Header list of 1h8b.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL PROTEIN 01-FEB-01 1H8B
TITLE EF-HANDS 3,4 FROM ALPHA-ACTININ / Z-REPEAT 7 FROM TITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-ACTININ 2, SKELETAL MUSCLE ISOFORM;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EF-HANDS 3&4 RESIDUE 822-894;
COMPND 5 SYNONYM: ACT-EF34;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TITIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: Z-REPEAT 7 RESIDUES 648-698;
COMPND 11 SYNONYM: ZR7;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: MUSCLE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 10 ORGANISM_COMMON: RABBIT;
SOURCE 11 ORGANISM_TAXID: 9986;
SOURCE 12 TISSUE: MUSCLE;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL PROTEIN, Z-DISK STRUCTURAL COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR R.A.ATKINSON,C.JOSEPH,G.KELLY,F.W.MUSKETT,T.A.FRENKIEL,
AUTHOR 2 D.NIETLISPACH,A.PASTORE
REVDAT 3 24-FEB-09 1H8B 1 VERSN
REVDAT 2 27-NOV-01 1H8B 1 JRNL
REVDAT 1 30-AUG-01 1H8B 0
JRNL AUTH R.A.ATKINSON,C.JOSEPH,G.KELLY,F.W.MUSKETT,
JRNL AUTH 2 T.A.FRENKIEL,D.NIETLISPACH,A.PASTORE
JRNL TITL CA2+-INDEPENDENT BINDING OF AN EF-HAND DOMAIN TO A
JRNL TITL 2 NOVEL MOTIF IN THE ALPHA-ACTININ-TITIN COMPLEX
JRNL REF NAT.STRUCT.BIOL. V. 8 853 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11573089
JRNL DOI 10.1038/NSB1001-853
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.A.ATKINSON,C.JOSEPH,F.D.PIAZ,L.BIROLO,G.STIER,
REMARK 1 AUTH 2 P.PUCCI,A.PASTORE
REMARK 1 TITL THE BINDING OF ALPHA-ACTININ TO TITIN:
REMARK 1 TITL 2 IMPLICATIONS FOR Z-DISK ASSEMBLY
REMARK 1 REF BIOCHEMISTRY V. 39 5255 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 10819994
REMARK 1 DOI 10.1021/BI991891U
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: REFINEMENT DETAILS MAY BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL
REMARK 3 SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS
REMARK 3 PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE
REMARK 3 CONSTRAINTS FOR THESE TWO RESIDUES WHICH ARE OMITTED FROM THE
REMARK 3 STRUCTURE CALCULATION. THE FIRST RESIDUE OF THE NATURAL
REMARK 3 SEQUENCE OF TITIN ZR7 IS REPLACED BY A MET. THIS IS PRECEDED
REMARK 3 BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS
REMARK 3 FOR THE N-TERMINAL 8 RESIDUES AND THE C-TERMINAL 22 RESIDUES
REMARK 3 WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION.
REMARK 4
REMARK 4 1H8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-01.
REMARK 100 THE PDBE ID CODE IS EBI-5821.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.7 MM COMPLEX
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PUBLICATION
REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 600; 800
REMARK 210 SPECTROMETER MODEL : UNITYPLUS500; UNITY600;
REMARK 210 INOVA600; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, X-PLOR
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 CARTESIAN DYANMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING
REMARK 210 CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND
REMARK 210 F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C,
REMARK 210 15N-LABELLED SAMPLES IN WHICH ONLY ONE OF THE TWO
REMARK 210 COMPONENTS WAS LABELLED
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 CHAIN A ENGINEERED MUTATION THR822MET, MODIFIED FOR EXPRESSION
REMARK 400 F-ACTIN CROSS-LINKING PROTEIN IS INVOLVED IN ANCHORING OF
REMARK 400 ACTIN TO A VARIETY OF INTRACELLULAR STRUCTURES.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 ALA A -1
REMARK 465 GLY B -2
REMARK 465 ALA B -1
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LYS B 3
REMARK 465 VAL B 4
REMARK 465 GLY B 5
REMARK 465 VAL B 6
REMARK 465 GLU B 30
REMARK 465 PRO B 31
REMARK 465 GLY B 32
REMARK 465 LEU B 33
REMARK 465 PRO B 34
REMARK 465 GLU B 35
REMARK 465 ASP B 36
REMARK 465 SER B 37
REMARK 465 TYR B 38
REMARK 465 ALA B 39
REMARK 465 GLN B 40
REMARK 465 GLN B 41
REMARK 465 THR B 42
REMARK 465 THR B 43
REMARK 465 LEU B 44
REMARK 465 GLU B 45
REMARK 465 TYR B 46
REMARK 465 GLY B 47
REMARK 465 TYR B 48
REMARK 465 LYS B 49
REMARK 465 GLU B 50
REMARK 465 HIS B 51
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 ASP A 5 33.81 175.46
REMARK 500 1 THR A 6 -71.58 63.16
REMARK 500 1 SER A 19 69.18 67.00
REMARK 500 1 ARG A 44 -72.62 -64.11
REMARK 500 1 PRO A 46 -157.58 -59.55
REMARK 500 1 TYR A 48 -156.46 32.73
REMARK 500 1 SER A 53 -162.74 -53.71
REMARK 500 1 SER A 71 146.69 65.47
REMARK 500 1 PRO B 28 -163.74 -54.51
REMARK 500 2 ALA A 2 127.22 -173.15
REMARK 500 2 ASP A 5 170.36 176.60
REMARK 500 2 SER A 19 68.79 62.43
REMARK 500 2 ARG A 44 -68.50 -92.24
REMARK 500 2 MET A 45 109.60 -55.55
REMARK 500 2 PRO A 46 -159.11 -66.63
REMARK 500 2 TYR A 48 -177.93 -58.68
REMARK 500 2 SER A 53 -143.25 25.98
REMARK 500 2 ARG B 26 66.42 60.58
REMARK 500 3 ALA A 2 175.95 57.28
REMARK 500 3 ASP A 5 -179.72 173.58
REMARK 500 3 SER A 19 77.37 64.93
REMARK 500 3 ASP A 20 45.36 37.44
REMARK 500 3 PRO A 35 -38.95 -35.18
REMARK 500 3 ARG A 44 -73.42 -60.13
REMARK 500 3 SER A 53 -179.25 56.06
REMARK 500 3 GLU A 70 49.59 -155.65
REMARK 500 3 SER A 71 105.33 65.43
REMARK 500 3 PRO B 28 79.83 -62.45
REMARK 500 4 ASP A 5 -49.40 -144.51
REMARK 500 4 THR A 6 -61.50 66.19
REMARK 500 4 PRO A 46 -146.69 -85.24
REMARK 500 4 SER A 53 -152.07 -56.76
REMARK 500 4 VAL A 54 -168.12 -60.88
REMARK 500 4 SER A 71 -42.94 -148.00
REMARK 500 5 ASP A 3 -38.20 -160.38
REMARK 500 5 THR A 4 98.65 49.06
REMARK 500 5 SER A 19 60.43 68.65
REMARK 500 5 MET A 45 101.59 -36.04
REMARK 500 5 PRO A 46 -166.01 -68.37
REMARK 500 5 SER A 53 -177.72 56.60
REMARK 500 5 PRO B 28 92.34 -63.87
REMARK 500 6 ASP A 5 -172.18 48.32
REMARK 500 6 ARG A 44 -64.14 -94.32
REMARK 500 6 MET A 45 112.15 -30.00
REMARK 500 6 PRO A 46 -158.17 -81.77
REMARK 500 6 SER A 53 -142.52 40.68
REMARK 500 7 ALA A 2 23.14 -140.41
REMARK 500 7 THR A 6 -57.61 67.21
REMARK 500 7 SER A 19 64.45 65.09
REMARK 500 7 ARG A 44 -66.54 -105.13
REMARK 500 7 MET A 45 108.98 -26.35
REMARK 500 7 PRO A 46 -167.74 -79.29
REMARK 500 7 SER A 53 -172.92 47.14
REMARK 500 7 PRO B 28 -157.08 -61.99
REMARK 500 8 ASP A 3 -153.54 51.40
REMARK 500 8 ASP A 5 48.63 -155.99
REMARK 500 8 THR A 6 -66.60 65.09
REMARK 500 8 SER A 19 63.34 66.93
REMARK 500 8 PRO A 34 -149.39 -58.41
REMARK 500 8 MET A 45 100.37 -35.30
REMARK 500 8 PRO A 46 -168.09 -71.59
REMARK 500 8 TYR A 48 -177.54 -53.56
REMARK 500 8 SER A 53 -152.10 178.23
REMARK 500 8 SER A 71 -60.64 -174.11
REMARK 500 9 ALA A 2 -86.62 -146.65
REMARK 500 9 ASP A 3 -176.95 51.67
REMARK 500 9 THR A 6 -71.12 -108.54
REMARK 500 9 PRO A 35 -37.75 -38.07
REMARK 500 9 ARG A 44 -76.47 -69.11
REMARK 500 9 MET A 45 102.73 -39.42
REMARK 500 9 PRO A 46 -158.79 -59.80
REMARK 500 9 TYR A 48 166.76 -41.32
REMARK 500 9 SER A 53 139.03 -35.90
REMARK 500 9 SER A 71 -150.33 -79.99
REMARK 500 9 LYS B 8 -62.56 66.28
REMARK 500 9 ARG B 26 69.25 63.08
REMARK 500 10 ALA A 2 -81.29 -173.08
REMARK 500 10 ASP A 5 51.48 -173.45
REMARK 500 10 THR A 6 -68.36 64.59
REMARK 500 10 SER A 19 74.69 65.29
REMARK 500 10 MET A 45 94.52 -29.48
REMARK 500 10 PRO A 46 -174.60 -59.07
REMARK 500 10 TYR A 48 -118.66 42.60
REMARK 500 10 SER A 53 -178.63 55.81
REMARK 500 10 GLU A 70 -65.60 -131.64
REMARK 500 10 LYS B 8 -62.04 66.22
REMARK 500 11 ALA A 2 86.12 47.52
REMARK 500 11 THR A 6 -69.11 64.08
REMARK 500 11 SER A 19 66.27 67.37
REMARK 500 11 PRO A 35 -38.49 -39.60
REMARK 500 11 ARG A 44 -74.71 -63.70
REMARK 500 11 PRO A 46 -167.05 -78.36
REMARK 500 11 SER A 53 -178.61 54.38
REMARK 500 11 GLU A 70 176.46 53.87
REMARK 500 11 LYS B 8 -45.32 -149.45
REMARK 500 11 PRO B 28 -75.75 -46.28
REMARK 500 12 ALA A 2 -168.27 -59.05
REMARK 500 12 SER A 19 62.43 67.61
REMARK 500 12 MET A 45 90.99 -26.96
REMARK 500 12 PRO A 46 -166.50 -67.01
REMARK 500 12 TYR A 48 168.71 -43.53
REMARK 500 12 SER A 53 -156.20 39.19
REMARK 500 12 GLU A 70 -64.16 -157.69
REMARK 500 12 SER A 71 150.34 65.28
REMARK 500 12 LYS B 8 -64.74 65.77
REMARK 500 12 PRO B 28 175.78 -50.24
REMARK 500 13 ALA A 2 -47.00 -155.21
REMARK 500 13 ASP A 5 -68.97 -168.56
REMARK 500 13 THR A 6 -67.01 -149.17
REMARK 500 13 SER A 19 74.75 59.01
REMARK 500 13 MET A 45 103.57 -33.98
REMARK 500 13 PRO A 46 -146.30 -60.60
REMARK 500 13 TYR A 48 156.57 -41.70
REMARK 500 13 SER A 53 -160.16 -54.92
REMARK 500 13 GLU A 70 69.53 63.83
REMARK 500 14 ASP A 5 -79.76 -156.43
REMARK 500 14 THR A 6 -59.27 -132.51
REMARK 500 14 SER A 19 61.39 60.60
REMARK 500 14 MET A 45 118.10 -30.43
REMARK 500 14 PRO A 46 -157.56 -74.14
REMARK 500 14 TYR A 48 -160.81 36.40
REMARK 500 14 SER A 53 -171.50 -51.56
REMARK 500 15 ASP A 3 101.90 -171.60
REMARK 500 15 THR A 4 109.04 60.65
REMARK 500 15 ASP A 5 40.40 -109.96
REMARK 500 15 MET A 45 103.46 -34.39
REMARK 500 15 PRO A 46 -155.48 -60.91
REMARK 500 15 TYR A 48 -83.12 -56.46
REMARK 500 15 SER A 53 -157.53 -55.51
REMARK 500 15 SER A 71 -64.66 -126.39
REMARK 500 15 LYS B 8 -48.07 73.78
REMARK 500 16 ALA A 2 84.79 46.51
REMARK 500 16 THR A 4 176.55 -50.30
REMARK 500 16 SER A 19 76.14 65.28
REMARK 500 16 ARG A 44 -71.63 -76.72
REMARK 500 16 PRO A 46 -158.61 -75.50
REMARK 500 16 TYR A 48 79.35 -61.88
REMARK 500 16 SER A 53 -178.59 53.70
REMARK 500 16 GLU A 70 -44.32 -136.46
REMARK 500 16 LYS B 8 -29.64 -177.77
REMARK 500 17 ALA A 2 -77.19 -109.32
REMARK 500 17 ASP A 3 -160.41 -168.83
REMARK 500 17 SER A 19 80.30 60.27
REMARK 500 17 ARG A 44 -67.92 -93.65
REMARK 500 17 MET A 45 105.44 -36.62
REMARK 500 17 PRO A 46 -158.79 -71.57
REMARK 500 17 SER A 53 -179.65 52.87
REMARK 500 17 SER A 71 95.89 -172.23
REMARK 500 17 LYS B 8 34.33 -174.52
REMARK 500 18 THR A 4 -146.38 -103.84
REMARK 500 18 ASP A 5 -84.89 -96.22
REMARK 500 18 THR A 6 -43.55 -156.60
REMARK 500 18 SER A 19 66.80 64.91
REMARK 500 18 MET A 45 111.10 -32.88
REMARK 500 18 TYR A 48 107.80 -59.23
REMARK 500 18 SER A 53 -163.83 178.37
REMARK 500 18 GLU A 70 -54.99 -166.85
REMARK 500 18 LYS B 8 37.04 -158.28
REMARK 500 18 PRO B 28 100.70 -43.71
REMARK 500 19 ASP A 5 154.12 62.21
REMARK 500 19 THR A 6 -59.88 66.62
REMARK 500 19 MET A 45 116.78 -32.04
REMARK 500 19 PRO A 46 -149.64 -87.83
REMARK 500 19 SER A 53 -162.55 -54.22
REMARK 500 19 GLU A 70 -169.09 -68.27
REMARK 500 19 ARG B 26 70.87 67.88
REMARK 500 20 ASP A 5 -160.51 -178.42
REMARK 500 20 SER A 19 67.44 68.07
REMARK 500 20 MET A 45 119.27 -38.29
REMARK 500 20 SER A 53 -159.82 -54.87
REMARK 500 21 ASP A 5 -166.41 53.21
REMARK 500 21 SER A 19 64.92 68.28
REMARK 500 21 ARG A 44 -75.66 -65.79
REMARK 500 21 MET A 45 108.58 -53.02
REMARK 500 21 PRO A 46 -147.17 -68.95
REMARK 500 21 SER A 53 -163.93 -53.63
REMARK 500 21 SER A 71 -164.70 -167.36
REMARK 500 21 LYS B 8 -65.59 -103.60
REMARK 500 22 THR A 6 -66.53 -108.78
REMARK 500 22 SER A 19 72.25 68.05
REMARK 500 22 ARG A 44 -72.83 -100.35
REMARK 500 22 PRO A 46 -170.33 -52.51
REMARK 500 22 TYR A 48 174.68 179.30
REMARK 500 22 SER A 53 139.50 -37.83
REMARK 500 22 SER A 71 -85.04 -163.25
REMARK 500 22 PRO B 28 69.12 -63.77
REMARK 500 23 ALA A 2 -105.63 56.84
REMARK 500 23 ASP A 3 122.02 59.20
REMARK 500 23 ASP A 5 48.36 -169.44
REMARK 500 23 THR A 6 -71.57 63.19
REMARK 500 23 SER A 19 63.87 68.71
REMARK 500 23 MET A 45 114.92 -29.91
REMARK 500 23 PRO A 46 -158.65 -94.18
REMARK 500 23 SER A 53 -166.56 130.91
REMARK 500 23 GLU A 70 -168.47 -129.33
REMARK 500 23 SER A 71 149.65 61.03
REMARK 500 23 LYS B 8 -59.68 66.85
REMARK 500 23 PRO B 28 80.28 -65.20
REMARK 500 24 ALA A 2 -179.51 53.49
REMARK 500 24 THR A 4 -152.83 37.97
REMARK 500 24 ASP A 20 64.66 63.96
REMARK 500 24 PRO A 35 -39.01 -39.92
REMARK 500 24 ILE A 42 -19.30 -47.10
REMARK 500 24 ARG A 44 -69.91 -95.79
REMARK 500 24 MET A 45 84.13 -14.99
REMARK 500 24 SER A 53 -153.33 -55.99
REMARK 500 24 LYS B 8 -74.39 62.05
REMARK 500 25 ASP A 3 119.92 -164.35
REMARK 500 25 SER A 19 64.30 68.38
REMARK 500 25 PRO A 34 171.21 -46.25
REMARK 500 25 MET A 45 96.77 -34.62
REMARK 500 25 PRO A 46 -153.79 -59.08
REMARK 500 25 SER A 53 -157.11 -55.02
REMARK 500 25 GLU A 70 95.63 -171.95
REMARK 500 25 LYS B 8 33.35 -173.36
REMARK 500 26 ALA A 2 -149.83 -165.12
REMARK 500 26 THR A 4 74.00 43.48
REMARK 500 26 ASP A 5 -72.42 -123.91
REMARK 500 26 THR A 6 -63.36 66.03
REMARK 500 26 SER A 19 70.58 57.73
REMARK 500 26 PRO A 34 167.11 -46.45
REMARK 500 26 MET A 45 103.32 -28.00
REMARK 500 26 PRO A 46 -160.58 -57.03
REMARK 500 26 ALA A 47 49.52 -98.35
REMARK 500 26 TYR A 48 177.58 49.63
REMARK 500 26 SER A 53 -156.86 -55.61
REMARK 500 26 VAL A 54 -160.09 -76.73
REMARK 500 26 SER A 71 107.41 178.90
REMARK 500 27 ALA A 2 -143.25 -130.10
REMARK 500 27 THR A 4 -144.23 -100.11
REMARK 500 27 ASP A 5 -168.72 66.60
REMARK 500 27 SER A 19 64.59 66.32
REMARK 500 27 MET A 45 118.14 -36.28
REMARK 500 27 PRO A 46 -154.66 -70.21
REMARK 500 27 SER A 53 139.91 -36.22
REMARK 500 27 SER A 71 -76.40 -128.00
REMARK 500 27 PRO B 28 71.60 -0.68
REMARK 500 28 ASP A 3 82.35 -171.21
REMARK 500 28 PRO A 35 -35.23 -39.24
REMARK 500 28 MET A 45 111.12 -39.44
REMARK 500 28 PRO A 46 -155.68 -67.20
REMARK 500 28 SER A 53 -161.75 -54.39
REMARK 500 28 LYS B 8 50.52 -94.10
REMARK 500 28 ARG B 26 -87.55 -87.78
REMARK 500 29 ALA A 2 -168.01 -129.71
REMARK 500 29 ASP A 3 -61.43 -147.78
REMARK 500 29 THR A 6 -58.46 67.07
REMARK 500 29 ASP A 20 65.02 65.82
REMARK 500 29 ARG A 44 -73.93 -64.11
REMARK 500 29 MET A 45 117.21 -38.47
REMARK 500 29 PRO A 46 -154.47 -72.39
REMARK 500 29 SER A 53 169.63 49.78
REMARK 500 29 LYS B 8 -63.95 66.29
REMARK 500 30 ALA A 2 73.56 -172.08
REMARK 500 30 ASP A 3 66.53 -160.86
REMARK 500 30 THR A 4 111.15 58.29
REMARK 500 30 PRO A 34 172.28 -55.00
REMARK 500 30 PRO A 46 -157.64 -63.37
REMARK 500 30 TYR A 48 -39.93 -39.24
REMARK 500 30 SER A 53 -159.93 -54.51
REMARK 500 30 LYS B 8 40.23 -164.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
DBREF 1H8B A -2 -1 PDB 1H8B 1H8B -2 -1
DBREF 1H8B A 1 73 UNP P35609 AAC2_HUMAN 822 894
DBREF 1H8B B -2 -1 PDB 1H8B 1H8B -2 -1
DBREF 1H8B B 1 51 UNP O97791 O97791 648 698
SEQADV 1H8B MET A 1 UNP P35609 THR 822 ENGINEERED MUTATION
SEQADV 1H8B MET B 1 UNP O97791 HIS 848 ENGINEERED MUTATION
SEQRES 1 A 75 GLY ALA MET ALA ASP THR ASP THR ALA GLU GLN VAL ILE
SEQRES 2 A 75 ALA SER PHE ARG ILE LEU ALA SER ASP LYS PRO TYR ILE
SEQRES 3 A 75 LEU ALA GLU GLU LEU ARG ARG GLU LEU PRO PRO ASP GLN
SEQRES 4 A 75 ALA GLN TYR CYS ILE LYS ARG MET PRO ALA TYR SER GLY
SEQRES 5 A 75 PRO GLY SER VAL PRO GLY ALA LEU ASP TYR ALA ALA PHE
SEQRES 6 A 75 SER SER ALA LEU TYR GLY GLU SER ASP LEU
SEQRES 1 B 53 GLY ALA MET GLY LYS VAL GLY VAL GLY LYS LYS ALA GLU
SEQRES 2 B 53 ALA VAL ALA THR VAL VAL ALA ALA VAL ASP GLN ALA ARG
SEQRES 3 B 53 VAL ARG GLU PRO ARG GLU PRO GLY LEU PRO GLU ASP SER
SEQRES 4 B 53 TYR ALA GLN GLN THR THR LEU GLU TYR GLY TYR LYS GLU
SEQRES 5 B 53 HIS
HELIX 1 H1 ALA A 7 ALA A 18 1 12
HELIX 2 H2 ALA A 26 GLU A 32 1 7
HELIX 3 H3 PRO A 35 ARG A 44 1 10
HELIX 4 H4 TYR A 60 TYR A 68 1 9
HELIX 5 H5 LYS B 8 ARG B 26 1 19
SHEET 1 S1 1 TYR A 23 LEU A 25 0
SHEET 2 S2 1 ALA A 57 ASP A 59 0
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