Header list of 1oh1.pdb file
Complete list - r 25 2 Bytes
HEADER CYSTEINE PROTEINASE INHIBITOR 21-MAY-03 1OH1
TITLE SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS
TITLE 2 AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE
TITLE 3 PROTEINASE INHIBITORS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAPHOSTATIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-107;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN SAV1910;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: DISULPHIDE BRIDGE BETWEEN C16 AND C55
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 STRAIN: V8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-5T
KEYWDS CYSTEINE PROTEINASE INHIBITOR, CYSTEINE PROTEASE INHIBITOR,
KEYWDS 2 STAPHOPAIN INHIBITOR, NOT SIMILAR TO CYSTATINS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.DUBIN,G.POPOWICZ,M.KRAJEWSKI,J.STEC,M.BOCHTLER,J.POTEMPA,
AUTHOR 2 A.DUBIN,T.A.HOLAK
REVDAT 2 24-FEB-09 1OH1 1 VERSN
REVDAT 1 20-NOV-03 1OH1 0
JRNL AUTH G.DUBIN,M.KRAJEWSKI,G.POPOWICZ,J.STEC-NIEMCZYK,
JRNL AUTH 2 M.BOCHTLER,J.POTEMPA,A.DUBIN,T.A.HOLAK
JRNL TITL A NOVEL CLASS OF CYSTEINE PROTEASE INHIBITORS:
JRNL TITL 2 SOLUTION STRUCTURE OF STAPHOSTATIN A FROM
JRNL TITL 3 STAPHYLOCOCCUS AUREUS
JRNL REF BIOCHEMISTRY V. 42 13449 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14621990
JRNL DOI 10.1021/BI035310J
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.RZYCHON,A.SABAT,K.KOSOWSKA,J.POTEMPA,A.DUBIN
REMARK 1 TITL STAPHOSTATINS: AN EXPANDING NEW GROUP OF
REMARK 1 TITL 2 PROTEINASE INHIBITORS WITH A UNIQUE SPECIFICITY
REMARK 1 TITL 3 FOR THE REGULATION OF STAPHOPAINS, STAPHYLOCOCCUS
REMARK 1 TITL 4 SPP. CYSTEINE PROTEINASES
REMARK 1 REF MOL.MICROBIOL. V. 49 1051 2003
REMARK 1 REFN ISSN 0950-382X
REMARK 1 PMID 12890028
REMARK 1 DOI 10.1046/J.1365-2958.2003.03613.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,
REMARK 3 RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OH1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAY-03.
REMARK 100 THE PDBE ID CODE IS EBI-12767.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 150 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; HSQC; HNHA;
REMARK 210 HNCA; HBHACOHN
REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 600; 750
REMARK 210 SPECTROMETER MODEL : AMX500; DRX600; DMX 750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS
REMARK 210 METHOD USED : SIMMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : FINAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 109 CB
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 22 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 PHE A 6 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 3 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 TYR A 22 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 6 TYR A 57 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 7 TYR A 23 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 13 TYR A 57 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 15 TYR A 22 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 17 TYR A 22 CB - CG - CD2 ANGL. DEV. = -4.0 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 MET A 3 -40.77 -179.54
REMARK 500 1 GLU A 4 76.38 -68.92
REMARK 500 1 GLN A 5 96.32 -173.85
REMARK 500 1 PHE A 6 76.91 63.98
REMARK 500 1 LYS A 15 -50.51 127.13
REMARK 500 1 CYS A 16 -163.05 57.71
REMARK 500 1 ASN A 17 -56.79 -137.72
REMARK 500 1 SER A 18 -157.15 -113.34
REMARK 500 1 GLU A 19 125.91 59.81
REMARK 500 1 ALA A 20 -90.84 -168.12
REMARK 500 1 LYS A 21 -79.20 -50.72
REMARK 500 1 ILE A 26 -52.21 -121.10
REMARK 500 1 HIS A 32 125.51 65.66
REMARK 500 1 ASP A 35 27.93 -78.51
REMARK 500 1 LEU A 36 85.78 -173.22
REMARK 500 1 ASP A 38 29.90 46.51
REMARK 500 1 PRO A 40 -157.10 -77.45
REMARK 500 1 SER A 46 167.00 59.64
REMARK 500 1 THR A 47 -88.22 54.29
REMARK 500 1 ASP A 49 -37.61 64.40
REMARK 500 1 ASP A 50 92.24 -168.00
REMARK 500 1 CYS A 55 97.52 -67.40
REMARK 500 1 LYS A 56 -75.85 -64.21
REMARK 500 1 THR A 60 14.10 -65.35
REMARK 500 1 GLU A 61 -80.44 -73.17
REMARK 500 1 LYS A 63 50.23 35.03
REMARK 500 1 ASN A 72 -67.70 -145.63
REMARK 500 1 SER A 73 -59.33 -178.79
REMARK 500 1 SER A 74 69.94 -166.74
REMARK 500 1 PRO A 82 -100.13 -87.10
REMARK 500 1 ASN A 83 -158.48 177.88
REMARK 500 1 ASN A 85 87.42 57.33
REMARK 500 1 LYS A 86 132.30 -171.18
REMARK 500 1 ALA A 96 -150.07 -165.69
REMARK 500 1 THR A 99 55.35 38.43
REMARK 500 1 SER A 100 -59.53 -136.59
REMARK 500 1 PRO A 101 -77.80 -69.43
REMARK 500 1 ARG A 102 107.74 58.00
REMARK 500 1 LYS A 107 77.19 -68.95
REMARK 500 2 SER A 2 -85.69 -156.63
REMARK 500 2 PHE A 6 98.46 176.34
REMARK 500 2 ASP A 12 3.96 -51.54
REMARK 500 2 LYS A 13 77.93 51.32
REMARK 500 2 PHE A 14 -115.63 -119.05
REMARK 500 2 LYS A 15 -47.43 173.01
REMARK 500 2 CYS A 16 -156.14 69.89
REMARK 500 2 SER A 18 -46.59 65.33
REMARK 500 2 ALA A 20 -91.04 -174.20
REMARK 500 2 LYS A 21 -82.98 -46.17
REMARK 500 2 HIS A 32 145.92 65.23
REMARK 500 2 ASP A 35 39.09 -92.36
REMARK 500 2 LEU A 36 82.74 -161.81
REMARK 500 2 ASN A 37 -32.95 64.66
REMARK 500 2 ASP A 38 77.17 78.95
REMARK 500 2 SER A 39 11.75 -152.67
REMARK 500 2 PRO A 40 -142.12 -78.47
REMARK 500 2 SER A 46 179.38 72.83
REMARK 500 2 THR A 47 -107.90 68.23
REMARK 500 2 SER A 48 58.47 29.12
REMARK 500 2 ASP A 49 -78.62 63.75
REMARK 500 2 SER A 51 170.90 57.86
REMARK 500 2 ASP A 52 -36.43 -130.95
REMARK 500 2 LYS A 56 -78.92 -80.99
REMARK 500 2 THR A 60 78.58 -66.55
REMARK 500 2 GLU A 61 -42.93 -162.76
REMARK 500 2 LYS A 63 56.39 19.86
REMARK 500 2 LYS A 70 65.20 -100.31
REMARK 500 2 ASN A 71 -57.90 -125.91
REMARK 500 2 ASN A 72 -76.90 -71.43
REMARK 500 2 SER A 73 -50.90 -174.06
REMARK 500 2 SER A 74 56.49 -149.50
REMARK 500 2 PRO A 82 -103.09 -88.73
REMARK 500 2 ASN A 83 -165.15 -177.89
REMARK 500 2 ALA A 96 -145.73 -163.25
REMARK 500 2 SER A 100 -38.79 -167.52
REMARK 500 3 GLU A 4 68.43 67.55
REMARK 500 3 GLN A 5 93.29 -164.79
REMARK 500 3 PHE A 6 78.40 63.04
REMARK 500 3 PHE A 14 -92.52 -132.96
REMARK 500 3 CYS A 16 97.44 75.95
REMARK 500 3 GLU A 19 119.22 65.29
REMARK 500 3 ALA A 20 -93.00 -172.87
REMARK 500 3 LYS A 21 -75.79 -55.82
REMARK 500 3 HIS A 32 145.96 69.60
REMARK 500 3 GLN A 34 57.29 -109.17
REMARK 500 3 LEU A 36 76.34 -165.78
REMARK 500 3 ASN A 37 -29.20 64.72
REMARK 500 3 ASP A 38 100.17 81.14
REMARK 500 3 SER A 39 40.27 -157.08
REMARK 500 3 PRO A 40 -148.66 -88.70
REMARK 500 3 SER A 46 -148.85 55.85
REMARK 500 3 THR A 47 -155.61 60.41
REMARK 500 3 ASP A 49 -86.62 61.40
REMARK 500 3 SER A 51 175.55 58.79
REMARK 500 3 ASN A 72 -82.91 -111.49
REMARK 500 3 SER A 73 -67.21 -142.83
REMARK 500 3 SER A 74 85.49 -172.05
REMARK 500 3 PRO A 82 -88.00 -90.30
REMARK 500 3 ASN A 83 -151.86 174.92
REMARK 500 3 ALA A 96 -149.22 -171.88
REMARK 500 3 THR A 99 83.85 38.86
REMARK 500 3 SER A 100 -66.78 -163.34
REMARK 500 3 ARG A 102 119.56 61.06
REMARK 500 3 LYS A 107 87.44 -67.84
REMARK 500 4 GLN A 5 117.14 -169.12
REMARK 500 4 PHE A 6 88.76 62.42
REMARK 500 4 PHE A 14 -102.22 -134.00
REMARK 500 4 LYS A 15 -57.15 -176.84
REMARK 500 4 ASN A 17 -90.16 68.68
REMARK 500 4 SER A 18 -153.86 -88.48
REMARK 500 4 GLU A 19 135.47 66.20
REMARK 500 4 ALA A 20 -88.39 -179.68
REMARK 500 4 LYS A 21 -77.86 -56.36
REMARK 500 4 TYR A 23 -70.39 -57.98
REMARK 500 4 HIS A 32 141.53 65.44
REMARK 500 4 PRO A 33 -81.73 -57.55
REMARK 500 4 GLN A 34 6.74 -150.78
REMARK 500 4 ASP A 35 44.01 -91.14
REMARK 500 4 LEU A 36 46.96 -152.33
REMARK 500 4 PRO A 40 -175.72 -66.93
REMARK 500 4 SER A 46 168.36 71.26
REMARK 500 4 ASP A 49 44.76 -89.09
REMARK 500 4 SER A 51 169.41 65.39
REMARK 500 4 TYR A 57 155.41 179.40
REMARK 500 4 HIS A 62 47.91 -166.64
REMARK 500 4 SER A 73 -71.87 -177.54
REMARK 500 4 SER A 74 62.16 -159.39
REMARK 500 4 PRO A 82 -96.91 -84.13
REMARK 500 4 ASN A 83 -160.86 168.90
REMARK 500 4 ALA A 96 -151.51 -166.63
REMARK 500 4 THR A 99 68.82 -64.82
REMARK 500 4 SER A 100 -41.54 -170.17
REMARK 500 5 MET A 3 64.77 -116.37
REMARK 500 5 PHE A 6 101.53 167.03
REMARK 500 5 PHE A 14 -88.32 -126.07
REMARK 500 5 CYS A 16 106.59 -166.65
REMARK 500 5 SER A 18 -70.81 65.11
REMARK 500 5 ALA A 20 -90.34 -174.94
REMARK 500 5 LYS A 21 -77.74 -52.98
REMARK 500 5 HIS A 32 146.50 78.09
REMARK 500 5 PRO A 33 -166.29 -68.50
REMARK 500 5 ASP A 35 30.46 -78.28
REMARK 500 5 LEU A 36 77.73 -175.41
REMARK 500 5 ASN A 37 8.53 58.56
REMARK 500 5 ASP A 38 72.22 55.22
REMARK 500 5 SER A 39 50.58 -142.82
REMARK 500 5 PRO A 40 -161.09 -79.82
REMARK 500 5 SER A 46 169.04 63.65
REMARK 500 5 THR A 47 53.56 -155.69
REMARK 500 5 SER A 48 -87.14 55.14
REMARK 500 5 ASP A 50 92.00 -163.84
REMARK 500 5 GLU A 61 -83.13 -151.46
REMARK 500 5 HIS A 62 37.41 -85.66
REMARK 500 5 LYS A 63 53.40 31.19
REMARK 500 5 SER A 73 -83.61 -169.55
REMARK 500 5 SER A 74 84.98 -169.91
REMARK 500 5 PRO A 82 -94.36 -76.77
REMARK 500 5 ASN A 83 -153.29 160.60
REMARK 500 5 ASN A 85 73.69 57.34
REMARK 500 5 THR A 94 -93.84 -0.99
REMARK 500 5 ALA A 96 -166.20 -127.39
REMARK 500 5 SER A 100 -49.26 -136.17
REMARK 500 5 PRO A 101 -71.52 -63.28
REMARK 500 5 ARG A 102 86.53 34.95
REMARK 500 5 LYS A 107 81.04 -69.89
REMARK 500 6 PHE A 6 104.14 171.45
REMARK 500 6 LYS A 15 -156.60 -173.09
REMARK 500 6 CYS A 16 90.01 65.99
REMARK 500 6 SER A 18 -117.79 -59.85
REMARK 500 6 ALA A 20 -89.85 -147.27
REMARK 500 6 PRO A 33 46.98 -77.75
REMARK 500 6 GLN A 34 27.55 -156.25
REMARK 500 6 LEU A 36 44.21 32.21
REMARK 500 6 ASN A 37 -31.92 174.19
REMARK 500 6 ASP A 38 76.94 76.33
REMARK 500 6 PRO A 40 -158.87 -83.05
REMARK 500 6 SER A 46 -135.60 58.57
REMARK 500 6 THR A 47 168.25 63.37
REMARK 500 6 ASP A 49 -67.75 60.48
REMARK 500 6 SER A 51 -156.26 45.91
REMARK 500 6 THR A 60 -113.71 -58.29
REMARK 500 6 HIS A 62 18.13 57.54
REMARK 500 6 LYS A 63 57.48 115.08
REMARK 500 6 ASN A 72 -93.71 -108.12
REMARK 500 6 SER A 73 80.19 -161.48
REMARK 500 6 PRO A 82 -91.87 -76.23
REMARK 500 6 ASN A 83 -156.85 164.82
REMARK 500 6 ALA A 96 -169.93 -169.88
REMARK 500 6 PRO A 101 -138.68 -67.61
REMARK 500 6 ARG A 102 63.45 69.50
REMARK 500 6 LYS A 107 41.41 -80.86
REMARK 500 7 SER A 2 94.75 65.26
REMARK 500 7 MET A 3 -78.84 61.14
REMARK 500 7 GLN A 5 86.83 56.00
REMARK 500 7 PHE A 6 77.64 71.00
REMARK 500 7 PHE A 14 -93.34 -118.00
REMARK 500 7 LYS A 15 -92.91 -102.63
REMARK 500 7 CYS A 16 -60.08 60.68
REMARK 500 7 ASN A 17 162.53 65.16
REMARK 500 7 SER A 18 -71.41 66.25
REMARK 500 7 ALA A 20 -81.78 -178.92
REMARK 500 7 LYS A 21 -77.10 -57.71
REMARK 500 7 PRO A 33 -95.98 -69.32
REMARK 500 7 ASP A 35 127.65 -178.17
REMARK 500 7 LEU A 36 54.90 -168.94
REMARK 500 7 PRO A 40 -162.55 -77.47
REMARK 500 7 SER A 46 -142.92 61.95
REMARK 500 7 THR A 47 110.27 66.56
REMARK 500 7 SER A 48 107.27 59.95
REMARK 500 7 ASP A 50 73.48 67.55
REMARK 500 7 THR A 60 78.99 -67.70
REMARK 500 7 GLU A 61 -96.20 -126.42
REMARK 500 7 LYS A 63 95.15 109.47
REMARK 500 7 ASN A 72 -92.11 -111.70
REMARK 500 7 SER A 73 80.56 -170.75
REMARK 500 7 PRO A 82 -91.67 -97.99
REMARK 500 7 ASN A 83 -159.74 178.38
REMARK 500 7 ASP A 84 28.46 47.24
REMARK 500 7 ASN A 85 85.31 55.36
REMARK 500 7 GLU A 95 31.41 -82.26
REMARK 500 7 ALA A 96 -160.82 -177.06
REMARK 500 7 SER A 100 91.18 -165.90
REMARK 500 7 ARG A 102 78.13 49.01
REMARK 500 7 LYS A 107 74.05 -66.36
REMARK 500 8 GLU A 4 177.00 52.25
REMARK 500 8 GLN A 5 77.43 50.88
REMARK 500 8 PHE A 6 79.59 67.27
REMARK 500 8 LYS A 15 73.67 54.68
REMARK 500 8 ASN A 17 -131.38 175.70
REMARK 500 8 SER A 18 164.81 -45.33
REMARK 500 8 GLU A 19 138.45 69.50
REMARK 500 8 ALA A 20 -87.37 165.93
REMARK 500 8 LYS A 21 -80.24 -47.01
REMARK 500 8 HIS A 32 153.39 105.52
REMARK 500 8 PRO A 33 21.98 -73.34
REMARK 500 8 GLN A 34 14.79 54.49
REMARK 500 8 ASP A 35 33.43 -83.86
REMARK 500 8 LEU A 36 71.74 -159.89
REMARK 500 8 ASN A 37 28.17 42.25
REMARK 500 8 PRO A 40 -135.09 -97.48
REMARK 500 8 SER A 46 154.43 64.25
REMARK 500 8 SER A 48 -55.38 66.93
REMARK 500 8 ASP A 50 91.21 55.59
REMARK 500 8 TYR A 57 148.70 -170.82
REMARK 500 8 THR A 60 29.42 -65.44
REMARK 500 8 HIS A 62 29.72 -163.57
REMARK 500 8 LYS A 63 84.16 100.70
REMARK 500 8 ASN A 72 -92.55 -136.01
REMARK 500 8 SER A 73 75.54 -167.71
REMARK 500 8 PRO A 82 -97.93 -97.05
REMARK 500 8 ASN A 83 -155.09 179.69
REMARK 500 8 GLU A 95 49.63 -143.60
REMARK 500 8 ALA A 96 -157.69 -142.66
REMARK 500 8 THR A 99 94.07 60.11
REMARK 500 8 SER A 100 86.69 -156.06
REMARK 500 8 PRO A 101 -104.52 -97.93
REMARK 500 8 LYS A 107 89.99 -68.39
REMARK 500 9 SER A 2 -81.63 -170.59
REMARK 500 9 GLU A 4 86.46 55.83
REMARK 500 9 GLN A 5 92.82 -171.39
REMARK 500 9 PHE A 6 81.23 54.60
REMARK 500 9 LYS A 13 -24.17 76.31
REMARK 500 9 PHE A 14 -0.88 -56.41
REMARK 500 9 LYS A 15 98.55 19.46
REMARK 500 9 CYS A 16 -77.49 -50.89
REMARK 500 9 ASN A 17 74.64 -175.50
REMARK 500 9 SER A 18 -69.33 148.31
REMARK 500 9 ALA A 20 -80.08 -162.31
REMARK 500 9 LYS A 21 -78.28 -50.69
REMARK 500 9 HIS A 32 135.34 59.91
REMARK 500 9 PRO A 33 40.62 -73.69
REMARK 500 9 GLN A 34 -5.25 55.80
REMARK 500 9 LEU A 36 76.59 -172.91
REMARK 500 9 ASN A 37 28.83 49.16
REMARK 500 9 PRO A 40 -148.37 -86.40
REMARK 500 9 SER A 46 161.30 75.76
REMARK 500 9 THR A 47 -104.89 -121.56
REMARK 500 9 SER A 48 -52.72 -166.78
REMARK 500 9 ASP A 49 -84.42 -67.08
REMARK 500 9 ASP A 50 40.41 -153.19
REMARK 500 9 SER A 51 178.79 56.14
REMARK 500 9 GLU A 61 -65.65 -155.93
REMARK 500 9 SER A 73 -70.38 177.20
REMARK 500 9 SER A 74 58.15 -155.44
REMARK 500 9 PRO A 82 -96.44 -79.61
REMARK 500 9 ASN A 83 -128.12 171.20
REMARK 500 9 ASP A 84 81.57 2.72
REMARK 500 9 ASN A 85 68.21 25.37
REMARK 500 9 GLU A 95 57.86 -106.26
REMARK 500 9 SER A 100 -28.70 -162.08
REMARK 500 9 PRO A 101 -108.10 -77.80
REMARK 500 9 ARG A 102 78.82 55.31
REMARK 500 10 SER A 2 17.30 58.38
REMARK 500 10 GLN A 5 89.91 73.16
REMARK 500 10 PHE A 6 96.39 143.28
REMARK 500 10 LYS A 15 75.44 32.29
REMARK 500 10 ASN A 17 -104.20 58.39
REMARK 500 10 GLU A 19 120.58 61.51
REMARK 500 10 ALA A 20 -80.22 176.62
REMARK 500 10 LYS A 21 -77.00 -52.11
REMARK 500 10 HIS A 32 163.84 63.27
REMARK 500 10 GLN A 34 44.15 -102.26
REMARK 500 10 LEU A 36 88.23 -171.59
REMARK 500 10 ASN A 37 -30.40 65.13
REMARK 500 10 ASP A 38 53.13 82.00
REMARK 500 10 PRO A 40 -125.62 -91.84
REMARK 500 10 THR A 47 -99.52 -162.53
REMARK 500 10 ASP A 49 14.60 -60.12
REMARK 500 10 ASP A 50 21.69 49.29
REMARK 500 10 SER A 51 -145.29 51.71
REMARK 500 10 THR A 60 39.64 -73.71
REMARK 500 10 GLU A 61 -55.61 -126.36
REMARK 500 10 HIS A 62 40.01 -106.94
REMARK 500 10 LYS A 63 45.81 33.47
REMARK 500 10 SER A 73 -66.01 178.99
REMARK 500 10 SER A 74 88.21 -172.57
REMARK 500 10 PRO A 82 -94.76 -83.56
REMARK 500 10 ASN A 83 -156.69 174.32
REMARK 500 10 ASN A 85 72.52 42.55
REMARK 500 10 ALA A 96 -127.03 -119.75
REMARK 500 10 PRO A 101 -75.28 -72.05
REMARK 500 10 ARG A 102 136.62 59.71
REMARK 500 11 SER A 2 77.58 52.90
REMARK 500 11 MET A 3 111.15 -160.15
REMARK 500 11 GLU A 4 157.08 60.15
REMARK 500 11 PHE A 6 92.00 124.75
REMARK 500 11 ASP A 12 10.01 -63.08
REMARK 500 11 LYS A 13 -13.76 62.57
REMARK 500 11 LYS A 15 -133.47 59.46
REMARK 500 11 CYS A 16 -63.60 -138.18
REMARK 500 11 ASN A 17 -79.37 -173.97
REMARK 500 11 ALA A 20 -85.39 -174.41
REMARK 500 11 LYS A 21 -75.56 -56.14
REMARK 500 11 HIS A 32 142.52 126.52
REMARK 500 11 PRO A 33 49.94 -74.71
REMARK 500 11 LEU A 36 85.84 -177.99
REMARK 500 11 ASN A 37 16.24 51.45
REMARK 500 11 PRO A 40 -156.44 -79.79
REMARK 500 11 SER A 46 -154.52 68.61
REMARK 500 11 THR A 47 -152.88 66.10
REMARK 500 11 ASP A 49 -39.32 64.62
REMARK 500 11 ASP A 50 32.14 -155.49
REMARK 500 11 SER A 51 170.13 59.56
REMARK 500 11 TYR A 57 166.31 177.49
REMARK 500 11 THR A 60 32.97 -72.45
REMARK 500 11 PRO A 82 -99.45 -80.69
REMARK 500 11 ASN A 83 -162.24 167.88
REMARK 500 11 ALA A 96 -150.59 -176.80
REMARK 500 11 SER A 100 -47.41 -175.68
REMARK 500 12 SER A 2 77.58 52.90
REMARK 500 12 MET A 3 111.15 -160.15
REMARK 500 12 GLU A 4 157.08 60.15
REMARK 500 12 PHE A 6 92.00 124.75
REMARK 500 12 ASP A 12 10.01 -63.08
REMARK 500 12 LYS A 13 -13.76 62.57
REMARK 500 12 LYS A 15 -133.47 59.46
REMARK 500 12 CYS A 16 -63.60 -138.18
REMARK 500 12 ASN A 17 -79.37 -173.97
REMARK 500 12 ALA A 20 -85.39 -174.41
REMARK 500 12 LYS A 21 -75.56 -56.14
REMARK 500 12 HIS A 32 142.52 126.52
REMARK 500 12 PRO A 33 49.94 -74.71
REMARK 500 12 LEU A 36 85.84 -177.99
REMARK 500 12 ASN A 37 16.24 51.45
REMARK 500 12 PRO A 40 -156.44 -79.79
REMARK 500 12 SER A 46 -154.52 68.61
REMARK 500 12 THR A 47 -152.88 66.10
REMARK 500 12 ASP A 49 -39.32 64.62
REMARK 500 12 ASP A 50 32.14 -155.49
REMARK 500 12 SER A 51 170.13 59.56
REMARK 500 12 TYR A 57 166.31 177.49
REMARK 500 12 THR A 60 32.97 -72.45
REMARK 500 12 PRO A 82 -99.45 -80.69
REMARK 500 12 ASN A 83 -162.24 167.88
REMARK 500 12 ALA A 96 -150.59 -176.80
REMARK 500 12 SER A 100 -47.41 -175.68
REMARK 500 13 GLU A 4 -166.31 57.70
REMARK 500 13 PHE A 6 91.36 170.54
REMARK 500 13 PHE A 14 -107.48 -126.68
REMARK 500 13 LYS A 15 116.15 -166.11
REMARK 500 13 ASN A 17 -93.52 179.24
REMARK 500 13 GLU A 19 115.74 54.50
REMARK 500 13 ALA A 20 -88.52 -162.89
REMARK 500 13 LYS A 21 -74.65 -56.95
REMARK 500 13 PRO A 33 -88.05 -57.94
REMARK 500 13 ASP A 35 70.01 50.86
REMARK 500 13 SER A 39 49.80 -166.17
REMARK 500 13 PRO A 40 -156.76 -80.63
REMARK 500 13 SER A 46 153.97 65.74
REMARK 500 13 ASP A 49 79.02 -112.14
REMARK 500 13 SER A 51 166.22 54.13
REMARK 500 13 THR A 60 18.19 -65.88
REMARK 500 13 HIS A 62 28.34 -170.77
REMARK 500 13 LYS A 63 89.03 103.88
REMARK 500 13 ASN A 72 -90.58 -120.29
REMARK 500 13 SER A 73 68.92 -171.57
REMARK 500 13 PRO A 82 -93.37 -87.09
REMARK 500 13 ASN A 83 -154.51 167.90
REMARK 500 13 ASN A 85 78.28 42.22
REMARK 500 13 ARG A 102 100.18 59.78
REMARK 500 14 SER A 2 113.00 60.25
REMARK 500 14 GLU A 4 -168.19 62.20
REMARK 500 14 GLN A 5 82.53 56.96
REMARK 500 14 PHE A 6 98.80 82.57
REMARK 500 14 ASP A 12 13.12 -66.74
REMARK 500 14 PHE A 14 -103.63 -93.87
REMARK 500 14 LYS A 15 -76.52 -176.07
REMARK 500 14 ASN A 17 -101.68 62.33
REMARK 500 14 GLU A 19 126.19 69.60
REMARK 500 14 ALA A 20 -86.20 172.48
REMARK 500 14 LYS A 21 -81.11 -48.56
REMARK 500 14 HIS A 32 140.32 72.23
REMARK 500 14 GLN A 34 2.98 -58.59
REMARK 500 14 ASP A 35 72.74 -108.23
REMARK 500 14 LEU A 36 51.47 -168.66
REMARK 500 14 ASN A 37 -4.62 62.89
REMARK 500 14 ASP A 38 66.37 65.81
REMARK 500 14 SER A 39 58.33 -158.43
REMARK 500 14 PRO A 40 -159.78 -78.86
REMARK 500 14 SER A 46 -167.39 81.96
REMARK 500 14 THR A 47 -141.37 64.84
REMARK 500 14 ASP A 49 -73.73 64.02
REMARK 500 14 SER A 51 -166.05 52.89
REMARK 500 14 TYR A 57 149.66 -174.77
REMARK 500 14 THR A 60 47.72 -71.15
REMARK 500 14 LYS A 63 44.39 33.64
REMARK 500 14 ASN A 72 -71.97 -116.72
REMARK 500 14 SER A 73 -69.23 -170.97
REMARK 500 14 SER A 74 57.70 -154.15
REMARK 500 14 PRO A 82 -93.39 -84.44
REMARK 500 14 ASN A 83 -153.36 175.19
REMARK 500 14 ASP A 84 43.54 35.86
REMARK 500 14 ASN A 85 85.41 57.69
REMARK 500 14 LYS A 86 139.24 -175.18
REMARK 500 14 ALA A 96 -158.26 -169.55
REMARK 500 14 SER A 100 -45.35 -171.24
REMARK 500 14 PRO A 101 -127.87 -72.94
REMARK 500 14 ARG A 102 87.45 68.47
REMARK 500 14 LYS A 107 76.62 -69.35
REMARK 500 15 SER A 2 25.67 -72.99
REMARK 500 15 MET A 3 163.46 58.87
REMARK 500 15 GLN A 5 81.22 -153.27
REMARK 500 15 PHE A 6 79.60 64.32
REMARK 500 15 LYS A 15 -64.70 65.88
REMARK 500 15 ASN A 17 -92.79 55.70
REMARK 500 15 GLU A 19 99.18 72.35
REMARK 500 15 ALA A 20 -88.64 -170.98
REMARK 500 15 LYS A 21 -80.60 -52.54
REMARK 500 15 ILE A 27 -28.11 -153.87
REMARK 500 15 PRO A 33 -117.69 -68.21
REMARK 500 15 GLN A 34 15.18 -140.76
REMARK 500 15 LEU A 36 75.25 49.95
REMARK 500 15 ASN A 37 76.31 -168.85
REMARK 500 15 SER A 39 44.07 -169.80
REMARK 500 15 PRO A 40 -158.95 -72.57
REMARK 500 15 SER A 46 166.01 71.09
REMARK 500 15 THR A 47 -95.27 -139.73
REMARK 500 15 SER A 48 74.96 -177.46
REMARK 500 15 ASP A 49 -1.35 58.14
REMARK 500 15 THR A 60 11.51 -67.74
REMARK 500 15 ASN A 72 -93.77 -84.29
REMARK 500 15 SER A 73 72.26 -170.28
REMARK 500 15 PRO A 82 -89.84 -80.29
REMARK 500 15 ASN A 83 -164.76 169.27
REMARK 500 15 ASN A 85 76.96 54.27
REMARK 500 15 ALA A 96 -167.68 -126.05
REMARK 500 15 ARG A 102 73.29 50.10
REMARK 500 15 LYS A 107 78.20 -69.87
REMARK 500 16 GLU A 4 86.08 50.93
REMARK 500 16 GLN A 5 101.37 -173.62
REMARK 500 16 PHE A 6 89.22 64.64
REMARK 500 16 PHE A 14 -113.63 -114.01
REMARK 500 16 LYS A 15 76.67 -174.19
REMARK 500 16 ASN A 17 163.19 63.14
REMARK 500 16 SER A 18 -84.84 59.84
REMARK 500 16 ALA A 20 -83.86 177.88
REMARK 500 16 LYS A 21 -70.40 -60.67
REMARK 500 16 TYR A 23 -70.39 -60.01
REMARK 500 16 HIS A 32 153.82 64.06
REMARK 500 16 PRO A 33 -139.95 -72.53
REMARK 500 16 ASP A 35 31.94 -82.34
REMARK 500 16 LEU A 36 41.78 -150.42
REMARK 500 16 ASP A 38 110.37 65.66
REMARK 500 16 SER A 39 31.11 -174.72
REMARK 500 16 PRO A 40 -141.25 -85.24
REMARK 500 16 SER A 46 168.75 65.62
REMARK 500 16 SER A 48 -85.34 66.71
REMARK 500 16 ASP A 49 -60.56 -140.69
REMARK 500 16 SER A 51 -155.80 55.37
REMARK 500 16 LYS A 63 50.98 31.12
REMARK 500 16 ASN A 72 -86.36 -111.09
REMARK 500 16 SER A 73 74.11 -175.42
REMARK 500 16 PRO A 82 -89.77 -92.99
REMARK 500 16 ASN A 83 -154.20 170.59
REMARK 500 16 ASN A 85 80.21 54.81
REMARK 500 16 LYS A 86 136.19 -170.11
REMARK 500 16 ALA A 96 -156.00 -166.56
REMARK 500 16 THR A 99 96.36 60.01
REMARK 500 16 SER A 100 -61.70 -176.74
REMARK 500 16 PRO A 101 -72.26 -66.13
REMARK 500 16 LYS A 107 74.08 -68.93
REMARK 500 17 GLU A 4 99.68 63.89
REMARK 500 17 GLN A 5 105.34 -168.27
REMARK 500 17 PHE A 6 87.85 53.58
REMARK 500 17 LYS A 13 14.47 51.76
REMARK 500 17 LYS A 15 92.07 53.38
REMARK 500 17 ASN A 17 -100.81 -179.45
REMARK 500 17 ALA A 20 -77.94 -173.96
REMARK 500 17 LYS A 21 -83.66 -56.84
REMARK 500 17 HIS A 32 129.02 77.01
REMARK 500 17 GLN A 34 55.17 -160.76
REMARK 500 17 ASP A 38 24.79 45.53
REMARK 500 17 SER A 46 -141.91 53.61
REMARK 500 17 THR A 47 -159.24 60.17
REMARK 500 17 SER A 51 161.34 66.45
REMARK 500 17 LYS A 63 52.06 39.94
REMARK 500 17 ASN A 72 -128.09 -113.83
REMARK 500 17 PRO A 82 -94.08 -82.64
REMARK 500 17 ASN A 83 -155.38 169.59
REMARK 500 17 ASN A 85 80.78 53.99
REMARK 500 17 ALA A 96 -167.36 -169.52
REMARK 500 17 SER A 100 -42.89 -161.80
REMARK 500 17 LYS A 107 76.22 -65.34
REMARK 500 18 SER A 2 53.80 -161.88
REMARK 500 18 MET A 3 -109.16 -134.74
REMARK 500 18 GLN A 5 110.06 -170.30
REMARK 500 18 PHE A 6 90.00 56.88
REMARK 500 18 SER A 18 175.67 73.82
REMARK 500 18 GLU A 19 163.56 65.24
REMARK 500 18 ALA A 20 -85.34 156.04
REMARK 500 18 LYS A 21 -81.62 -48.25
REMARK 500 18 HIS A 32 142.02 76.52
REMARK 500 18 PRO A 33 39.02 -71.94
REMARK 500 18 GLN A 34 59.30 38.92
REMARK 500 18 ASP A 38 88.52 53.59
REMARK 500 18 SER A 39 61.68 -156.70
REMARK 500 18 PRO A 40 -159.42 -97.40
REMARK 500 18 SER A 46 -155.91 63.87
REMARK 500 18 THR A 47 -59.29 177.02
REMARK 500 18 SER A 48 -63.37 -179.47
REMARK 500 18 ASP A 50 81.97 52.50
REMARK 500 18 ASN A 72 -92.11 -80.04
REMARK 500 18 SER A 73 81.98 -174.46
REMARK 500 18 PRO A 82 -86.26 -87.93
REMARK 500 18 ASN A 83 -149.85 168.34
REMARK 500 18 ALA A 96 -156.92 -165.11
REMARK 500 18 THR A 99 19.28 -141.91
REMARK 500 19 SER A 2 95.08 65.19
REMARK 500 19 MET A 3 -56.84 -122.72
REMARK 500 19 GLU A 4 72.70 -64.25
REMARK 500 19 GLN A 5 86.17 -167.29
REMARK 500 19 PHE A 6 82.99 68.09
REMARK 500 19 PHE A 14 -87.28 -122.65
REMARK 500 19 LYS A 15 -144.34 -77.98
REMARK 500 19 CYS A 16 153.23 72.85
REMARK 500 19 ASN A 17 -81.22 -143.82
REMARK 500 19 ALA A 20 -87.90 -177.27
REMARK 500 19 LYS A 21 -80.70 -50.53
REMARK 500 19 HIS A 32 121.12 61.95
REMARK 500 19 PRO A 33 -93.09 -64.39
REMARK 500 19 LEU A 36 50.92 -168.12
REMARK 500 19 ASN A 37 29.14 44.78
REMARK 500 19 SER A 39 42.33 -156.81
REMARK 500 19 PRO A 40 -150.41 -83.78
REMARK 500 19 SER A 46 165.78 61.47
REMARK 500 19 THR A 47 49.56 -152.93
REMARK 500 19 SER A 48 -65.07 58.86
REMARK 500 19 ASP A 49 11.78 -163.01
REMARK 500 19 ASP A 50 89.67 -150.42
REMARK 500 19 CYS A 55 98.88 -62.90
REMARK 500 19 TYR A 57 149.31 -170.30
REMARK 500 19 THR A 60 33.89 -77.24
REMARK 500 19 LYS A 63 46.90 39.92
REMARK 500 19 SER A 73 -73.77 175.83
REMARK 500 19 SER A 74 88.02 -161.09
REMARK 500 19 PRO A 82 -87.87 -79.47
REMARK 500 19 ASN A 83 -151.90 156.13
REMARK 500 19 THR A 99 64.10 34.23
REMARK 500 19 SER A 100 25.66 -168.74
REMARK 500 19 ARG A 102 76.52 -172.45
REMARK 500 20 SER A 2 71.24 56.84
REMARK 500 20 GLN A 5 75.33 63.85
REMARK 500 20 PHE A 6 81.94 77.60
REMARK 500 20 PHE A 14 -102.43 -118.43
REMARK 500 20 LYS A 15 142.87 -173.31
REMARK 500 20 ASN A 17 -99.10 41.77
REMARK 500 20 ALA A 20 -75.72 -175.80
REMARK 500 20 LYS A 21 -78.89 -58.69
REMARK 500 20 HIS A 32 82.03 61.70
REMARK 500 20 LEU A 36 87.20 50.26
REMARK 500 20 PRO A 40 -148.42 -85.99
REMARK 500 20 SER A 46 165.35 65.15
REMARK 500 20 SER A 48 -82.48 60.98
REMARK 500 20 SER A 51 -177.08 54.31
REMARK 500 20 LYS A 56 -70.70 -67.33
REMARK 500 20 ASN A 72 -91.91 -88.35
REMARK 500 20 SER A 73 82.86 -174.30
REMARK 500 20 PRO A 82 -90.77 -80.13
REMARK 500 20 ASN A 83 -159.55 167.57
REMARK 500 20 ALA A 96 -159.03 -166.06
REMARK 500 20 THR A 99 101.21 65.80
REMARK 500 20 SER A 100 -56.54 -179.19
REMARK 500 20 LYS A 107 73.44 -67.24
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 TYR A 53 0.08 SIDE CHAIN
REMARK 500 2 TYR A 23 0.12 SIDE CHAIN
REMARK 500 2 TRP A 31 0.10 SIDE CHAIN
REMARK 500 2 TYR A 53 0.09 SIDE CHAIN
REMARK 500 2 TYR A 57 0.07 SIDE CHAIN
REMARK 500 2 PHE A 105 0.11 SIDE CHAIN
REMARK 500 3 TRP A 31 0.07 SIDE CHAIN
REMARK 500 3 TYR A 53 0.09 SIDE CHAIN
REMARK 500 4 TRP A 31 0.08 SIDE CHAIN
REMARK 500 5 TYR A 22 0.07 SIDE CHAIN
REMARK 500 5 TYR A 53 0.07 SIDE CHAIN
REMARK 500 5 PHE A 105 0.08 SIDE CHAIN
REMARK 500 6 TYR A 22 0.10 SIDE CHAIN
REMARK 500 6 TYR A 53 0.16 SIDE CHAIN
REMARK 500 6 PHE A 105 0.09 SIDE CHAIN
REMARK 500 7 TYR A 22 0.10 SIDE CHAIN
REMARK 500 7 TRP A 31 0.08 SIDE CHAIN
REMARK 500 7 TYR A 53 0.10 SIDE CHAIN
REMARK 500 8 TRP A 31 0.12 SIDE CHAIN
REMARK 500 8 TYR A 57 0.17 SIDE CHAIN
REMARK 500 9 TYR A 22 0.08 SIDE CHAIN
REMARK 500 9 TYR A 53 0.16 SIDE CHAIN
REMARK 500 9 PHE A 105 0.10 SIDE CHAIN
REMARK 500 11 TYR A 22 0.07 SIDE CHAIN
REMARK 500 11 TYR A 53 0.14 SIDE CHAIN
REMARK 500 11 TYR A 57 0.13 SIDE CHAIN
REMARK 500 12 TYR A 22 0.07 SIDE CHAIN
REMARK 500 12 TYR A 53 0.14 SIDE CHAIN
REMARK 500 12 TYR A 57 0.13 SIDE CHAIN
REMARK 500 13 TYR A 22 0.11 SIDE CHAIN
REMARK 500 14 TRP A 31 0.11 SIDE CHAIN
REMARK 500 14 TYR A 53 0.19 SIDE CHAIN
REMARK 500 15 TYR A 22 0.07 SIDE CHAIN
REMARK 500 15 TYR A 53 0.10 SIDE CHAIN
REMARK 500 15 PHE A 105 0.09 SIDE CHAIN
REMARK 500 16 TRP A 31 0.08 SIDE CHAIN
REMARK 500 16 TYR A 53 0.07 SIDE CHAIN
REMARK 500 17 TYR A 22 0.07 SIDE CHAIN
REMARK 500 17 TYR A 53 0.10 SIDE CHAIN
REMARK 500 17 TYR A 57 0.08 SIDE CHAIN
REMARK 500 17 PHE A 105 0.08 SIDE CHAIN
REMARK 500 18 PHE A 6 0.10 SIDE CHAIN
REMARK 500 18 TYR A 23 0.12 SIDE CHAIN
REMARK 500 18 TRP A 31 0.06 SIDE CHAIN
REMARK 500 18 TYR A 53 0.13 SIDE CHAIN
REMARK 500 18 PHE A 105 0.08 SIDE CHAIN
REMARK 500 19 TRP A 31 0.11 SIDE CHAIN
REMARK 500 19 TYR A 53 0.08 SIDE CHAIN
REMARK 500 19 TYR A 57 0.07 SIDE CHAIN
REMARK 500 20 TRP A 31 0.06 SIDE CHAIN
REMARK 500 20 TYR A 53 0.15 SIDE CHAIN
REMARK 500 20 TYR A 57 0.06 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, 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 LEU A 24 -10.43
REMARK 500 1 GLN A 34 -10.58
REMARK 500 1 LEU A 36 13.00
REMARK 500 1 HIS A 62 11.07
REMARK 500 2 ALA A 20 -10.12
REMARK 500 2 GLN A 34 -10.18
REMARK 500 3 GLN A 5 11.37
REMARK 500 4 CYS A 16 -10.63
REMARK 500 4 GLN A 34 -10.43
REMARK 500 5 GLN A 34 -11.79
REMARK 500 7 ALA A 20 -12.14
REMARK 500 7 LEU A 24 -10.40
REMARK 500 8 ALA A 20 -10.49
REMARK 500 8 GLN A 34 -10.94
REMARK 500 9 SER A 51 10.15
REMARK 500 11 GLN A 5 -12.38
REMARK 500 11 LEU A 24 -10.39
REMARK 500 12 GLN A 5 -12.38
REMARK 500 12 LEU A 24 -10.39
REMARK 500 13 SER A 73 10.12
REMARK 500 14 ALA A 20 -10.33
REMARK 500 15 LEU A 24 -10.26
REMARK 500 16 LEU A 24 -10.94
REMARK 500 18 ASN A 17 -11.60
REMARK 500 18 GLN A 34 -10.45
REMARK 500 20 LEU A 24 -10.91
REMARK 500 20 ASP A 35 11.32
REMARK 500 20 SER A 73 10.83
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 ASP A 12 24.0 L L OUTSIDE RANGE
REMARK 500 13 ILE A 26 25.0 L L OUTSIDE RANGE
REMARK 500 13 GLU A 78 23.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OH1 A 1 2 PDB 1OH1 1OH1 1 2
DBREF 1OH1 A 3 109 UNP Q99SX7 Q99SX7 1 107
SEQRES 1 A 109 GLY SER MET GLU GLN PHE GLU LEU PHE SER ILE ASP LYS
SEQRES 2 A 109 PHE LYS CYS ASN SER GLU ALA LYS TYR TYR LEU ASN ILE
SEQRES 3 A 109 ILE GLU GLY GLU TRP HIS PRO GLN ASP LEU ASN ASP SER
SEQRES 4 A 109 PRO LEU LYS PHE ILE LEU SER THR SER ASP ASP SER ASP
SEQRES 5 A 109 TYR ILE CYS LYS TYR ILE ASN THR GLU HIS LYS GLN LEU
SEQRES 6 A 109 THR LEU TYR ASN LYS ASN ASN SER SER ILE VAL ILE GLU
SEQRES 7 A 109 ILE PHE ILE PRO ASN ASP ASN LYS ILE LEU LEU THR ILE
SEQRES 8 A 109 MET ASN THR GLU ALA LEU GLY THR SER PRO ARG MET THR
SEQRES 9 A 109 PHE ILE LYS HIS LYS
HELIX 1 1 ALA A 20 ILE A 27 1 8
SHEET 1 AA 3 GLU A 7 ILE A 11 0
SHEET 2 AA 3 LEU A 41 LEU A 45 1 O LYS A 42 N PHE A 9
SHEET 3 AA 3 GLY A 29 TRP A 31 -1 O GLY A 29 N PHE A 43
SHEET 1 AB 5 TYR A 53 ASN A 59 0
SHEET 2 AB 5 GLN A 64 ASN A 69 -1 O GLN A 64 N ASN A 59
SHEET 3 AB 5 ILE A 75 PHE A 80 -1 O ILE A 75 N ASN A 69
SHEET 4 AB 5 ILE A 87 ASN A 93 -1 O LEU A 88 N PHE A 80
SHEET 5 AB 5 MET A 103 PHE A 105 -1 O MET A 103 N LEU A 89
SSBOND 1 CYS A 16 CYS A 55 1555 1555 2.04
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