Header list of 1gjx.pdb file
Complete list - r 25 2 Bytes
HEADER OXIDOREDUCTASE 03-AUG-01 1GJX
TITLE SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC
TITLE 2 DIHYDROLIPOYL DEHYDROGENASE P64K FROM NEISSERIA
TITLE 3 MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIPOYL DOMAIN RESIDUES 2-82;
COMPND 5 SYNONYM: LIPOAMIDE DEHYDROGENASE, E3 COMPONENT;
COMPND 6 EC: 1.8.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 487;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PM-143
KEYWDS OXIDOREDUCTASE, LIPOYL DOMAIN, DIHYDROLIPOYL DEHYDROGENASE,
KEYWDS 2 MULTIENZYME COMPLEX, NEISSERIA MENINGITIDIS,
KEYWDS 3 POST-TRANSLATIONAL MODIFICATION
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR K.TOZAWA,R.W.BROADHURST,A.R.C.RAINE,C.FULLER,A.ALVAREZ,
AUTHOR 2 G.GUILLEN,G.PADRON,R.N.PERHAM
REVDAT 2 24-FEB-09 1GJX 1 VERSN
REVDAT 1 28-NOV-01 1GJX 0
JRNL AUTH K.TOZAWA,R.W.BROADHURST,A.R.RAINE,C.FULLER,
JRNL AUTH 2 A.ALVAREZ,G.GUILLEN,G.PADRON,R.N.PERHAM
JRNL TITL SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE
JRNL TITL 2 CHIMERIC DIHYDROLIPOYL DEHYDROGENASE P64K FROM
JRNL TITL 3 NEISSERIA MENINGITIDIS
JRNL REF EUR.J.BIOCHEM. V. 268 4908 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11559360
JRNL DOI 10.1046/J.0014-2956.2001.02422.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 1GJX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-01.
REMARK 100 THE PDBE ID CODE IS EBI-8427.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY, TOCSY, HNCA, HN
REMARK 210 (CO)CA, 15N NOESY-HSQC,
REMARK 210 15N-TOCSY-HSQC, HCCH-TOCSY,
REMARK 210 13C-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA, ANSIG3.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATIONS, LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED LIPOYL DOMAIN
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 H LEU A 5 - O VAL A 73 1.57
REMARK 500 H LEU A 35 - O VAL A 47 1.52
REMARK 500 H LYS A 56 - O VAL A 74 1.56
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 LEU A 2 172.50 56.59
REMARK 500 1 LEU A 5 -176.01 -51.87
REMARK 500 1 PRO A 8 -167.05 -72.70
REMARK 500 1 HIS A 13 -85.71 175.06
REMARK 500 1 GLU A 22 47.72 -140.09
REMARK 500 1 VAL A 31 48.54 -86.03
REMARK 500 1 ASP A 32 73.89 163.65
REMARK 500 1 THR A 40 -89.58 -132.55
REMARK 500 1 ASP A 41 21.68 -150.26
REMARK 500 1 LYS A 42 -43.44 -134.71
REMARK 500 1 ALA A 49 150.05 59.67
REMARK 500 1 VAL A 51 -178.83 -178.33
REMARK 500 1 VAL A 58 119.68 -165.37
REMARK 500 1 LYS A 61 -159.93 -170.97
REMARK 500 1 LEU A 71 95.45 49.06
REMARK 500 1 ILE A 72 -74.86 -95.20
REMARK 500 1 ALA A 77 138.04 57.12
REMARK 500 2 PRO A 8 -169.36 -75.37
REMARK 500 2 ASN A 15 94.95 46.01
REMARK 500 2 GLU A 22 59.48 -146.41
REMARK 500 2 VAL A 31 47.68 -87.96
REMARK 500 2 ASP A 32 70.45 166.61
REMARK 500 2 THR A 40 -59.26 -121.28
REMARK 500 2 ASP A 41 -38.39 -172.68
REMARK 500 2 MET A 45 -164.54 -117.25
REMARK 500 2 ALA A 49 106.16 56.10
REMARK 500 2 GLU A 50 70.69 -110.60
REMARK 500 2 VAL A 60 148.55 -173.58
REMARK 500 2 ILE A 72 -85.74 -48.07
REMARK 500 2 ALA A 77 147.05 56.73
REMARK 500 3 LEU A 2 176.86 -49.90
REMARK 500 3 PRO A 8 -166.17 -76.38
REMARK 500 3 ASN A 15 95.51 44.89
REMARK 500 3 GLU A 22 40.09 -146.30
REMARK 500 3 VAL A 31 42.45 -89.94
REMARK 500 3 ASP A 32 72.84 163.70
REMARK 500 3 THR A 40 -82.92 -133.03
REMARK 500 3 ASP A 41 -43.48 -143.79
REMARK 500 3 ALA A 43 133.64 -175.65
REMARK 500 3 MET A 45 -167.95 -117.29
REMARK 500 3 PRO A 48 33.35 -89.64
REMARK 500 3 ALA A 49 163.93 56.57
REMARK 500 3 GLU A 50 44.83 -157.76
REMARK 500 3 ASP A 64 132.81 -173.15
REMARK 500 3 LEU A 71 94.43 -53.06
REMARK 500 3 ILE A 72 -78.83 -92.45
REMARK 500 3 ALA A 77 124.18 56.39
REMARK 500 3 THR A 80 -71.58 -111.27
REMARK 500 4 LEU A 2 176.33 -51.76
REMARK 500 4 LEU A 5 155.18 -48.41
REMARK 500 4 PRO A 8 -166.66 -68.73
REMARK 500 4 HIS A 13 176.51 171.26
REMARK 500 4 ASN A 15 66.75 169.82
REMARK 500 4 GLU A 22 44.19 -150.23
REMARK 500 4 VAL A 31 39.53 -91.14
REMARK 500 4 ASP A 32 68.25 168.29
REMARK 500 4 ASP A 41 -43.28 -151.00
REMARK 500 4 LYS A 42 25.43 -141.40
REMARK 500 4 PRO A 48 35.81 -90.86
REMARK 500 4 ALA A 49 175.47 59.72
REMARK 500 4 GLU A 50 43.31 -162.85
REMARK 500 4 VAL A 51 167.18 176.23
REMARK 500 4 LYS A 61 -163.09 -160.42
REMARK 500 4 ILE A 72 -80.20 -49.35
REMARK 500 4 ALA A 77 122.66 57.57
REMARK 500 5 PRO A 8 -166.79 -63.32
REMARK 500 5 HIS A 13 -85.86 -157.31
REMARK 500 5 ASN A 15 95.02 44.33
REMARK 500 5 GLU A 22 44.45 -149.07
REMARK 500 5 VAL A 31 48.21 -85.66
REMARK 500 5 ASP A 32 72.80 164.11
REMARK 500 5 THR A 40 -57.54 -121.93
REMARK 500 5 ASP A 41 -37.12 -175.33
REMARK 500 5 PRO A 48 34.13 -89.58
REMARK 500 5 ALA A 49 -51.25 81.64
REMARK 500 5 VAL A 51 -169.97 -174.16
REMARK 500 5 LYS A 61 -160.60 -161.43
REMARK 500 5 ILE A 72 -73.96 -49.95
REMARK 500 5 GLU A 76 46.70 -101.10
REMARK 500 5 ALA A 77 143.37 -36.04
REMARK 500 6 PRO A 8 -168.04 -75.32
REMARK 500 6 HIS A 13 -174.01 -179.08
REMARK 500 6 ASN A 15 78.71 43.74
REMARK 500 6 VAL A 31 47.90 -91.94
REMARK 500 6 ASP A 32 67.24 172.68
REMARK 500 6 ASP A 41 -37.92 -174.63
REMARK 500 6 ALA A 43 131.47 177.25
REMARK 500 6 PRO A 48 37.27 -87.37
REMARK 500 6 ALA A 49 93.44 46.83
REMARK 500 6 VAL A 51 148.73 163.43
REMARK 500 6 LYS A 59 59.35 -140.65
REMARK 500 6 ILE A 72 -80.72 -87.35
REMARK 500 6 ALA A 77 116.40 60.99
REMARK 500 7 VAL A 7 147.04 58.75
REMARK 500 7 GLU A 14 -168.27 -66.52
REMARK 500 7 ASN A 15 94.94 44.15
REMARK 500 7 GLU A 22 32.86 -153.30
REMARK 500 7 VAL A 31 41.31 -90.32
REMARK 500 7 ASP A 32 67.50 168.05
REMARK 500 7 THR A 40 -72.27 -120.70
REMARK 500 7 ASP A 41 25.77 -159.72
REMARK 500 7 LYS A 42 -43.42 176.24
REMARK 500 7 MET A 45 -165.28 -104.07
REMARK 500 7 PRO A 48 42.11 -89.35
REMARK 500 7 ALA A 49 177.04 55.70
REMARK 500 7 GLU A 50 38.25 -163.19
REMARK 500 7 VAL A 51 168.93 175.74
REMARK 500 7 ILE A 72 -76.87 -43.26
REMARK 500 7 ALA A 77 131.06 59.40
REMARK 500 7 THR A 80 114.02 174.34
REMARK 500 8 PRO A 8 -167.47 -70.78
REMARK 500 8 HIS A 13 158.63 169.43
REMARK 500 8 ASN A 15 57.27 -179.34
REMARK 500 8 ASP A 32 70.78 162.09
REMARK 500 8 THR A 37 51.95 -157.70
REMARK 500 8 LEU A 38 163.73 -41.83
REMARK 500 8 THR A 40 -82.87 -102.01
REMARK 500 8 ASP A 41 21.41 -150.96
REMARK 500 8 LYS A 42 -41.42 -179.98
REMARK 500 8 PRO A 48 35.41 -88.40
REMARK 500 8 ALA A 49 168.34 54.23
REMARK 500 8 GLU A 50 67.88 -165.65
REMARK 500 8 SER A 67 48.39 -147.13
REMARK 500 8 ILE A 72 -82.96 -45.98
REMARK 500 8 ALA A 77 159.84 53.62
REMARK 500 8 THR A 80 -49.57 -177.35
REMARK 500 9 LEU A 2 174.88 -53.17
REMARK 500 9 PRO A 8 -166.08 -68.72
REMARK 500 9 HIS A 13 -162.49 -129.92
REMARK 500 9 GLU A 14 -179.67 -68.09
REMARK 500 9 ASN A 15 95.47 44.03
REMARK 500 9 ILE A 19 10.07 -140.75
REMARK 500 9 ALA A 20 146.48 -177.95
REMARK 500 9 GLU A 22 39.19 -148.82
REMARK 500 9 VAL A 31 33.16 -94.34
REMARK 500 9 ASP A 32 62.14 176.23
REMARK 500 9 ASP A 41 -41.39 -168.53
REMARK 500 9 ALA A 43 118.96 -178.51
REMARK 500 9 PRO A 48 37.74 -88.07
REMARK 500 9 ALA A 49 95.41 44.66
REMARK 500 9 VAL A 51 141.33 161.85
REMARK 500 9 LYS A 59 67.96 -152.27
REMARK 500 9 LYS A 61 -167.24 -171.81
REMARK 500 9 ILE A 72 -76.46 -52.35
REMARK 500 10 LEU A 2 177.15 -55.18
REMARK 500 10 PRO A 8 -168.44 -73.69
REMARK 500 10 ASN A 15 73.16 169.32
REMARK 500 10 VAL A 23 113.93 -163.95
REMARK 500 10 VAL A 31 41.85 -90.21
REMARK 500 10 ASP A 32 73.84 172.08
REMARK 500 10 THR A 37 56.90 -142.08
REMARK 500 10 LEU A 38 166.29 -41.45
REMARK 500 10 THR A 40 -72.65 -100.04
REMARK 500 10 ASP A 41 26.99 -160.22
REMARK 500 10 LYS A 42 -42.10 173.04
REMARK 500 10 ALA A 49 151.44 59.28
REMARK 500 10 VAL A 51 153.36 176.81
REMARK 500 10 LYS A 61 -172.89 -171.89
REMARK 500 10 ILE A 72 -79.88 -48.11
REMARK 500 10 ALA A 77 133.44 57.21
REMARK 500 10 THR A 80 177.94 55.68
REMARK 500 11 PRO A 8 -169.72 -76.94
REMARK 500 11 ASN A 15 95.05 45.38
REMARK 500 11 VAL A 31 41.24 -91.55
REMARK 500 11 ASP A 32 71.97 167.14
REMARK 500 11 THR A 37 45.79 -144.56
REMARK 500 11 LEU A 38 165.66 -39.69
REMARK 500 11 THR A 40 -158.38 -120.35
REMARK 500 11 LYS A 42 54.81 -162.78
REMARK 500 11 ALA A 43 113.27 -178.78
REMARK 500 11 PRO A 48 36.83 -90.92
REMARK 500 11 ALA A 49 160.91 57.88
REMARK 500 11 VAL A 51 153.68 165.25
REMARK 500 11 VAL A 58 137.83 -173.83
REMARK 500 11 LYS A 59 51.01 -153.12
REMARK 500 11 LYS A 61 145.78 -170.72
REMARK 500 11 ILE A 72 -83.60 -46.84
REMARK 500 11 ALA A 77 107.56 65.08
REMARK 500 12 PRO A 8 -168.17 -73.79
REMARK 500 12 ASN A 15 76.54 162.64
REMARK 500 12 VAL A 31 44.24 -90.00
REMARK 500 12 ASP A 32 73.12 170.62
REMARK 500 12 THR A 37 57.51 -144.39
REMARK 500 12 LEU A 38 162.63 -39.16
REMARK 500 12 THR A 40 -83.79 -123.71
REMARK 500 12 ASP A 41 -42.75 -144.56
REMARK 500 12 ALA A 43 136.62 176.21
REMARK 500 12 PRO A 48 30.13 -90.02
REMARK 500 12 ALA A 49 102.80 51.35
REMARK 500 12 VAL A 60 148.62 -173.13
REMARK 500 12 ILE A 72 -82.92 -43.18
REMARK 500 12 ALA A 77 149.03 56.94
REMARK 500 13 PRO A 8 -168.16 -70.04
REMARK 500 13 HIS A 13 -176.59 172.84
REMARK 500 13 ASN A 15 91.06 42.73
REMARK 500 13 VAL A 16 -154.56 -127.79
REMARK 500 13 GLU A 22 75.02 -161.26
REMARK 500 13 VAL A 31 43.96 -90.39
REMARK 500 13 ASP A 32 68.02 178.28
REMARK 500 13 THR A 40 -58.96 -131.49
REMARK 500 13 ASP A 41 -38.30 -175.24
REMARK 500 13 ALA A 43 170.74 175.38
REMARK 500 13 MET A 45 -168.56 -109.09
REMARK 500 13 PRO A 48 30.41 -89.74
REMARK 500 13 ALA A 49 106.41 53.53
REMARK 500 13 GLU A 50 69.56 -102.95
REMARK 500 13 VAL A 60 148.53 -170.21
REMARK 500 13 LEU A 71 74.15 42.84
REMARK 500 13 ILE A 72 -76.28 -66.75
REMARK 500 13 GLU A 76 45.99 -102.61
REMARK 500 13 ALA A 77 152.55 -39.94
REMARK 500 14 PRO A 8 -166.69 -73.13
REMARK 500 14 GLU A 14 -169.96 -110.49
REMARK 500 14 ASN A 15 71.09 46.01
REMARK 500 14 VAL A 31 44.07 -90.26
REMARK 500 14 ASP A 32 70.03 163.75
REMARK 500 14 THR A 40 -58.35 -120.32
REMARK 500 14 ASP A 41 -36.06 -179.54
REMARK 500 14 MET A 45 -166.31 -120.00
REMARK 500 14 PRO A 48 30.64 -90.28
REMARK 500 14 ALA A 49 164.44 56.17
REMARK 500 14 GLU A 50 46.10 -160.61
REMARK 500 14 LYS A 61 128.60 -172.56
REMARK 500 14 SER A 67 51.09 -144.95
REMARK 500 14 ILE A 72 -83.46 -46.31
REMARK 500 14 ALA A 77 139.88 58.35
REMARK 500 15 LYS A 6 59.72 -149.59
REMARK 500 15 VAL A 7 145.62 60.83
REMARK 500 15 PRO A 8 -89.58 -67.99
REMARK 500 15 ASP A 9 56.83 166.60
REMARK 500 15 HIS A 13 164.17 170.97
REMARK 500 15 ASN A 15 85.88 176.97
REMARK 500 15 GLU A 22 25.48 -155.17
REMARK 500 15 VAL A 31 39.57 -90.85
REMARK 500 15 ASP A 32 64.95 168.19
REMARK 500 15 THR A 40 -59.39 -124.76
REMARK 500 15 ASP A 41 -40.48 -171.84
REMARK 500 15 PRO A 48 43.53 -88.82
REMARK 500 15 ALA A 49 171.12 54.35
REMARK 500 15 GLU A 50 33.03 -156.09
REMARK 500 15 VAL A 58 119.60 -160.57
REMARK 500 15 LEU A 71 44.37 -157.58
REMARK 500 15 ILE A 72 -82.45 -40.63
REMARK 500 15 ALA A 77 132.70 59.60
REMARK 500 15 THR A 80 85.27 -57.43
REMARK 500 16 LEU A 2 172.10 -51.91
REMARK 500 16 VAL A 7 139.46 59.83
REMARK 500 16 PRO A 8 -166.59 -72.65
REMARK 500 16 ASP A 9 72.24 -101.68
REMARK 500 16 HIS A 13 171.07 170.28
REMARK 500 16 ASN A 15 85.52 44.49
REMARK 500 16 ALA A 30 -169.01 -123.94
REMARK 500 16 VAL A 31 43.79 -90.64
REMARK 500 16 ASP A 32 68.83 171.84
REMARK 500 16 THR A 37 38.13 -161.30
REMARK 500 16 LEU A 38 152.51 -31.87
REMARK 500 16 THR A 40 -58.01 -123.90
REMARK 500 16 ASP A 41 -34.05 174.78
REMARK 500 16 PRO A 48 31.33 -90.79
REMARK 500 16 ALA A 49 99.03 49.40
REMARK 500 16 LYS A 61 -161.28 -164.90
REMARK 500 16 ILE A 72 -70.31 -53.88
REMARK 500 16 ALA A 77 125.64 57.71
REMARK 500 17 LEU A 2 175.41 56.55
REMARK 500 17 PRO A 8 -156.75 -66.76
REMARK 500 17 ASN A 15 78.66 44.00
REMARK 500 17 GLU A 22 41.80 -159.28
REMARK 500 17 VAL A 31 39.06 -94.18
REMARK 500 17 ASP A 32 64.50 172.35
REMARK 500 17 THR A 37 53.82 -144.03
REMARK 500 17 LEU A 38 154.30 -38.13
REMARK 500 17 GLU A 39 117.88 -160.40
REMARK 500 17 THR A 40 -85.04 -70.94
REMARK 500 17 ASP A 41 23.16 -153.00
REMARK 500 17 LYS A 42 -43.43 -177.28
REMARK 500 17 PRO A 48 30.60 -90.39
REMARK 500 17 ALA A 49 99.80 50.34
REMARK 500 17 VAL A 51 144.60 161.75
REMARK 500 17 LEU A 71 79.69 48.38
REMARK 500 17 ILE A 72 -73.94 -73.19
REMARK 500 17 ALA A 77 -178.43 84.39
REMARK 500 18 LEU A 2 170.03 62.12
REMARK 500 18 VAL A 7 149.27 58.55
REMARK 500 18 PRO A 8 -157.53 -83.17
REMARK 500 18 ASN A 15 86.39 47.93
REMARK 500 18 VAL A 16 -155.39 -137.94
REMARK 500 18 GLU A 22 28.39 -142.39
REMARK 500 18 VAL A 31 47.84 -86.66
REMARK 500 18 ASP A 32 74.80 166.85
REMARK 500 18 ASP A 33 117.72 -160.46
REMARK 500 18 THR A 40 -157.35 -142.25
REMARK 500 18 LYS A 42 53.06 -172.79
REMARK 500 18 ALA A 43 134.48 -173.47
REMARK 500 18 ALA A 49 93.44 46.72
REMARK 500 18 VAL A 58 116.34 -160.80
REMARK 500 18 SER A 67 49.49 -154.59
REMARK 500 18 ILE A 72 -83.23 -45.05
REMARK 500 18 ALA A 77 162.86 54.06
REMARK 500 18 THR A 80 35.30 -159.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GJX A 1 81 UNP Q9JZ09 Q9JZ09 2 82
SEQRES 1 A 81 ALA LEU VAL GLU LEU LYS VAL PRO ASP ILE GLY GLY HIS
SEQRES 2 A 81 GLU ASN VAL ASP ILE ILE ALA VAL GLU VAL ASN VAL GLY
SEQRES 3 A 81 ASP THR ILE ALA VAL ASP ASP THR LEU ILE THR LEU GLU
SEQRES 4 A 81 THR ASP LYS ALA THR MET ASP VAL PRO ALA GLU VAL ALA
SEQRES 5 A 81 GLY VAL VAL LYS GLU VAL LYS VAL LYS VAL GLY ASP LYS
SEQRES 6 A 81 ILE SER GLU GLY GLY LEU ILE VAL VAL VAL GLU ALA GLU
SEQRES 7 A 81 GLY THR ALA
SHEET 1 AA 4 LEU A 2 LYS A 6 0
SHEET 2 AA 4 ILE A 72 ALA A 77 -1 O VAL A 75 N VAL A 3
SHEET 3 AA 4 LYS A 56 LYS A 61 -1 O GLU A 76 N LYS A 56
SHEET 4 AA 4 ASP A 27 ALA A 30 -1 O LYS A 56 N ASP A 27
SHEET 1 AB 4 ALA A 43 VAL A 47 0
SHEET 2 AB 4 LEU A 35 THR A 40 -1 O ILE A 36 N VAL A 47
SHEET 3 AB 4 ILE A 18 VAL A 21 -1 O ASP A 17 N GLU A 39
SHEET 4 AB 4 ASP A 64 SER A 67 -1 O ILE A 66 N VAL A 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