HEADER HYDROLASE 19-JAN-09 2KDV
TITLE SOLUTION STRUCTURE OF RNA PYROPHOSPHOHYDROLASE RPPH FROM ESCHERICHIA
TITLE 2 COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA PYROPHOSPHOHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-164;
COMPND 5 SYNONYM: RPPH, (DI)NUCLEOSIDE POLYPHOSPHATE HYDROLASE, AP5A
COMPND 6 PYROPHOSPHATASE;
COMPND 7 EC: 3.6.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: RPPH, NUDH, YGDP, B2830, JW2798;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET21
KEYWDS NUDIX FAMILY, HYDROLASE, MAGNESIUM, MANGANESE, ZINC
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR Y.BI,H.LI,C.JIN
REVDAT 2 16-MAR-22 2KDV 1 REMARK
REVDAT 1 26-JAN-10 2KDV 0
JRNL AUTH Y.BI,H.LI,C.JIN
JRNL TITL SOLUTION STRUCTURE OF RNA PYROPHOSPHOHYDROLASE RPPH FROM
JRNL TITL 2 ESCHERICHIA COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, AMBER
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), CASE, DARDEN, CHEATHAM, III, SIMMERLING,
REMARK 3 WANG, DUKE, LUO, ... AND KOLLM (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000100998.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 90
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50MM SODIUM ACETATE-1, 20MM
REMARK 210 SODIUM CHLORIDE-2, 40MM DTT-3,
REMARK 210 10MM ARGININE-4, 10MM GLUTAMIC-5,
REMARK 210 0.8MM [U-13C; U-15N] RPPH
REMARK 210 PROTEIN-6, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D 1H-15N NOESY;
REMARK 210 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, XWINNMR, CYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
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 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 HE1 TRP A 24 HB3 TRP A 33 1.34
REMARK 500
REMARK 500 REMARK: NULL
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 1 PRO A 163 CD PRO A 163 N -0.099
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 MET A 1 CA - CB - CG ANGL. DEV. = 11.0 DEGREES
REMARK 500 1 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 ARG A 8 CD - NE - CZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 1 ARG A 18 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 1 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 1 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 TRP A 24 CB - CG - CD2 ANGL. DEV. = 11.5 DEGREES
REMARK 500 1 TRP A 24 CD1 - CG - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 1 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 1 TRP A 24 NE1 - CE2 - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 1 TRP A 24 CE2 - CD2 - CE3 ANGL. DEV. = -12.2 DEGREES
REMARK 500 1 TRP A 24 CE2 - CD2 - CG ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 TRP A 24 CZ3 - CH2 - CZ2 ANGL. DEV. = -17.9 DEGREES
REMARK 500 1 TRP A 24 CH2 - CZ2 - CE2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 1 ARG A 26 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 TRP A 33 CA - CB - CG ANGL. DEV. = 22.1 DEGREES
REMARK 500 1 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 1 VAL A 58 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 1 VAL A 58 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 1 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 1 ARG A 66 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 ARG A 76 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 TYR A 77 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 TYR A 129 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 TYR A 131 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 PRO A 132 CA - CB - CG ANGL. DEV. = 11.6 DEGREES
REMARK 500 1 ARG A 134 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 ARG A 141 CD - NE - CZ ANGL. DEV. = -8.9 DEGREES
REMARK 500 1 ARG A 141 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 1 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 PHE A 151 CD1 - CG - CD2 ANGL. DEV. = -13.8 DEGREES
REMARK 500 1 PHE A 151 CG - CD1 - CE1 ANGL. DEV. = -9.0 DEGREES
REMARK 500 1 THR A 162 CA - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 1 PRO A 163 N - CA - CB ANGL. DEV. = 7.7 DEGREES
REMARK 500 1 PRO A 163 CA - C - N ANGL. DEV. = -16.9 DEGREES
REMARK 500 2 PRO A 163 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 3 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 5 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 12 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 17 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 19 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 21 ARG A 26 NE - CZ - NH2 ANGL. DEV. = -3.2 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 1 ASP A 4 -53.00 -164.16
REMARK 500 1 ARG A 85 75.44 -103.15
REMARK 500 1 THR A 162 62.09 26.03
REMARK 500 2 ASP A 3 -72.87 -72.18
REMARK 500 2 ASP A 4 -49.96 -162.25
REMARK 500 2 GLN A 114 33.02 -147.66
REMARK 500 2 THR A 162 26.65 48.63
REMARK 500 2 PRO A 163 49.84 12.95
REMARK 500 3 ASP A 4 -50.47 -163.90
REMARK 500 3 GLU A 57 -60.85 -94.39
REMARK 500 3 GLU A 110 50.96 -90.49
REMARK 500 4 ILE A 2 129.20 64.81
REMARK 500 4 ASP A 4 -51.28 -163.43
REMARK 500 4 GLN A 114 75.29 -117.69
REMARK 500 5 ILE A 2 135.15 67.50
REMARK 500 5 ASP A 4 -49.43 -164.14
REMARK 500 5 ASN A 112 -52.73 -120.34
REMARK 500 5 GLN A 114 78.46 -153.79
REMARK 500 5 PRO A 163 -178.49 -67.41
REMARK 500 6 ASP A 4 -50.47 -164.00
REMARK 500 6 THR A 162 59.31 -143.90
REMARK 500 7 ASP A 4 -49.54 -164.09
REMARK 500 7 HIS A 31 -23.38 65.06
REMARK 500 7 GLN A 114 71.84 -119.19
REMARK 500 7 THR A 162 50.10 -142.22
REMARK 500 8 ASP A 4 -49.76 -164.47
REMARK 500 8 GLU A 120 32.50 -76.62
REMARK 500 8 ASP A 122 17.48 -149.75
REMARK 500 8 THR A 162 64.68 39.60
REMARK 500 9 GLN A 114 74.32 -112.73
REMARK 500 10 ASP A 4 -53.84 -162.21
REMARK 500 10 GLU A 57 -61.09 -91.04
REMARK 500 11 ASP A 4 -48.78 -164.74
REMARK 500 11 ASN A 112 -51.84 -122.23
REMARK 500 11 GLN A 114 29.84 -140.58
REMARK 500 11 THR A 162 62.59 39.35
REMARK 500 12 ASP A 4 -48.92 -164.74
REMARK 500 13 ASP A 4 -53.42 -162.85
REMARK 500 13 GLU A 110 48.08 -82.58
REMARK 500 13 GLN A 114 71.03 -151.87
REMARK 500 13 THR A 162 79.55 -160.34
REMARK 500 13 PRO A 163 22.93 -76.48
REMARK 500 14 ILE A 2 117.66 62.53
REMARK 500 14 ASP A 4 -53.31 -163.04
REMARK 500 14 HIS A 31 -21.84 64.55
REMARK 500 14 ASN A 112 -50.98 -120.60
REMARK 500 14 GLN A 114 76.96 -154.71
REMARK 500 14 PRO A 163 -178.93 -66.98
REMARK 500 15 ILE A 2 134.76 66.76
REMARK 500 15 ASP A 4 -51.68 -163.06
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
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 ASN A 161 THR A 162 1 -142.57
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 8 0.10 SIDE CHAIN
REMARK 500 1 ARG A 27 0.08 SIDE CHAIN
REMARK 500 1 ARG A 62 0.25 SIDE CHAIN
REMARK 500 1 TYR A 77 0.11 SIDE CHAIN
REMARK 500 1 TYR A 129 0.08 SIDE CHAIN
REMARK 500 1 ARG A 141 0.25 SIDE CHAIN
REMARK 500 1 PHE A 151 0.19 SIDE CHAIN
REMARK 500 2 TYR A 51 0.09 SIDE CHAIN
REMARK 500 3 ARG A 27 0.08 SIDE CHAIN
REMARK 500 4 TYR A 51 0.07 SIDE CHAIN
REMARK 500 5 ARG A 27 0.08 SIDE CHAIN
REMARK 500 6 ARG A 27 0.08 SIDE CHAIN
REMARK 500 7 TYR A 51 0.07 SIDE CHAIN
REMARK 500 9 TYR A 51 0.09 SIDE CHAIN
REMARK 500 10 TYR A 51 0.07 SIDE CHAIN
REMARK 500 11 ARG A 18 0.09 SIDE CHAIN
REMARK 500 12 ARG A 26 0.10 SIDE CHAIN
REMARK 500 12 TYR A 51 0.06 SIDE CHAIN
REMARK 500 13 ARG A 27 0.09 SIDE CHAIN
REMARK 500 13 ARG A 66 0.28 SIDE CHAIN
REMARK 500 14 ARG A 27 0.11 SIDE CHAIN
REMARK 500 14 TYR A 51 0.08 SIDE CHAIN
REMARK 500 15 TYR A 51 0.07 SIDE CHAIN
REMARK 500 17 TYR A 51 0.09 SIDE CHAIN
REMARK 500 18 ARG A 27 0.09 SIDE CHAIN
REMARK 500 18 TYR A 51 0.06 SIDE CHAIN
REMARK 500 19 TYR A 51 0.08 SIDE CHAIN
REMARK 500 19 ARG A 52 0.08 SIDE CHAIN
REMARK 500 19 TYR A 77 0.09 SIDE CHAIN
REMARK 500 19 ARG A 146 0.08 SIDE CHAIN
REMARK 500 20 TYR A 51 0.08 SIDE CHAIN
REMARK 500 20 TYR A 77 0.07 SIDE CHAIN
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 PRO A 163 12.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2KDW RELATED DB: PDB
REMARK 900 RPPH MUTANT E53A
REMARK 900 RELATED ID: 16124 RELATED DB: BMRB
DBREF 2KDV A 1 164 UNP P0A776 RPPH_ECOLI 1 164
SEQRES 1 A 164 MET ILE ASP ASP ASP GLY TYR ARG PRO ASN VAL GLY ILE
SEQRES 2 A 164 VAL ILE CYS ASN ARG GLN GLY GLN VAL MET TRP ALA ARG
SEQRES 3 A 164 ARG PHE GLY GLN HIS SER TRP GLN PHE PRO GLN GLY GLY
SEQRES 4 A 164 ILE ASN PRO GLY GLU SER ALA GLU GLN ALA MET TYR ARG
SEQRES 5 A 164 GLU LEU PHE GLU GLU VAL GLY LEU SER ARG LYS ASP VAL
SEQRES 6 A 164 ARG ILE LEU ALA SER THR ARG ASN TRP LEU ARG TYR LYS
SEQRES 7 A 164 LEU PRO LYS ARG LEU VAL ARG TRP ASP THR LYS PRO VAL
SEQRES 8 A 164 CYS ILE GLY GLN LYS GLN LYS TRP PHE LEU LEU GLN LEU
SEQRES 9 A 164 VAL SER GLY ASP ALA GLU ILE ASN MET GLN THR SER SER
SEQRES 10 A 164 THR PRO GLU PHE ASP GLY TRP ARG TRP VAL SER TYR TRP
SEQRES 11 A 164 TYR PRO VAL ARG GLN VAL VAL SER PHE LYS ARG ASP VAL
SEQRES 12 A 164 TYR ARG ARG VAL MET LYS GLU PHE ALA SER VAL VAL MET
SEQRES 13 A 164 SER LEU GLN GLU ASN THR PRO LYS
HELIX 1 1 SER A 45 GLY A 59 1 15
HELIX 2 2 SER A 61 LYS A 63 5 3
HELIX 3 3 GLY A 107 ILE A 111 5 5
HELIX 4 4 TYR A 131 VAL A 136 5 6
HELIX 5 5 VAL A 137 ASN A 161 1 25
SHEET 1 A 4 GLN A 37 GLY A 39 0
SHEET 2 A 4 TYR A 7 CYS A 16 -1 N VAL A 11 O GLY A 38
SHEET 3 A 4 GLY A 94 LEU A 104 1 O LEU A 102 N VAL A 14
SHEET 4 A 4 VAL A 65 SER A 70 -1 N LEU A 68 O LEU A 101
SHEET 1 B 4 GLN A 37 GLY A 39 0
SHEET 2 B 4 TYR A 7 CYS A 16 -1 N VAL A 11 O GLY A 38
SHEET 3 B 4 GLY A 94 LEU A 104 1 O LEU A 102 N VAL A 14
SHEET 4 B 4 LEU A 75 LYS A 78 -1 N LEU A 75 O GLN A 97
SHEET 1 C 3 TRP A 33 GLN A 34 0
SHEET 2 C 3 GLN A 21 ARG A 27 -1 N ALA A 25 O GLN A 34
SHEET 3 C 3 PHE A 121 SER A 128 -1 O VAL A 127 N VAL A 22
CISPEP 1 LYS A 89 PRO A 90 1 -16.05
CISPEP 2 LYS A 89 PRO A 90 2 -10.29
CISPEP 3 LYS A 89 PRO A 90 3 -10.15
CISPEP 4 LYS A 89 PRO A 90 4 -10.34
CISPEP 5 LYS A 89 PRO A 90 5 -10.34
CISPEP 6 LYS A 89 PRO A 90 6 -10.14
CISPEP 7 LYS A 89 PRO A 90 7 -10.36
CISPEP 8 LYS A 89 PRO A 90 8 -10.34
CISPEP 9 LYS A 89 PRO A 90 9 -10.55
CISPEP 10 LYS A 89 PRO A 90 10 -10.34
CISPEP 11 LYS A 89 PRO A 90 11 -10.36
CISPEP 12 LYS A 89 PRO A 90 12 -10.46
CISPEP 13 LYS A 89 PRO A 90 13 -9.60
CISPEP 14 LYS A 89 PRO A 90 14 -10.41
CISPEP 15 LYS A 89 PRO A 90 15 -10.25
CISPEP 16 LYS A 89 PRO A 90 16 -11.08
CISPEP 17 LYS A 89 PRO A 90 17 -10.34
CISPEP 18 LYS A 89 PRO A 90 18 -10.24
CISPEP 19 LYS A 89 PRO A 90 19 -10.50
CISPEP 20 LYS A 89 PRO A 90 20 -10.37
CISPEP 21 LYS A 89 PRO A 90 21 -10.15
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
