HEADER CHOLINE-BINDING PROTEIN 10-APR-13 2M6U
TITLE NMR STRUCTURE OF CBPAN FROM STREPTOCOCCUS PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINE BINDING PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 67-148;
COMPND 5 SYNONYM: CBPA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 GENE: SPAR136_2333;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET17BHR
KEYWDS THREE-HELIX BUNDLE, CHOLINE BINDING PROTEIN, CHOLINE-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.LIU,H.YAN,D.ACHILA,E.MARTINEZ-HACKERT,Y.LI,R.BANERJEE
REVDAT 4 14-JUN-23 2M6U 1 KEYWDS REMARK SEQADV
REVDAT 3 21-JAN-15 2M6U 1 JRNL
REVDAT 2 05-NOV-14 2M6U 1 JRNL
REVDAT 1 16-APR-14 2M6U 0
JRNL AUTH D.ACHILA,A.LIU,R.BANERJEE,Y.LI,E.MARTINEZ-HACKERT,J.R.ZHANG,
JRNL AUTH 2 H.YAN
JRNL TITL STRUCTURAL DETERMINANTS OF HOST SPECIFICITY OF COMPLEMENT
JRNL TITL 2 FACTOR H RECRUITMENT BY STREPTOCOCCUS PNEUMONIAE.
JRNL REF BIOCHEM.J. V. 465 325 2015
JRNL REFN ISSN 0264-6021
JRNL PMID 25330773
JRNL DOI 10.1042/BJ20141069
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, CYANA, AMBER
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 GUNTERT, MUMENTHALER AND WUTHRICH (CYANA), CASE,
REMARK 3 DARDEN, CHEATHAM, III, SIMMERLING, WANG, DUKE, LUO,
REMARK 3 ... AND KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2M6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000103282.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50 UM DSS, 100 UM SODIUM AZIDE,
REMARK 210 50 MM SODIUM PHOSPHATE, 50 MM
REMARK 210 SODIUM CHLORIDE, 95% H2O/5% D2O;
REMARK 210 50 UM DSS, 100 UM SODIUM AZIDE,
REMARK 210 50 MM SODIUM PHOSPHATE, 50 MM
REMARK 210 SODIUM CHLORIDE, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCA; 3D
REMARK 210 HN(CO)CA; 3D HNCACB; 3D CBCA(CO)
REMARK 210 NH; 3D HNCO; 3D HN(CA)CO; 3D 1H-
REMARK 210 15N NOESY; 2D 1H-13C HSQC; 3D
REMARK 210 HCCH-TOCSY; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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: 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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 HIS A -1
REMARK 465 MET 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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 7 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 8 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 10 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 11 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 13 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 13 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 14 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 14 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 15 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 16 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 16 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 17 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 17 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 18 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 18 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 18 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 19 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 19 ARG A 9 CD - NE - CZ ANGL. DEV. = 9.8 DEGREES
REMARK 500 19 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 20 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
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 5 SER A 27 -157.12 -143.61
REMARK 500 7 THR A 57 30.53 -81.74
REMARK 500 11 SER A 27 -159.08 -88.97
REMARK 500 11 THR A 57 -38.89 -142.73
REMARK 500 11 GLU A 59 31.73 -71.72
REMARK 500 11 SER A 60 -56.94 -127.32
REMARK 500 14 ASP A 2 -62.51 -98.35
REMARK 500 14 LYS A 30 4.11 -68.00
REMARK 500 16 ARG A 31 36.73 -74.97
REMARK 500 18 ASP A 2 -61.13 -19.82
REMARK 500 20 THR A 57 -21.61 48.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 1 ASP A 2 18 149.39
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 TYR A 49 0.07 SIDE CHAIN
REMARK 500 3 ARG A 5 0.09 SIDE CHAIN
REMARK 500 3 TYR A 49 0.08 SIDE CHAIN
REMARK 500 4 ARG A 70 0.09 SIDE CHAIN
REMARK 500 7 ARG A 9 0.09 SIDE CHAIN
REMARK 500 9 ARG A 5 0.09 SIDE CHAIN
REMARK 500 9 TYR A 49 0.07 SIDE CHAIN
REMARK 500 11 TYR A 49 0.07 SIDE CHAIN
REMARK 500 13 ARG A 31 0.08 SIDE CHAIN
REMARK 500 13 TYR A 49 0.07 SIDE CHAIN
REMARK 500 20 ARG A 5 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19155 RELATED DB: BMRB
REMARK 900 RELATED ID: 4K12 RELATED DB: PDB
DBREF 2M6U A 1 82 UNP G6W2B2 G6W2B2_STREE 67 148
SEQADV 2M6U GLY A -2 UNP G6W2B2 EXPRESSION TAG
SEQADV 2M6U HIS A -1 UNP G6W2B2 EXPRESSION TAG
SEQADV 2M6U MET A 0 UNP G6W2B2 EXPRESSION TAG
SEQRES 1 A 85 GLY HIS MET LEU ASP SER GLU ARG ASP LYS ALA ARG LYS
SEQRES 2 A 85 GLU VAL GLU GLU TYR VAL LYS LYS ILE VAL GLY GLU SER
SEQRES 3 A 85 TYR ALA LYS SER THR LYS LYS ARG HIS THR ILE THR VAL
SEQRES 4 A 85 ALA LEU VAL ASN GLU LEU ASN ASN ILE LYS ASN GLU TYR
SEQRES 5 A 85 LEU ASN LYS ILE VAL GLU SER THR SER GLU SER GLN LEU
SEQRES 6 A 85 GLN ILE LEU MET MET GLU SER ARG SER LYS VAL ASP GLU
SEQRES 7 A 85 ALA VAL SER LYS PHE GLU LYS
HELIX 1 1 LEU A 1 SER A 27 1 27
HELIX 2 2 ARG A 31 GLU A 55 1 25
HELIX 3 3 SER A 58 GLU A 81 1 24
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
