HEADER PERIPLASMIC BINDING PROTEIN 18-SEP-14 2MV0
TITLE SOLUTION NMR STRUCTURE OF MALTOSE-BINDING PROTEIN FROM ESCHERICHIA
TITLE 2 COLI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET ER690
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MBP, MMBP, MALTODEXTRIN-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B4034, JW3994, MALE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET21_NESG
KEYWDS STRUCTURAL GENOMICS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,
KEYWDS 2 PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE, PERIPLASMIC BINDING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.ROSSI,O.F.LANGE,N.G.SGOURAKIS,Y.SONG,H.LEE,J.M.ARAMINI,A.ERTEKIN,
AUTHOR 2 R.XIAO,T.B.ACTON,D.BAKER,G.T.MONTELIONE,NORTHEAST STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (NESG)
REVDAT 3 14-JUN-23 2MV0 1 REMARK
REVDAT 2 01-JUL-15 2MV0 1 JRNL
REVDAT 1 10-DEC-14 2MV0 0
JRNL AUTH O.F.LANGE,P.ROSSI,N.G.SGOURAKIS,Y.SONG,H.W.LEE,J.M.ARAMINI,
JRNL AUTH 2 A.ERTEKIN,R.XIAO,T.B.ACTON,G.T.MONTELIONE,D.BAKER
JRNL TITL DETERMINATION OF SOLUTION STRUCTURES OF PROTEINS UP TO 40
JRNL TITL 2 KDA USING CS-ROSETTA WITH SPARSE NMR DATA FROM DEUTERATED
JRNL TITL 3 SAMPLES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 10873 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22733734
JRNL DOI 10.1073/PNAS.1203013109
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS, CYANA 3.0, AUTOSTRUCTURE 2.1, ROSETTA
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3 (CNS), GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 HUANG, TEJERO, POWERS AND MONTELIONE
REMARK 3 (AUTOSTRUCTURE), BAKER (ROSETTA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MV0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000104078.
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 : 1.05 MM ER690.005, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCO; 3D CBCA(CO)NH; 3D
REMARK 210 HNCACB; 3D 1H-13C NOESY; 3D 1H-
REMARK 210 15N NOESY; 3D HCCH-TOCSY; 3D (H)
REMARK 210 NNH HSQC-NOESY-HSQC; 3D (H)CCH
REMARK 210 HSQC-NOESY-HSQC; 3D (H)CNH HSQC-
REMARK 210 NOESY-HSQC; 3D (H)NCH HSQC-NOESY-
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS, CYANA 3.0, AUTOSTRUCTURE
REMARK 210 2.1, AUTOASSIGN 2.1, NMRPIPE,
REMARK 210 XEASY, TOPSPIN, VNMRJ, PINE,
REMARK 210 SPARKY, TALOS+, PALES, REDCAT,
REMARK 210 PSVS
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 1
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 TRP A 230 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 230 CZ3 CH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 10 PRO A 159 CD PRO A 159 N 0.110
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 15 -135.95 -125.01
REMARK 500 1 ASP A 55 -165.35 -120.02
REMARK 500 1 SER A 255 -72.74 -139.34
REMARK 500 1 TYR A 283 -64.74 -123.71
REMARK 500 2 ASP A 55 -165.43 -129.59
REMARK 500 2 SER A 255 -84.98 -125.01
REMARK 500 3 LYS A 42 70.99 55.18
REMARK 500 3 ALA A 146 -72.86 -65.10
REMARK 500 3 ASN A 173 -69.18 74.12
REMARK 500 3 TYR A 176 77.22 -110.46
REMARK 500 3 ASP A 209 -164.98 -119.97
REMARK 500 3 ILE A 235 -61.33 -90.77
REMARK 500 3 SER A 255 -94.93 -114.97
REMARK 500 3 ASN A 272 59.92 -118.00
REMARK 500 3 TYR A 283 -62.97 -125.00
REMARK 500 4 LEU A 115 108.42 -53.06
REMARK 500 4 LYS A 189 -64.40 -95.04
REMARK 500 4 THR A 208 108.54 -54.59
REMARK 500 4 SER A 255 -74.93 -139.54
REMARK 500 4 TYR A 283 -70.66 -125.07
REMARK 500 5 ASP A 55 -166.02 -119.99
REMARK 500 5 LEU A 113 118.47 -161.55
REMARK 500 5 ASN A 150 77.29 -117.69
REMARK 500 5 ASN A 173 -119.95 58.85
REMARK 500 5 SER A 255 -75.01 -137.60
REMARK 500 5 LEU A 285 51.10 -115.85
REMARK 500 6 TYR A 17 25.24 -158.98
REMARK 500 6 ASN A 173 -65.07 80.30
REMARK 500 6 THR A 208 109.39 -53.88
REMARK 500 6 SER A 255 -75.02 -154.94
REMARK 500 6 TYR A 283 -64.94 -124.94
REMARK 500 6 ASN A 332 50.01 -105.83
REMARK 500 7 ASP A 55 -168.42 -113.23
REMARK 500 7 TYR A 99 119.61 -160.42
REMARK 500 7 ILE A 108 -21.59 -165.06
REMARK 500 7 TYR A 171 107.95 -54.93
REMARK 500 7 ASP A 209 -166.82 -129.97
REMARK 500 7 TRP A 230 -35.09 175.04
REMARK 500 7 LEU A 247 51.58 -140.96
REMARK 500 7 SER A 255 -87.37 -125.19
REMARK 500 7 ASN A 272 60.04 -110.55
REMARK 500 8 LYS A 15 40.01 -151.41
REMARK 500 8 ILE A 108 14.96 163.94
REMARK 500 8 ALA A 109 144.78 -171.22
REMARK 500 8 ASN A 173 -67.40 73.26
REMARK 500 8 SER A 255 -99.97 -105.10
REMARK 500 8 TYR A 283 -50.09 -120.00
REMARK 500 9 ASP A 209 -166.76 -123.06
REMARK 500 9 TRP A 230 -22.49 -175.02
REMARK 500 9 SER A 255 -75.27 -139.99
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25237 RELATED DB: BMRB
REMARK 900 RELATED ID: NESG-ER690 RELATED DB: TARGETTRACK
DBREF 2MV0 A 1 370 UNP P0AEX9 MALE_ECOLI 27 396
SEQRES 1 A 370 LYS ILE 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 GLY A 32 1 17
HELIX 2 2 LYS A 42 ALA A 52 1 11
HELIX 3 3 ARG A 66 SER A 73 1 8
HELIX 4 4 ASP A 82 LEU A 89 1 8
HELIX 5 5 TYR A 90 ASP A 95 1 6
HELIX 6 6 THR A 128 GLU A 130 5 3
HELIX 7 7 GLU A 131 ALA A 141 1 11
HELIX 8 8 GLU A 153 PHE A 156 5 4
HELIX 9 9 THR A 157 ASP A 164 1 8
HELIX 10 10 ASN A 185 ASN A 201 1 17
HELIX 11 11 ASP A 209 GLY A 220 1 12
HELIX 12 12 ALA A 231 ASP A 236 1 6
HELIX 13 13 THR A 237 LYS A 239 5 3
HELIX 14 14 ASN A 272 TYR A 283 1 12
HELIX 15 15 THR A 286 ASN A 294 1 9
HELIX 16 16 LEU A 304 ALA A 312 1 9
HELIX 17 17 ASP A 314 GLN A 325 1 12
HELIX 18 18 ILE A 333 SER A 352 1 20
HELIX 19 19 THR A 356 LYS A 370 1 15
SHEET 1 A 5 LYS A 34 GLU A 38 0
SHEET 2 A 5 LYS A 6 TRP A 10 1 N ILE A 9 O THR A 36
SHEET 3 A 5 ILE A 59 TRP A 62 1 O ILE A 59 N TRP A 10
SHEET 4 A 5 VAL A 259 ILE A 266 -1 O SER A 263 N TRP A 62
SHEET 5 A 5 TYR A 106 ALA A 112 -1 N GLU A 111 O GLY A 260
SHEET 1 B 5 LYS A 34 GLU A 38 0
SHEET 2 B 5 LYS A 6 TRP A 10 1 N ILE A 9 O THR A 36
SHEET 3 B 5 ILE A 59 TRP A 62 1 O ILE A 59 N TRP A 10
SHEET 4 B 5 VAL A 259 ILE A 266 -1 O SER A 263 N TRP A 62
SHEET 5 B 5 ILE A 329 MET A 330 1 O MET A 330 N VAL A 259
SHEET 1 C 2 ARG A 98 TYR A 99 0
SHEET 2 C 2 LYS A 102 LEU A 103 -1 O LYS A 102 N TYR A 99
SHEET 1 D 2 LEU A 115 ASN A 118 0
SHEET 2 D 2 TYR A 242 THR A 245 -1 O THR A 245 N LEU A 115
CISPEP 1 PRO A 123 ASN A 124 5 -12.55
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
(ATOM LINES ARE NOT SHOWN.)
END
