Header list of 1o78.pdb file
Complete list - r 25 2 Bytes
HEADER CARRIER PROTEIN 24-OCT-02 1O78
TITLE BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (1.3S)
TITLE 2 [10-48] DELETION MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOTIN CARBOXYL CARRIER PROTEIN OF
COMPND 3 METHYLMALONYL-COA CARBOXYL-TRANSFERASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: TRANSCARBOXYLASE, 1.3S SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: RESIDUES 10-48 DELETION MUTANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROPIONIBACTERIUM FREUDENREICHII
SOURCE 3 SUBSP. SHERMANII;
SOURCE 4 ORGANISM_TAXID: 1752;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTAC1.3DELTA10-48, PCY216
KEYWDS CARRIER PROTEIN, TRANSCARBOXYLASE, CARBOXYL CARRIER,
KEYWDS 2 TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.M.JANK,J.D.SADOWSKY,C.PEIKERT,S.BERGER
REVDAT 2 24-FEB-09 1O78 1 VERSN
REVDAT 1 21-NOV-02 1O78 0
JRNL AUTH M.M.JANK,J.D.SADOWSKY,C.PEIKERT,S.BERGER
JRNL TITL NMR STUDIES ON THE SOLUTION STRUCTURE OF A
JRNL TITL 2 DELETION MUTANT OF THE TRANSCARBOXYLASE BIOTIN
JRNL TITL 3 CARRIER SUBUNIT
JRNL REF INT.J.BIOL.MACROMOL. V. 30 233 2002
JRNL REFN ISSN 0141-8130
JRNL PMID 12297230
JRNL DOI 10.1016/S0141-8130(02)00033-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.V.REDDY,B.C.SHENOY,P.R.CAREY,F.D.SONNICHSEN
REMARK 1 TITL HIGH RESOLUTION SOLUTION STRUCTURE OF THE 1.3S
REMARK 1 TITL 2 SUBUNIT OF TRANSCARBOXYLASE FROM PROPIONIBACTERIUM
REMARK 1 TITL 3 SHERMANII(DAGGER)
REMARK 1 REF BIOCHEMISTRY V. 39 2509 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 10704200
REMARK 1 DOI 10.1021/BI9925367
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.M.JANK,S.BOKORNY,K.-H.ROEHM,S.BERGER
REMARK 1 TITL EXPRESSION AND BIOTINYLATION OF A MUTANT OF THE
REMARK 1 TITL 2 TRANSCARBOXYLASE CARRIER PROTEIN FROM PROPIONI
REMARK 1 TITL 3 SHERMANII
REMARK 1 REF PROTEIN EXPR.PURIF. V. 17 123 1999
REMARK 1 REFN ISSN 1046-5928
REMARK 1 PMID 10497077
REMARK 1 DOI 10.1006/PREP.1999.1097
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DGSA, REFINEMENT WITH NOES AND
REMARK 3 HYDROGEN-BOND CONSTRAINTS
REMARK 4
REMARK 4 1O78 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-OCT-02.
REMARK 100 THE PDBE ID CODE IS EBI-11596.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 2 MM AMMONIUM ACETATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.3 MM PROTEIN, N15/C13
REMARK 210 LABELED TC 1.3S [10-48],
REMARK 210 BIOTIN (UNLABELED)
REMARK 210 COVALENTLY ATTACHED TO LYS 89
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC-NOESY, HNCA,
REMARK 210 HNCO, CBCANH, CBCA(CO)NH,
REMARK 210 HN(CA)CO, HCACO,HN-HSQC-TOCSY,
REMARK 210 HBHA(CBCACO)NH,(H)N(CA)NNH,
REMARK 210 HCCH-TOCSY,2D 15N-1H HSQC
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 : X-PLOR, PROCHECK 3.5.3,
REMARK 210 AQUA 2.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY/
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. BIOTIN WAS
REMARK 210 UNLABELED AND NOT INCLUDED IN THE STRUCTURE CALCULATION.
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 400
REMARK 400 COMPOUND
REMARK 400 BIOTINYL 1.3S SUBUNIT (CHAIN A) SERVES AS A CARBOXYL CARRIER
REMARK 400 BETWEEN THE SUBSTRATE BINDING SITES ON THE 12S AND 5S SUBUNITS.
REMARK 400 TRANSCARBOXYLASE IS COMPRISED OF THREE SUBUNITS: 1.3S,
REMARK 400 5S, AND 12S.
REMARK 400
REMARK 400 RESIDUES 10-48 DELETION MUTANT, CHAIN A
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 THR A 6 159.55 59.06
REMARK 500 1 LEU A 22 -49.13 -151.84
REMARK 500 1 LYS A 28 133.81 -174.00
REMARK 500 1 THR A 42 95.69 -52.10
REMARK 500 1 LEU A 44 -160.01 -167.11
REMARK 500 1 GLU A 47 100.14 -161.79
REMARK 500 1 MET A 49 49.57 -149.88
REMARK 500 1 MET A 51 27.32 -152.33
REMARK 500 1 GLU A 52 -81.47 -143.06
REMARK 500 1 THR A 53 -152.44 51.92
REMARK 500 1 GLU A 54 109.77 -54.25
REMARK 500 1 LYS A 65 137.47 179.17
REMARK 500 1 VAL A 74 56.58 36.84
REMARK 500 2 LYS A 4 -178.13 53.81
REMARK 500 2 THR A 6 -70.25 -127.66
REMARK 500 2 LEU A 22 59.09 -171.54
REMARK 500 2 THR A 42 104.59 -59.05
REMARK 500 2 LYS A 65 117.49 178.44
REMARK 500 2 ARG A 71 -45.49 177.83
REMARK 500 2 VAL A 74 164.41 56.44
REMARK 500 2 LEU A 80 -65.90 -135.50
REMARK 500 3 LYS A 2 59.67 -98.33
REMARK 500 3 LEU A 3 -50.45 -162.25
REMARK 500 3 THR A 6 31.20 -159.54
REMARK 500 3 LYS A 28 126.71 -172.69
REMARK 500 3 LYS A 32 46.01 -145.35
REMARK 500 3 THR A 42 94.63 -54.42
REMARK 500 3 GLU A 47 -176.38 52.82
REMARK 500 3 ALA A 48 -62.60 -163.30
REMARK 500 3 MET A 51 117.90 -175.79
REMARK 500 3 GLU A 52 94.99 -53.12
REMARK 500 3 ILE A 55 91.19 -68.85
REMARK 500 3 LYS A 65 89.27 179.24
REMARK 500 4 LYS A 4 -54.33 -132.18
REMARK 500 4 VAL A 5 137.72 61.14
REMARK 500 4 THR A 6 37.36 -99.14
REMARK 500 4 LYS A 12 177.80 54.39
REMARK 500 4 THR A 42 102.73 -55.68
REMARK 500 4 ALA A 48 -157.92 -125.07
REMARK 500 4 MET A 51 105.30 57.30
REMARK 500 4 GLU A 52 74.31 57.16
REMARK 500 4 LYS A 65 131.15 -179.09
REMARK 500 4 LEU A 67 -58.45 -125.12
REMARK 500 4 GLU A 70 80.29 -63.79
REMARK 500 4 ARG A 71 -47.05 -176.88
REMARK 500 4 VAL A 74 42.74 36.60
REMARK 500 4 LEU A 80 -79.96 -55.73
REMARK 500 5 LYS A 12 -88.42 55.24
REMARK 500 5 LEU A 22 33.20 -142.18
REMARK 500 5 THR A 25 -146.83 -110.23
REMARK 500 5 VAL A 31 -158.03 -98.98
REMARK 500 5 MET A 49 -83.29 59.04
REMARK 500 5 THR A 53 -74.74 61.00
REMARK 500 5 GLU A 54 90.77 -56.08
REMARK 500 5 LYS A 65 138.08 179.69
REMARK 500 5 LEU A 67 -67.44 -126.36
REMARK 500 5 ALA A 73 142.82 61.82
REMARK 500 5 VAL A 74 89.93 34.53
REMARK 500 5 ILE A 81 143.37 -175.67
REMARK 500 6 THR A 6 30.53 37.99
REMARK 500 6 VAL A 26 100.59 -50.28
REMARK 500 6 THR A 42 101.29 -57.19
REMARK 500 6 ALA A 48 -80.34 -129.36
REMARK 500 6 GLU A 52 109.11 -57.59
REMARK 500 6 LYS A 65 156.61 179.36
REMARK 500 6 VAL A 68 153.82 -46.70
REMARK 500 6 GLU A 70 143.45 61.27
REMARK 500 6 ASP A 72 42.62 -154.53
REMARK 500 7 LEU A 3 87.00 51.87
REMARK 500 7 VAL A 7 160.90 57.75
REMARK 500 7 VAL A 26 168.17 -47.38
REMARK 500 7 SER A 27 -42.19 -149.69
REMARK 500 7 LYS A 28 119.42 -160.24
REMARK 500 7 LYS A 32 -162.58 -121.38
REMARK 500 7 ALA A 48 -157.24 -166.64
REMARK 500 7 MET A 51 19.57 56.33
REMARK 500 7 GLU A 52 96.45 179.49
REMARK 500 7 LYS A 65 139.56 -177.86
REMARK 500 8 LEU A 3 54.06 -160.44
REMARK 500 8 VAL A 5 170.13 -54.07
REMARK 500 8 THR A 6 99.95 53.99
REMARK 500 8 VAL A 7 75.38 -119.70
REMARK 500 8 GLU A 17 -175.46 -57.23
REMARK 500 8 LYS A 28 139.94 -172.84
REMARK 500 8 MET A 51 75.52 54.63
REMARK 500 8 THR A 53 -83.80 56.81
REMARK 500 8 GLU A 54 97.60 -58.46
REMARK 500 8 THR A 59 -159.41 -165.69
REMARK 500 8 LYS A 65 174.71 179.99
REMARK 500 8 ASP A 72 67.55 -112.95
REMARK 500 8 ALA A 73 173.30 -59.35
REMARK 500 8 VAL A 74 86.46 53.55
REMARK 500 8 LEU A 80 -68.57 -96.57
REMARK 500 9 LYS A 2 -72.62 62.94
REMARK 500 9 LYS A 12 176.80 53.73
REMARK 500 9 LYS A 32 39.17 -155.93
REMARK 500 9 THR A 36 178.22 -57.61
REMARK 500 9 GLU A 47 109.38 -168.13
REMARK 500 9 ALA A 48 -165.32 -168.30
REMARK 500 9 THR A 53 -127.61 36.50
REMARK 500 9 GLU A 54 133.79 -37.69
REMARK 500 9 LYS A 65 163.60 179.86
REMARK 500 9 ALA A 73 117.17 60.73
REMARK 500 10 LYS A 4 63.30 -106.63
REMARK 500 10 THR A 6 38.40 -153.85
REMARK 500 10 VAL A 31 -158.07 -101.91
REMARK 500 10 GLU A 47 72.60 -154.47
REMARK 500 10 ALA A 48 69.70 -114.04
REMARK 500 10 MET A 49 16.64 59.00
REMARK 500 10 THR A 53 -92.28 52.10
REMARK 500 10 GLU A 54 105.63 -59.90
REMARK 500 10 ALA A 57 175.30 -53.43
REMARK 500 10 THR A 59 -167.66 -163.42
REMARK 500 10 LYS A 65 157.30 178.19
REMARK 500 10 LEU A 67 -70.37 -56.06
REMARK 500 10 LEU A 80 -70.44 -67.90
REMARK 500 11 LYS A 4 -88.92 54.91
REMARK 500 11 VAL A 31 -115.47 -131.52
REMARK 500 11 VAL A 37 -171.79 -67.04
REMARK 500 11 THR A 42 109.80 -52.22
REMARK 500 11 ALA A 48 139.68 -179.32
REMARK 500 11 MET A 49 78.32 54.50
REMARK 500 11 THR A 53 -64.99 65.70
REMARK 500 11 GLU A 54 98.83 -56.57
REMARK 500 11 LYS A 65 149.26 179.97
REMARK 500 11 LEU A 67 -68.52 -138.27
REMARK 500 11 VAL A 68 155.12 -48.55
REMARK 500 11 GLU A 70 72.69 -68.00
REMARK 500 11 ARG A 71 -37.30 -176.79
REMARK 500 11 VAL A 74 48.02 36.91
REMARK 500 11 LEU A 80 -68.75 -109.18
REMARK 500 12 LYS A 12 -38.92 -162.56
REMARK 500 12 THR A 25 -141.99 -68.32
REMARK 500 12 LYS A 28 108.39 -54.95
REMARK 500 12 THR A 42 105.12 -55.25
REMARK 500 12 ALA A 48 -69.21 -176.42
REMARK 500 12 ALA A 57 170.09 -50.77
REMARK 500 12 LYS A 65 169.06 178.50
REMARK 500 12 LEU A 67 -52.62 -129.88
REMARK 500 12 GLU A 70 135.79 61.61
REMARK 500 12 VAL A 74 139.71 60.86
REMARK 500 13 LYS A 4 -155.94 -143.20
REMARK 500 13 THR A 6 -40.55 -161.78
REMARK 500 13 LYS A 12 -74.21 -98.09
REMARK 500 13 THR A 42 94.06 -53.19
REMARK 500 13 MET A 49 42.41 -96.78
REMARK 500 13 GLU A 52 102.21 -56.91
REMARK 500 13 LYS A 65 140.43 -178.31
REMARK 500 13 GLU A 70 135.94 61.97
REMARK 500 14 LYS A 4 155.11 59.94
REMARK 500 14 LEU A 22 127.96 61.52
REMARK 500 14 LYS A 28 122.80 -171.93
REMARK 500 14 THR A 42 109.91 -56.60
REMARK 500 14 LYS A 50 -56.28 -168.91
REMARK 500 14 MET A 51 -73.41 174.44
REMARK 500 14 GLU A 52 -92.48 54.08
REMARK 500 14 THR A 53 -89.78 51.67
REMARK 500 14 LYS A 69 -165.73 -129.69
REMARK 500 14 LEU A 80 -70.05 -92.21
REMARK 500 15 LYS A 2 -166.35 52.74
REMARK 500 15 LEU A 3 51.55 -168.18
REMARK 500 15 THR A 6 -153.86 44.26
REMARK 500 15 LEU A 22 -166.87 53.36
REMARK 500 15 LYS A 28 140.78 -175.52
REMARK 500 15 LYS A 32 52.43 -145.93
REMARK 500 15 LYS A 38 49.58 -142.70
REMARK 500 15 GLU A 52 100.25 55.33
REMARK 500 15 LYS A 65 156.06 179.83
REMARK 500 15 LYS A 69 -164.87 -125.73
REMARK 500 15 ALA A 73 111.12 56.33
REMARK 500 15 LEU A 80 -61.01 -107.64
REMARK 500 16 LYS A 4 24.51 -144.85
REMARK 500 16 VAL A 7 58.30 -165.22
REMARK 500 16 LYS A 12 70.93 56.36
REMARK 500 16 THR A 25 -133.34 -122.99
REMARK 500 16 LYS A 28 94.71 -51.93
REMARK 500 16 ILE A 29 86.74 -68.09
REMARK 500 16 GLU A 52 88.62 53.17
REMARK 500 16 LYS A 65 148.14 -174.84
REMARK 500 16 LEU A 67 -53.31 -130.97
REMARK 500 16 GLU A 70 132.39 61.95
REMARK 500 17 LYS A 2 -170.91 -62.27
REMARK 500 17 THR A 6 82.33 52.93
REMARK 500 17 LYS A 12 -160.02 54.00
REMARK 500 17 ALA A 20 74.34 -113.25
REMARK 500 17 ALA A 48 73.81 -167.93
REMARK 500 17 LYS A 50 29.59 -160.73
REMARK 500 17 MET A 51 -85.67 57.04
REMARK 500 17 GLU A 52 -77.15 62.86
REMARK 500 17 THR A 53 -92.92 44.77
REMARK 500 17 GLU A 54 104.62 -52.14
REMARK 500 17 THR A 59 -171.86 -170.62
REMARK 500 17 LYS A 65 161.10 177.24
REMARK 500 17 ARG A 71 -42.63 74.09
REMARK 500 17 ALA A 73 -156.83 -165.12
REMARK 500 17 VAL A 74 115.85 57.40
REMARK 500 17 LEU A 80 -70.76 -91.51
REMARK 500 18 LEU A 3 -60.13 -125.07
REMARK 500 18 VAL A 7 151.11 60.05
REMARK 500 18 MET A 49 90.56 51.56
REMARK 500 18 MET A 51 -63.28 65.58
REMARK 500 18 GLU A 52 -65.15 67.76
REMARK 500 18 THR A 53 -103.46 52.45
REMARK 500 18 LYS A 65 166.64 179.55
REMARK 500 18 ARG A 71 -36.73 -176.92
REMARK 500 18 ASP A 72 107.84 -51.96
REMARK 500 18 VAL A 74 113.17 57.43
REMARK 500 19 VAL A 7 -77.09 -117.10
REMARK 500 19 LYS A 12 164.92 57.38
REMARK 500 19 SER A 27 -39.52 -134.98
REMARK 500 19 THR A 42 100.93 -53.57
REMARK 500 19 ALA A 48 -156.45 -126.21
REMARK 500 19 MET A 49 39.82 -92.73
REMARK 500 19 LYS A 50 -47.03 -153.04
REMARK 500 19 MET A 51 -173.93 -170.27
REMARK 500 19 LYS A 65 107.14 178.19
REMARK 500 19 GLU A 70 68.10 -68.99
REMARK 500 19 ARG A 71 -42.79 -173.62
REMARK 500 19 VAL A 74 68.82 36.22
REMARK 500 19 LEU A 80 -71.52 -102.15
REMARK 500 20 LEU A 3 93.87 -66.51
REMARK 500 20 LEU A 22 -53.08 -155.26
REMARK 500 20 LYS A 32 -45.91 -165.78
REMARK 500 20 ALA A 48 -160.24 -128.02
REMARK 500 20 GLU A 52 73.37 -154.10
REMARK 500 20 THR A 53 -59.96 66.84
REMARK 500 20 ALA A 57 166.21 -47.84
REMARK 500 20 LYS A 65 164.65 176.87
REMARK 500 20 GLU A 70 76.50 -65.65
REMARK 500 20 ARG A 71 -51.30 179.90
REMARK 500 20 VAL A 74 49.60 36.73
REMARK 500 20 LEU A 80 -58.02 -131.84
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 71 0.19 SIDE CHAIN
REMARK 500 2 ARG A 71 0.31 SIDE CHAIN
REMARK 500 3 ARG A 71 0.20 SIDE CHAIN
REMARK 500 4 ARG A 71 0.24 SIDE CHAIN
REMARK 500 5 ARG A 71 0.25 SIDE CHAIN
REMARK 500 6 ARG A 71 0.27 SIDE CHAIN
REMARK 500 7 ARG A 71 0.24 SIDE CHAIN
REMARK 500 8 ARG A 71 0.31 SIDE CHAIN
REMARK 500 9 ARG A 71 0.24 SIDE CHAIN
REMARK 500 10 ARG A 71 0.21 SIDE CHAIN
REMARK 500 11 ARG A 71 0.21 SIDE CHAIN
REMARK 500 12 ARG A 71 0.25 SIDE CHAIN
REMARK 500 13 ARG A 71 0.20 SIDE CHAIN
REMARK 500 14 ARG A 71 0.30 SIDE CHAIN
REMARK 500 15 ARG A 71 0.20 SIDE CHAIN
REMARK 500 16 ARG A 71 0.19 SIDE CHAIN
REMARK 500 17 ARG A 71 0.21 SIDE CHAIN
REMARK 500 18 ARG A 71 0.17 SIDE CHAIN
REMARK 500 19 ARG A 71 0.24 SIDE CHAIN
REMARK 500 20 ARG A 71 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DCZ RELATED DB: PDB
REMARK 900 BIOTIN CARBOXYL CARRIER DOMAIN OF
REMARK 900 TRANSCARBOXYLASE (TC 1.3S)
REMARK 900 RELATED ID: 1DD2 RELATED DB: PDB
REMARK 900 BIOTIN CARBOXYL CARRIER DOMAIN OF
REMARK 900 TRANSCARBOXYLASE (TC 1.3S)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 10-48 DELETION MUTANT
DBREF 1O78 A 1 9 UNP P02904 BCCP_PROFR 1 9
DBREF 1O78 A 10 84 UNP P02904 BCCP_PROFR 49 123
SEQRES 1 A 84 MET LYS LEU LYS VAL THR VAL ASN GLY ALA GLY LYS ALA
SEQRES 2 A 84 GLY GLU GLY GLU ILE PRO ALA PRO LEU ALA GLY THR VAL
SEQRES 3 A 84 SER LYS ILE LEU VAL LYS GLU GLY ASP THR VAL LYS ALA
SEQRES 4 A 84 GLY GLN THR VAL LEU VAL LEU GLU ALA MET LYS MET GLU
SEQRES 5 A 84 THR GLU ILE ASN ALA PRO THR ASP GLY LYS VAL GLU LYS
SEQRES 6 A 84 VAL LEU VAL LYS GLU ARG ASP ALA VAL GLN GLY GLY GLN
SEQRES 7 A 84 GLY LEU ILE LYS ILE GLY
SHEET 1 AA 3 LYS A 28 ILE A 29 0
SHEET 2 AA 3 THR A 42 VAL A 45 -1 N VAL A 45 O LYS A 28
SHEET 3 AA 3 ILE A 55 ASN A 56 -1 O ILE A 55 N VAL A 43
SHEET 1 AB 3 THR A 36 VAL A 37 0
SHEET 2 AB 3 GLY A 61 VAL A 66 -1 O GLY A 61 N VAL A 37
SHEET 3 AB 3 ILE A 81 ILE A 83 -1 O LYS A 82 N GLU A 64
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