Header list of 1gyz.pdb file
Complete list - r 25 2 Bytes
HEADER RIBOSOMAL PROTEIN 02-MAY-02 1GYZ
TITLE BACTERIAL RIBOSOMAL PROTEIN L20 FROM AQUIFEX AEOLICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L20;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 59-118;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 224324;
SOURCE 4 STRAIN: VF5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PUBS520;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS RIBOSOMAL PROTEIN, RIBOSOME, PROTEIN SYNTHESIS,
KEYWDS 2 TRANSLATIONAL CONTROL, RRNA-BINDING, COMPLETE PROTEOME
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.RAIBAUD,I.LEBARS,F.BONTEMS,F.DARDEL
REVDAT 3 24-FEB-09 1GYZ 1 VERSN
REVDAT 2 10-OCT-02 1GYZ 1 JRNL REMARK
REVDAT 1 10-MAY-02 1GYZ 0
JRNL AUTH S.RAIBAUD,I.LEBARS,M.GUILLIER,C.CHIARUTTINI,
JRNL AUTH 2 F.BONTEMS,A.RAK,M.GARBER,F.ALLEMAND,M.SPRINGER,
JRNL AUTH 3 F.DARDEL
JRNL TITL NMR STRUCTURE OF BACTERIAL RIBOSOMAL PROTEIN L20:
JRNL TITL 2 IMPLICATIONS FOR RIBOSOME ASSEMBLY AND
JRNL TITL 3 TRANSLATIONAL CONTROL
JRNL REF J.MOL.BIOL. V. 323 143 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12368106
JRNL DOI 10.1016/S0022-2836(02)00921-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.89
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED SIMUATED ANNEALING
REMARK 3 FOLLOWED BY A FINAL MINIMIZATION USING THE CHARMM22 FORCEFIELD
REMARK 4
REMARK 4 1GYZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAY-02.
REMARK 100 THE PDBE ID CODE IS EBI-9812.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.5
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA,NOESY-HMQC,
REMARK 210 TOCSY-HMQC,
REMARK 210 HCCH-TOCSY,
REMARK 210 NOESY,
REMARK 210 DQF-COSY,
REMARK 210 HNHA,
REMARK 210 HNHB
REMARK 210
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA,XPLOR
REMARK 210 METHOD USED : HYBRID : DIANA FOLLOWED
REMARK 210 BY RESTRAINED SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST DIANA TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED L20. THE FIRST 58
REMARK 210 RESIDUES ARE PRESENT IN THE SAMPLE BUT ARE DISORDERED IN
REMARK 210 SOLUTION
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HD11 LEU A 72 - HG1 THR A 76 1.54
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 TYR A 74 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 TYR A 74 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 3 TYR A 74 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 3 TYR A 74 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 LEU A 93 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 5 PHE A 77 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 9 TRP A 59 CA - CB - CG ANGL. DEV. = 20.2 DEGREES
REMARK 500 9 LYS A 91 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 9 LEU A 93 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 10 ALA A 94 CB - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 13 TRP A 59 CA - CB - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500 13 TRP A 59 CB - CG - CD2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 13 ALA A 94 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 15 TYR A 74 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 15 TYR A 74 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 16 ALA A 94 CB - CA - C ANGL. DEV. = -10.5 DEGREES
REMARK 500 17 LEU A 93 CB - CA - C ANGL. DEV. = -11.6 DEGREES
REMARK 500 19 LEU A 81 CB - CA - C ANGL. DEV. = -11.7 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 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 ILE A 60 -61.03 -147.50
REMARK 500 1 TYR A 74 -24.22 84.80
REMARK 500 1 LEU A 88 -166.98 -127.94
REMARK 500 1 LYS A 91 126.35 136.23
REMARK 500 1 ILE A 92 22.12 82.30
REMARK 500 1 LEU A 115 -72.11 -100.30
REMARK 500 2 ILE A 60 -60.91 -154.49
REMARK 500 2 ALA A 69 -45.86 172.32
REMARK 500 2 TYR A 74 -36.97 91.00
REMARK 500 2 ARG A 90 -33.51 120.25
REMARK 500 2 LYS A 91 127.99 -178.01
REMARK 500 2 ILE A 92 76.08 79.79
REMARK 500 2 LEU A 93 -35.04 177.35
REMARK 500 2 LEU A 115 -77.24 -71.61
REMARK 500 2 VAL A 117 40.74 81.07
REMARK 500 3 ALA A 61 -13.70 71.46
REMARK 500 3 TYR A 74 -27.13 85.09
REMARK 500 3 ILE A 86 -64.86 -99.42
REMARK 500 3 ASP A 89 -141.91 -139.94
REMARK 500 3 ARG A 90 -179.20 76.79
REMARK 500 4 ILE A 60 -63.18 -152.39
REMARK 500 4 TYR A 74 -28.66 84.00
REMARK 500 4 ILE A 86 -62.85 -100.50
REMARK 500 4 GLU A 87 71.67 32.04
REMARK 500 4 ARG A 90 -24.03 101.69
REMARK 500 4 LYS A 91 118.87 -175.52
REMARK 500 4 ILE A 92 81.81 78.46
REMARK 500 4 LEU A 93 -36.08 176.13
REMARK 500 4 VAL A 98 -63.73 -91.07
REMARK 500 4 GLN A 116 51.51 71.00
REMARK 500 5 ILE A 60 44.89 -148.49
REMARK 500 5 TYR A 74 -39.51 96.16
REMARK 500 5 ILE A 86 -65.41 -106.10
REMARK 500 5 ARG A 90 -38.26 171.81
REMARK 500 5 LYS A 91 131.92 169.08
REMARK 500 5 ILE A 92 78.04 70.18
REMARK 500 5 LEU A 93 -34.07 169.54
REMARK 500 5 LEU A 115 -76.94 -103.80
REMARK 500 6 ILE A 60 -63.85 -160.05
REMARK 500 6 TYR A 74 -21.48 87.07
REMARK 500 6 ILE A 86 -70.88 -105.85
REMARK 500 6 ARG A 90 -27.51 89.96
REMARK 500 6 LYS A 91 118.67 -178.57
REMARK 500 6 ILE A 92 82.41 79.50
REMARK 500 6 LEU A 93 -32.92 167.80
REMARK 500 6 GLN A 116 50.71 71.16
REMARK 500 7 ILE A 60 -64.19 -147.57
REMARK 500 7 TYR A 74 -25.57 83.43
REMARK 500 7 ASP A 89 2.57 174.33
REMARK 500 7 ARG A 90 39.34 -95.74
REMARK 500 7 LYS A 91 131.89 112.57
REMARK 500 7 ILE A 92 12.96 86.88
REMARK 500 7 LEU A 115 -75.85 -102.76
REMARK 500 8 ILE A 60 -60.38 -141.50
REMARK 500 8 ARG A 68 31.71 -86.88
REMARK 500 8 TYR A 74 -22.20 82.12
REMARK 500 8 ILE A 86 -71.48 -98.09
REMARK 500 8 ARG A 90 -26.77 107.89
REMARK 500 8 LYS A 91 132.07 177.52
REMARK 500 8 ILE A 92 14.92 85.53
REMARK 500 9 ILE A 60 -58.90 -137.52
REMARK 500 9 ALA A 69 -49.61 175.91
REMARK 500 9 TYR A 74 -26.63 84.76
REMARK 500 9 LEU A 88 -166.70 -124.13
REMARK 500 9 ASP A 89 164.56 48.99
REMARK 500 9 ARG A 90 66.76 95.44
REMARK 500 9 LYS A 91 73.61 43.73
REMARK 500 9 ILE A 92 -48.14 -149.60
REMARK 500 9 VAL A 111 33.79 -93.55
REMARK 500 9 LEU A 115 -81.53 -71.60
REMARK 500 10 ILE A 60 -64.99 -131.07
REMARK 500 10 TYR A 74 -26.69 84.66
REMARK 500 10 ILE A 86 -72.88 -88.79
REMARK 500 10 ASP A 89 -51.22 -149.46
REMARK 500 10 LEU A 93 -36.99 -156.70
REMARK 500 11 ILE A 60 -62.08 -161.39
REMARK 500 11 TYR A 74 -29.44 81.15
REMARK 500 11 GLU A 87 80.01 58.22
REMARK 500 11 LEU A 88 -153.33 -121.05
REMARK 500 11 ASP A 89 90.88 25.25
REMARK 500 11 LYS A 91 132.48 171.78
REMARK 500 11 ILE A 92 24.38 85.22
REMARK 500 11 GLN A 116 49.85 70.59
REMARK 500 12 ILE A 60 -62.09 -148.51
REMARK 500 12 TYR A 74 -28.81 79.44
REMARK 500 12 LYS A 91 126.21 126.65
REMARK 500 12 ILE A 92 82.45 81.18
REMARK 500 12 LEU A 93 -35.84 179.08
REMARK 500 13 ILE A 60 -69.27 -138.26
REMARK 500 13 TYR A 74 -19.04 83.08
REMARK 500 13 ASP A 89 131.51 161.99
REMARK 500 13 ARG A 90 80.52 179.38
REMARK 500 13 LYS A 91 61.35 76.11
REMARK 500 13 ILE A 92 -33.75 -152.63
REMARK 500 13 ALA A 94 -47.12 -25.98
REMARK 500 14 ILE A 60 -77.44 -141.56
REMARK 500 14 TYR A 74 -28.96 83.10
REMARK 500 14 ARG A 90 53.81 94.70
REMARK 500 14 LYS A 91 64.55 68.75
REMARK 500 14 ILE A 92 -47.09 -158.70
REMARK 500 14 GLN A 116 -69.64 -157.86
REMARK 500 14 VAL A 117 -26.73 -162.33
REMARK 500 15 ILE A 60 -57.39 -147.47
REMARK 500 15 ALA A 69 -47.98 -179.57
REMARK 500 15 TYR A 74 -22.87 92.36
REMARK 500 15 LEU A 88 -161.26 -126.94
REMARK 500 15 LYS A 91 137.99 165.74
REMARK 500 15 ILE A 92 4.89 86.97
REMARK 500 15 VAL A 98 -62.73 -97.51
REMARK 500 15 ASP A 100 75.44 -119.44
REMARK 500 15 GLN A 116 42.14 70.86
REMARK 500 16 ILE A 60 -74.40 -149.10
REMARK 500 16 TYR A 74 -26.83 82.16
REMARK 500 16 ILE A 86 -66.91 -98.23
REMARK 500 16 LEU A 88 -127.72 -121.08
REMARK 500 16 ASP A 89 -173.96 73.41
REMARK 500 16 ARG A 90 50.35 87.11
REMARK 500 16 LYS A 91 65.68 70.16
REMARK 500 16 ILE A 92 -46.55 -159.38
REMARK 500 17 ILE A 60 -86.63 -141.03
REMARK 500 17 TYR A 74 -15.01 83.31
REMARK 500 17 ARG A 90 -168.88 -125.77
REMARK 500 17 GLN A 116 36.87 71.48
REMARK 500 18 ILE A 60 -65.02 -160.04
REMARK 500 18 TYR A 74 -31.67 82.54
REMARK 500 18 ILE A 86 -71.37 -111.44
REMARK 500 18 ARG A 90 -33.36 -148.19
REMARK 500 18 LYS A 91 135.81 177.16
REMARK 500 18 ILE A 92 -3.19 91.54
REMARK 500 19 ILE A 60 -56.28 -150.22
REMARK 500 19 TYR A 74 -30.42 85.56
REMARK 500 19 ILE A 86 -69.43 -103.18
REMARK 500 19 GLU A 87 62.76 37.93
REMARK 500 19 ARG A 90 -29.65 163.55
REMARK 500 19 LYS A 91 123.67 -178.41
REMARK 500 19 ILE A 92 82.89 76.18
REMARK 500 19 LEU A 93 -33.64 168.33
REMARK 500 20 ILE A 60 -76.21 -159.17
REMARK 500 20 ARG A 68 35.40 -90.19
REMARK 500 20 TYR A 74 -28.03 81.38
REMARK 500 20 GLU A 87 76.65 22.46
REMARK 500 20 LEU A 88 -135.42 -126.70
REMARK 500 20 ASP A 89 96.44 70.10
REMARK 500 20 ARG A 90 58.69 -160.62
REMARK 500 20 LYS A 91 65.80 66.33
REMARK 500 20 ILE A 92 -53.18 -151.07
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 115 GLN A 116 1 -144.04
REMARK 500 LEU A 115 GLN A 116 5 -145.47
REMARK 500 LEU A 115 GLN A 116 7 -144.31
REMARK 500 VAL A 111 LYS A 112 9 149.93
REMARK 500 ASP A 89 ARG A 90 10 -145.01
REMARK 500 ASP A 89 ARG A 90 13 111.56
REMARK 500 LEU A 115 GLN A 116 18 -146.91
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 13 TRP A 59 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 9 ARG A 90 24.9 L L OUTSIDE RANGE
REMARK 500 9 LYS A 91 19.0 L L OUTSIDE RANGE
REMARK 500 10 ILE A 60 24.6 L L OUTSIDE RANGE
REMARK 500 20 ILE A 60 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GYZ A 59 118 UNP O67086 RL20_AQUAE 59 118
SEQRES 1 A 60 TRP ILE ALA ARG ILE ASN ALA ALA VAL ARG ALA TYR GLY
SEQRES 2 A 60 LEU ASN TYR SER THR PHE ILE ASN GLY LEU LYS LYS ALA
SEQRES 3 A 60 GLY ILE GLU LEU ASP ARG LYS ILE LEU ALA ASP MET ALA
SEQRES 4 A 60 VAL ARG ASP PRO GLN ALA PHE GLU GLN VAL VAL ASN LYS
SEQRES 5 A 60 VAL LYS GLU ALA LEU GLN VAL GLN
HELIX 1 1 ILE A 60 ARG A 68 1 9
HELIX 2 2 TYR A 74 GLY A 85 1 12
HELIX 3 3 LEU A 93 ASP A 100 1 8
HELIX 4 4 ASP A 100 LEU A 115 1 16
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 25 2 Bytes