Z-GRADIENTS
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 1-16
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
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 HZ2 LYS A 47 OD2 ASP A 56 1.59
REMARK 500 HZ3 LYS A 40 OD2 ASP A 63 1.59
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 PHE A 3 174.78 67.81
REMARK 500 1 LYS A 7 -68.58 -144.23
REMARK 500 1 ASN A 8 65.78 -153.42
REMARK 500 1 ALA A 11 23.25 -165.67
REMARK 500 1 PHE A 31 -64.73 -122.71
REMARK 500 1 TYR A 32 -154.87 161.44
REMARK 500 1 TYR A 37 -142.63 -86.41
REMARK 500 1 PRO A 83 -75.57 -92.14
REMARK 500 1 ASN A 93 59.94 -164.38
REMARK 500 1 PRO A 100 119.94 -37.27
REMARK 500 2 PHE A 3 49.04 -106.83
REMARK 500 2 THR A 6 77.66 65.93
REMARK 500 2 LYS A 7 36.67 -90.78
REMARK 500 2 ASN A 9 95.20 -163.75
REMARK 500 2 SER A 36 49.12 -87.97
REMARK 500 2 ALA A 38 173.56 72.26
REMARK 500 2 PRO A 82 104.62 -39.17
REMARK 500 2 ASN A 93 67.69 -164.93
REMARK 500 3 ASN A 5 -60.65 70.29
REMARK 500 3 LYS A 7 80.36 62.98
REMARK 500 3 ASN A 8 -70.62 72.63
REMARK 500 3 ALA A 14 -67.50 -105.95
REMARK 500 3 SER A 29 24.48 -76.90
REMARK 500 3 LYS A 30 -33.39 -133.34
REMARK 500 3 TYR A 32 -121.13 62.02
REMARK 500 3 TYR A 37 -93.84 -92.56
REMARK 500 3 PRO A 50 0.81 -63.88
REMARK 500 3 ASN A 93 74.82 -158.11
REMARK 500 3 PRO A 100 97.66 -53.50
REMARK 500 4 PHE A 3 -103.36 -110.14
REMARK 500 4 SER A 36 -46.27 71.36
REMARK 500 4 PRO A 83 -75.50 -79.38
REMARK 500 4 ASN A 93 38.47 -151.87
REMARK 500 4 PRO A 100 107.38 -53.55
REMARK 500 4 HIS A 101 95.67 -68.20
REMARK 500 5 ASN A 8 100.68 74.81
REMARK 500 5 SER A 12 -95.47 54.94
REMARK 500 5 TYR A 32 90.60 -47.49
REMARK 500 5 ASP A 33 17.64 53.24
REMARK 500 5 TYR A 37 -117.78 -81.76
REMARK 500 5 ALA A 38 147.36 -172.68
REMARK 500 5 ASN A 93 34.64 -173.74
REMARK 500 5 PRO A 100 119.64 -31.61
REMARK 500 6 GLU A 2 94.14 62.62
REMARK 500 6 LYS A 7 57.86 -97.93
REMARK 500 6 LYS A 30 33.30 -148.89
REMARK 500 6 TYR A 32 -72.24 71.10
REMARK 500 6 ASP A 33 24.94 -149.84
REMARK 500 6 SER A 36 -73.27 -109.46
REMARK 500 6 TYR A 37 -107.57 37.23
REMARK 500
REMARK 500 THIS ENTRY HAS 137 RAMACHANDRAN OUTLIERS.
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 1 TYR A 32 -10.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4771 RELATED DB: BMRB
REMARK 900 ASSIGNMENT OF THE 1H, 15N AND 13C RESONANCES OF THE SAME PROTEIN,
REMARK 900 USED TO CALCULATE ITS STRUCTURE
DBREF 1S62 A 4 100 UNP P19934 TOLA_ECOLI 325 421
SEQADV 1S62 ALA A 1 UNP P19934 CLONING ARTIFACT
SEQADV 1S62 GLU A 2 UNP P19934 CLONING ARTIFACT
SEQADV 1S62 PHE A 3 UNP P19934 CLONING ARTIFACT
SEQADV 1S62 HIS A 101 UNP P19934 EXPRESSION TAG
SEQADV 1S62 HIS A 102 UNP P19934 EXPRESSION TAG
SEQADV 1S62 HIS A 103 UNP P19934 EXPRESSION TAG
SEQADV 1S62 HIS A 104 UNP P19934 EXPRESSION TAG
SEQADV 1S62 HIS A 105 UNP P19934 EXPRESSION TAG
SEQADV 1S62 HIS A 106 UNP P19934 EXPRESSION TAG
SEQRES 1 A 106 ALA GLU PHE GLY ASN THR LYS ASN ASN GLY ALA SER GLY
SEQRES 2 A 106 ALA ASP ILE ASN ASN TYR ALA GLY GLN ILE LYS SER ALA
SEQRES 3 A 106 ILE GLU SER LYS PHE TYR ASP ALA SER SER TYR ALA GLY
SEQRES 4 A 106 LYS THR CYS THR LEU ARG ILE LYS LEU ALA PRO ASP GLY
SEQRES 5 A 106 MET LEU LEU ASP ILE LYS PRO GLU GLY GLY ASP PRO ALA
SEQRES 6 A 106 LEU CYS GLN ALA ALA LEU ALA ALA ALA LYS LEU ALA LYS
SEQRES 7 A 106 ILE PRO LYS PRO PRO SER GLN ALA VAL TYR GLU VAL PHE
SEQRES 8 A 106 LYS ASN ALA PRO LEU ASP PHE LYS PRO HIS HIS HIS HIS
SEQRES 9 A 106 HIS HIS
HELIX 1 1 GLY A 13 SER A 29 1 17
HELIX 2 2 ASP A 63 LEU A 76 1 14
HELIX 3 3 SER A 84 LYS A 92 1 9
SHEET 1 A 2 LEU A 44 LEU A 48 0
SHEET 2 A 2 LEU A 54 PRO A 59 -1 O LYS A 58 N ARG A 45
SSBOND 1 CYS A 42 CYS A 67 1555 1555 2.03
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