Header list of 1rrz.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS,BIOSYNTHETIC PROTEIN09-DEC-03 1RRZ
TITLE SOLUTION STRUCTURE OF GLGS PROTEIN FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN SYNTHESIS PROTEIN GLGS;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GLGS, B3049;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ALL-HELICAL DOMAIN, STRUCTURAL GENOMICS, MONTREAL-KINGSTON BACTERIAL
KEYWDS 2 STRUCTURAL GENOMICS INITIATIVE, BSGI, BIOSYNTHETIC PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR G.KOZLOV,K.GEHRING,MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS
AUTHOR 2 INITIATIVE (BSGI)
REVDAT 3 02-MAR-22 1RRZ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RRZ 1 VERSN
REVDAT 1 01-JUN-04 1RRZ 0
JRNL AUTH G.KOZLOV,D.ELIAS,M.CYGLER,K.GEHRING
JRNL TITL STRUCTURE OF GLGS FROM ESCHERICHIA COLI SUGGESTS A ROLE IN
JRNL TITL 2 PROTEIN-PROTEIN INTERACTIONS.
JRNL REF BMC BIOL. V. 2 10 2004
JRNL REFN ESSN 1741-7007
JRNL PMID 15161493
JRNL DOI 10.1186/1741-7007-2-10
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, XPLOR-NIH 2.9.2
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 449 RESTRAINTS, 311 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 109 TALOS-DERIVED DIHEDRAL ANGLE RESTRAINTS,
REMARK 3 29 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1RRZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020999.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 5MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM GLGS U-15N; 5MM POTASSIUM
REMARK 210 PHOSPHATE; 1MM DTT; 0.1MM SODIUM
REMARK 210 AZIDE; 1MM GLGS; 5MM POTASSIUM
REMARK 210 PHOSPHATE; 1MM DTT; 0.1MM SODIUM
REMARK 210 AZIDE; 1MM GLGS; 5MM POTASSIUM
REMARK 210 PHOSPHATE; 1MM DTT; 0.1MM SODIUM
REMARK 210 AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, XEASY 1.3.13, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE AND HOMONUCLEAR 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: 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 1-15
REMARK 465 RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 14 H PHE A 18 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 MET A 37 106.96 64.62
REMARK 500 1 GLU A 61 -59.25 -159.81
REMARK 500 1 GLU A 65 -64.11 -132.80
REMARK 500 2 ASP A 29 87.16 -68.69
REMARK 500 2 ASP A 38 -54.53 -145.33
REMARK 500 2 GLU A 61 -77.85 -76.36
REMARK 500 2 GLU A 63 72.34 57.53
REMARK 500 3 ASP A 29 86.74 -69.62
REMARK 500 3 MET A 37 97.48 61.59
REMARK 500 3 ARG A 60 -46.01 73.20
REMARK 500 3 GLU A 61 -80.87 -153.84
REMARK 500 3 LEU A 62 -74.91 60.29
REMARK 500 4 ASP A 38 -44.83 -139.13
REMARK 500 4 LEU A 62 -52.72 -126.08
REMARK 500 5 ASP A 2 65.74 -119.57
REMARK 500 5 HIS A 3 -167.35 -115.95
REMARK 500 5 ASP A 38 -43.17 -138.74
REMARK 500 5 ARG A 60 -70.94 -65.06
REMARK 500 5 GLU A 61 -84.65 59.58
REMARK 500 5 GLU A 65 -57.43 -126.71
REMARK 500 6 ASP A 2 -173.82 57.62
REMARK 500 6 HIS A 3 177.06 62.06
REMARK 500 6 GLU A 61 -55.46 -142.25
REMARK 500 6 GLU A 65 -51.21 -128.25
REMARK 500 7 ASP A 38 -54.46 -143.95
REMARK 500 7 GLU A 61 -50.45 -123.70
REMARK 500 7 GLU A 63 177.10 59.48
REMARK 500 7 GLU A 65 -75.38 -145.20
REMARK 500 8 ASP A 38 -51.12 -145.46
REMARK 500 8 GLU A 63 -165.97 57.76
REMARK 500 9 GLU A 61 -57.63 -157.43
REMARK 500 9 GLU A 65 -50.30 -150.85
REMARK 500 10 ASP A 2 41.64 -143.94
REMARK 500 10 ASP A 29 86.20 -69.09
REMARK 500 10 ASN A 36 54.88 -163.89
REMARK 500 10 MET A 37 49.84 -162.18
REMARK 500 10 ARG A 60 147.34 58.46
REMARK 500 11 ASP A 2 84.84 56.95
REMARK 500 11 HIS A 3 -178.42 -68.37
REMARK 500 11 MET A 37 91.44 59.37
REMARK 500 11 ARG A 60 71.57 43.79
REMARK 500 11 LEU A 62 151.02 66.04
REMARK 500 11 GLU A 65 98.86 63.69
REMARK 500 12 HIS A 3 150.95 70.07
REMARK 500 12 ASP A 38 -52.36 -150.33
REMARK 500 12 LEU A 62 -69.12 68.62
REMARK 500 13 ASP A 29 86.13 -68.57
REMARK 500 13 ASP A 38 -42.62 -140.60
REMARK 500 13 ARG A 60 89.27 -68.55
REMARK 500 13 GLU A 61 -50.48 -171.79
REMARK 500
REMARK 500 THIS ENTRY HAS 59 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 16 0.32 SIDE CHAIN
REMARK 500 1 ARG A 20 0.32 SIDE CHAIN
REMARK 500 1 ARG A 26 0.32 SIDE CHAIN
REMARK 500 1 ARG A 42 0.32 SIDE CHAIN
REMARK 500 1 ARG A 48 0.17 SIDE CHAIN
REMARK 500 1 ARG A 60 0.32 SIDE CHAIN
REMARK 500 2 ARG A 16 0.32 SIDE CHAIN
REMARK 500 2 ARG A 20 0.24 SIDE CHAIN
REMARK 500 2 ARG A 26 0.32 SIDE CHAIN
REMARK 500 2 ARG A 42 0.32 SIDE CHAIN
REMARK 500 2 ARG A 48 0.32 SIDE CHAIN
REMARK 500 2 ARG A 60 0.30 SIDE CHAIN
REMARK 500 3 ARG A 16 0.32 SIDE CHAIN
REMARK 500 3 ARG A 20 0.32 SIDE CHAIN
REMARK 500 3 ARG A 26 0.32 SIDE CHAIN
REMARK 500 3 ARG A 42 0.32 SIDE CHAIN
REMARK 500 3 ARG A 48 0.32 SIDE CHAIN
REMARK 500 3 ARG A 60 0.32 SIDE CHAIN
REMARK 500 4 ARG A 16 0.32 SIDE CHAIN
REMARK 500 4 ARG A 20 0.31 SIDE CHAIN
REMARK 500 4 ARG A 26 0.31 SIDE CHAIN
REMARK 500 4 ARG A 42 0.31 SIDE CHAIN
REMARK 500 4 ARG A 48 0.32 SIDE CHAIN
REMARK 500 4 ARG A 60 0.32 SIDE CHAIN
REMARK 500 5 ARG A 16 0.32 SIDE CHAIN
REMARK 500 5 ARG A 20 0.32 SIDE CHAIN
REMARK 500 5 ARG A 26 0.30 SIDE CHAIN
REMARK 500 5 ARG A 42 0.32 SIDE CHAIN
REMARK 500 5 ARG A 48 0.30 SIDE CHAIN
REMARK 500 5 ARG A 60 0.32 SIDE CHAIN
REMARK 500 6 ARG A 16 0.32 SIDE CHAIN
REMARK 500 6 ARG A 20 0.31 SIDE CHAIN
REMARK 500 6 ARG A 26 0.32 SIDE CHAIN
REMARK 500 6 ARG A 42 0.32 SIDE CHAIN
REMARK 500 6 ARG A 48 0.30 SIDE CHAIN
REMARK 500 6 ARG A 60 0.32 SIDE CHAIN
REMARK 500 7 ARG A 16 0.32 SIDE CHAIN
REMARK 500 7 ARG A 20 0.32 SIDE CHAIN
REMARK 500 7 ARG A 26 0.32 SIDE CHAIN
REMARK 500 7 ARG A 42 0.32 SIDE CHAIN
REMARK 500 7 ARG A 48 0.24 SIDE CHAIN
REMARK 500 7 ARG A 60 0.32 SIDE CHAIN
REMARK 500 8 ARG A 16 0.32 SIDE CHAIN
REMARK 500 8 ARG A 20 0.32 SIDE CHAIN
REMARK 500 8 ARG A 26 0.31 SIDE CHAIN
REMARK 500 8 ARG A 42 0.30 SIDE CHAIN
REMARK 500 8 ARG A 48 0.20 SIDE CHAIN
REMARK 500 8 ARG A 60 0.31 SIDE CHAIN
REMARK 500 9 ARG A 16 0.32 SIDE CHAIN
REMARK 500 9 ARG A 20 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 90 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GLGS_ECOLI RELATED DB: TARGETDB
DBREF 1RRZ A 1 66 UNP P26649 GLGS_ECOLI 1 66
SEQADV 1RRZ MET A -19 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ GLY A -18 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ SER A -17 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ SER A -16 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A -15 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A -14 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A -13 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A -12 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A -11 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A -10 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ SER A -9 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ SER A -8 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ GLY A -7 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ LEU A -6 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ VAL A -5 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ PRO A -4 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ ARG A -3 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ GLY A -2 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ SER A -1 UNP P26649 EXPRESSION TAG
SEQADV 1RRZ HIS A 0 UNP P26649 EXPRESSION TAG
SEQRES 1 A 86 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 86 LEU VAL PRO ARG GLY SER HIS MET ASP HIS SER LEU ASN
SEQRES 3 A 86 SER LEU ASN ASN PHE ASP PHE LEU ALA ARG SER PHE ALA
SEQRES 4 A 86 ARG MET HIS ALA GLU GLY ARG PRO VAL ASP ILE LEU ALA
SEQRES 5 A 86 VAL THR GLY ASN MET ASP GLU GLU HIS ARG THR TRP PHE
SEQRES 6 A 86 CYS ALA ARG TYR ALA TRP TYR CYS GLN GLN MET MET GLN
SEQRES 7 A 86 ALA ARG GLU LEU GLU LEU GLU HIS
HELIX 1 1 ASN A 6 GLY A 25 1 20
HELIX 2 2 ASP A 29 MET A 37 1 9
HELIX 3 3 GLU A 40 ARG A 60 1 21
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