Header list of 1ezo.pdb file
Complete list - v 3 2 Bytes
HEADER SUGAR BINDING PROTEIN 11-MAY-00 1EZO
TITLE GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH BETA-
TITLE 2 CYCLODEXTRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MALTODEXTRIN BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBR322
KEYWDS MALTODEXTRIN BINDING PROTEIN, MBP, DEUTERATION, METHYL LABELING,
KEYWDS 2 SUGAR BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.A.MUELLER,W.Y.CHOY,D.YANG,J.D.FORMAN-KAY,R.A.VENTERS,L.E.KAY
REVDAT 4 03-NOV-21 1EZO 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1EZO 1 VERSN
REVDAT 2 01-APR-03 1EZO 1 JRNL
REVDAT 1 03-MAY-01 1EZO 0
JRNL AUTH G.A.MUELLER,W.Y.CHOY,D.YANG,J.D.FORMAN-KAY,R.A.VENTERS,
JRNL AUTH 2 L.E.KAY
JRNL TITL GLOBAL FOLDS OF PROTEINS WITH LOW DENSITIES OF NOES USING
JRNL TITL 2 RESIDUAL DIPOLAR COUPLINGS: APPLICATION TO THE 370-RESIDUE
JRNL TITL 3 MALTODEXTRIN-BINDING PROTEIN.
JRNL REF J.MOL.BIOL. V. 300 197 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10864509
JRNL DOI 10.1006/JMBI.2000.3842
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EZO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011064.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4 MM MALTODEXTRIN BINDING
REMARK 210 PROTEIN U-15N,13C,2H, WITH 1H
REMARK 210 AMIDE AND METHYL ON VAL, LEU,
REMARK 210 AND ILE(DELTA1) 2MM BETA-
REMARK 210 CYCLODEXTRIN, 20 MM SODIUM
REMARK 210 PHOSPHATE PH 7.2, 3UM NAN3,
REMARK 210 100UM EDTA.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_NOESY;
REMARK 210 4D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; (HM)CMCB(CMHM)-
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 3.0, CNS 0.5
REMARK 210 METHOD USED : SIMULATED ANNEALING FROM
REMARK 210 EXTENDED COORDINATES, TORSION
REMARK 210 ANGLE DYNAMICS, AND FINISH WITH
REMARK 210 CARTESIAN DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 384
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 GLU A 4 -75.30 64.97
REMARK 500 1 ASN A 12 112.67 -163.75
REMARK 500 1 ASP A 14 -48.73 -176.92
REMARK 500 1 THR A 31 37.11 157.61
REMARK 500 1 ASP A 41 -47.03 -151.46
REMARK 500 1 THR A 53 -74.11 -169.66
REMARK 500 1 ASP A 55 -71.83 -136.18
REMARK 500 1 PRO A 57 -177.74 -64.27
REMARK 500 1 ASP A 58 106.43 167.09
REMARK 500 1 ALA A 63 -168.61 -57.26
REMARK 500 1 LEU A 75 83.51 -176.77
REMARK 500 1 ALA A 77 83.28 -62.49
REMARK 500 1 GLU A 78 96.65 -65.11
REMARK 500 1 ASP A 82 -55.20 -130.12
REMARK 500 1 LEU A 89 -170.08 -66.69
REMARK 500 1 ASN A 100 -68.82 68.40
REMARK 500 1 ALA A 105 124.76 -171.51
REMARK 500 1 ALA A 109 95.20 176.02
REMARK 500 1 ASP A 120 -65.71 -131.11
REMARK 500 1 LYS A 127 -76.42 -174.43
REMARK 500 1 LEU A 147 115.45 179.14
REMARK 500 1 LEU A 151 -46.82 -135.04
REMARK 500 1 GLN A 152 40.06 -97.62
REMARK 500 1 PHE A 156 -56.35 -121.08
REMARK 500 1 TYR A 167 -66.22 -176.18
REMARK 500 1 LYS A 202 -75.73 -120.15
REMARK 500 1 ASN A 205 -43.84 -136.50
REMARK 500 1 ALA A 206 73.31 67.52
REMARK 500 1 GLU A 221 101.65 171.78
REMARK 500 1 ALA A 223 39.56 -79.88
REMARK 500 1 MET A 224 99.68 -162.47
REMARK 500 1 PRO A 229 76.83 -69.34
REMARK 500 1 TRP A 230 -52.15 -156.25
REMARK 500 1 ALA A 231 79.49 -156.54
REMARK 500 1 ASN A 234 40.07 -154.47
REMARK 500 1 ILE A 235 -67.33 69.11
REMARK 500 1 VAL A 240 -67.57 68.79
REMARK 500 1 SER A 255 -172.82 -56.14
REMARK 500 1 PRO A 257 -168.30 -79.69
REMARK 500 1 ASN A 272 86.67 59.10
REMARK 500 1 TYR A 283 48.20 -177.31
REMARK 500 1 LEU A 284 -55.84 -178.25
REMARK 500 1 LEU A 285 65.12 -107.44
REMARK 500 1 LEU A 299 -40.37 -175.72
REMARK 500 1 GLU A 328 89.34 -173.31
REMARK 500 1 PRO A 331 -168.23 -72.42
REMARK 500 1 ASN A 332 -65.07 -98.45
REMARK 500 1 ILE A 333 90.32 34.90
REMARK 500 2 ASN A 12 -169.88 -176.53
REMARK 500 2 ASP A 14 -51.42 -150.31
REMARK 500
REMARK 500 THIS ENTRY HAS 519 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EZP RELATED DB: PDB
REMARK 900 1EZP CONTAINS THE NMR ENSEMBLE CALCULATED WITH THE DIPOLAR COUPLING
REMARK 900 RESTRAINTS DEVELOPED AS DESCRIBED IN THE CITATION.
DBREF 1EZO A 1 370 UNP P02928 MALE_ECOLI 27 396
SEQADV 1EZO THR A 2 UNP P02928 ILE 28 ENGINEERED MUTATION
SEQRES 1 A 370 LYS THR GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY
SEQRES 2 A 370 ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS
SEQRES 3 A 370 PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS
SEQRES 4 A 370 PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA
SEQRES 5 A 370 THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP
SEQRES 6 A 370 ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU
SEQRES 7 A 370 ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR PRO
SEQRES 8 A 370 PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE
SEQRES 9 A 370 ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR
SEQRES 10 A 370 ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU
SEQRES 11 A 370 GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY
SEQRES 12 A 370 LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE
SEQRES 13 A 370 THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE
SEQRES 14 A 370 LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL GLY
SEQRES 15 A 370 VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE LEU
SEQRES 16 A 370 VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP THR
SEQRES 17 A 370 ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY GLU
SEQRES 18 A 370 THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER ASN
SEQRES 19 A 370 ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL LEU
SEQRES 20 A 370 PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL GLY
SEQRES 21 A 370 VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN LYS
SEQRES 22 A 370 GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU THR
SEQRES 23 A 370 ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO LEU
SEQRES 24 A 370 GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU ALA
SEQRES 25 A 370 LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA GLN
SEQRES 26 A 370 LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER ALA
SEQRES 27 A 370 PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA ALA
SEQRES 28 A 370 SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS ASP ALA
SEQRES 29 A 370 GLN THR ARG ILE THR LYS
HELIX 1 1 GLY A 16 LYS A 29 1 14
HELIX 2 2 LYS A 42 ALA A 51 1 10
HELIX 3 3 ALA A 63 GLN A 72 1 10
HELIX 4 4 ASP A 82 LYS A 88 1 7
HELIX 5 5 TYR A 90 ALA A 96 1 7
HELIX 6 6 GLU A 131 ALA A 141 1 11
HELIX 7 7 PHE A 156 ALA A 163 1 8
HELIX 8 8 ASN A 185 ASN A 201 1 17
HELIX 9 9 ASP A 209 LYS A 219 1 11
HELIX 10 10 ASN A 272 ASN A 282 1 11
HELIX 11 11 THR A 286 LYS A 297 1 12
HELIX 12 12 TYR A 307 ALA A 312 1 6
HELIX 13 13 ASP A 314 GLY A 327 1 14
HELIX 14 14 GLN A 335 GLY A 353 1 19
HELIX 15 15 THR A 356 LYS A 370 1 15
SHEET 1 A 3 LYS A 34 GLU A 38 0
SHEET 2 A 3 LYS A 6 TRP A 10 1 O LEU A 7 N THR A 36
SHEET 3 A 3 ILE A 59 ILE A 60 1 O ILE A 59 N TRP A 10
SHEET 1 B 2 PRO A 107 VAL A 110 0
SHEET 2 B 2 VAL A 261 SER A 263 -1 O LEU A 262 N ILE A 108
SHEET 1 C 2 LEU A 115 TYR A 117 0
SHEET 2 C 2 GLY A 243 THR A 245 -1 N GLY A 243 O TYR A 117
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 - v 3 2 Bytes