Header list of 1pm6.pdb file
Complete list - t 27 2 Bytes
HEADER GENE REGULATION 10-JUN-03 1PM6
TITLE SOLUTION STRUCTURE OF FULL-LENGTH EXCISIONASE (XIS) FROM BACTERIOPHAGE
TITLE 2 HK022
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXCISIONASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE HK022;
SOURCE 3 ORGANISM_TAXID: 10742;
SOURCE 4 GENE: XIS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)*;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPG14_C28S
KEYWDS ANTIPARALLEL BETA-SHEET, WINGED-HELIX, CIS-TRANS-TRANS TRIPROLINE,
KEYWDS 2 GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.V.ROGOV,C.LUECKE,L.MURESANU,H.WIENK,I.KLEINHAUS,K.WERNER,F.LOEHR,
AUTHOR 2 P.PRISTOVSEK,H.RUETERJANS
REVDAT 4 27-OCT-21 1PM6 1 REMARK SEQADV
REVDAT 3 21-APR-09 1PM6 1 REMARK
REVDAT 2 24-FEB-09 1PM6 1 VERSN
REVDAT 1 30-DEC-03 1PM6 0
JRNL AUTH V.V.ROGOV,C.LUCKE,L.MURESANU,H.WIENK,I.KLEINHAUS,K.WERNER,
JRNL AUTH 2 F.LOHR,P.PRISTOVSEK,H.RUTERJANS
JRNL TITL SOLUTION STRUCTURE AND STABILITY OF THE FULL-LENGTH
JRNL TITL 2 EXCISIONASE FROM BACTERIOPHAGE HK022.
JRNL REF EUR.J.BIOCHEM. V. 270 4846 2003
JRNL REFN ISSN 0014-2956
JRNL PMID 14653811
JRNL DOI 10.1111/J.1432-1033.2003.03884.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DISCOVER 2.98, PROCHECK-NMR 3.4.4
REMARK 3 AUTHORS : BRUKER (XWINNMR), ACCELRYS (DISCOVER), LASKOWSKI
REMARK 3 (PROCHECK-NMR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PM6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019421.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM XIS, 50 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 0.2 MM EDTA DISODIUM
REMARK 210 SALT, 0.03% SODIUM AZIDE, 100%
REMARK 210 D2O; 1 MM XIS, 50 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 0.2 MM EDTA DISODIUM
REMARK 210 SALT, 0.03 % SODIUM AZIDE, 95%
REMARK 210 H2O, 5% D2O; 1 MM XIS U-15N, 50
REMARK 210 MM SODIUM PHOSPHATE, 100 MM
REMARK 210 SODIUM CHLORIDE, 0.2 MM EDTA
REMARK 210 DISODIUM SALT, 0.03 % SODIUM
REMARK 210 AZIDE, 95% H2O, 5% D2O; 1 MM XIS
REMARK 210 U-13C,15N, 50 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 0.2 MM EDTA DISODIUM
REMARK 210 SALT, 0.03 % SODIUM AZIDE, 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.7.5, FELIX 97, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE AND
REMARK 210 HOMONUCLEAR NMR SPECTROSCOPY.
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 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 7 CD GLU A 7 OE2 0.111
REMARK 500 1 GLU A 19 CD GLU A 19 OE1 0.109
REMARK 500 1 GLU A 27 CD GLU A 27 OE1 0.110
REMARK 500 1 GLU A 40 CD GLU A 40 OE1 0.111
REMARK 500 1 GLU A 45 CD GLU A 45 OE2 0.111
REMARK 500 2 GLU A 7 CD GLU A 7 OE2 0.114
REMARK 500 2 GLU A 19 CD GLU A 19 OE2 0.110
REMARK 500 2 GLU A 27 CD GLU A 27 OE2 0.109
REMARK 500 2 GLU A 40 CD GLU A 40 OE1 0.110
REMARK 500 2 GLU A 45 CD GLU A 45 OE2 0.113
REMARK 500 3 GLU A 7 CD GLU A 7 OE1 0.115
REMARK 500 3 GLU A 19 CD GLU A 19 OE2 0.113
REMARK 500 3 GLU A 27 CD GLU A 27 OE2 0.110
REMARK 500 3 GLU A 40 CD GLU A 40 OE2 0.109
REMARK 500 3 GLU A 45 CD GLU A 45 OE2 0.114
REMARK 500 4 GLU A 7 CD GLU A 7 OE1 0.112
REMARK 500 4 GLU A 19 CD GLU A 19 OE2 0.111
REMARK 500 4 GLU A 27 CD GLU A 27 OE1 0.116
REMARK 500 4 GLU A 40 CD GLU A 40 OE2 0.115
REMARK 500 4 GLU A 45 CD GLU A 45 OE1 0.113
REMARK 500 5 GLU A 7 CD GLU A 7 OE2 0.111
REMARK 500 5 GLU A 19 CD GLU A 19 OE2 0.110
REMARK 500 5 GLU A 27 CD GLU A 27 OE1 0.112
REMARK 500 5 GLU A 40 CD GLU A 40 OE2 0.111
REMARK 500 5 GLU A 45 CD GLU A 45 OE1 0.110
REMARK 500 6 GLU A 7 CD GLU A 7 OE2 0.112
REMARK 500 6 GLU A 19 CD GLU A 19 OE2 0.115
REMARK 500 6 GLU A 27 CD GLU A 27 OE1 0.110
REMARK 500 6 GLU A 40 CD GLU A 40 OE2 0.114
REMARK 500 6 GLU A 45 CD GLU A 45 OE1 0.114
REMARK 500 7 GLU A 7 CD GLU A 7 OE2 0.109
REMARK 500 7 GLU A 19 CD GLU A 19 OE1 0.115
REMARK 500 7 GLU A 27 CD GLU A 27 OE1 0.110
REMARK 500 7 GLU A 40 CD GLU A 40 OE1 0.113
REMARK 500 7 GLU A 45 CD GLU A 45 OE2 0.108
REMARK 500 8 GLU A 7 CD GLU A 7 OE2 0.110
REMARK 500 8 GLU A 19 CD GLU A 19 OE2 0.109
REMARK 500 8 GLU A 27 CD GLU A 27 OE2 0.110
REMARK 500 8 GLU A 40 CD GLU A 40 OE2 0.117
REMARK 500 8 GLU A 45 CD GLU A 45 OE1 0.114
REMARK 500 9 GLU A 7 CD GLU A 7 OE2 0.114
REMARK 500 9 GLU A 19 CD GLU A 19 OE2 0.115
REMARK 500 9 GLU A 27 CD GLU A 27 OE2 0.111
REMARK 500 9 GLU A 40 CD GLU A 40 OE1 0.115
REMARK 500 9 GLU A 45 CD GLU A 45 OE2 0.114
REMARK 500 10 GLU A 7 CD GLU A 7 OE2 0.111
REMARK 500 10 GLU A 19 CD GLU A 19 OE2 0.110
REMARK 500 10 GLU A 27 CD GLU A 27 OE2 0.110
REMARK 500 10 GLU A 40 CD GLU A 40 OE2 0.114
REMARK 500 10 GLU A 45 CD GLU A 45 OE2 0.110
REMARK 500
REMARK 500 THIS ENTRY HAS 100 BOND DEVIATIONS.
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 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ASP A 37 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 HIS A 44 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 ASP A 51 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 1 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ASP A 37 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 2 ASP A 37 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 HIS A 44 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ASP A 51 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 26 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ASP A 37 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 3 ASP A 37 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 HIS A 44 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 3 ASP A 51 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 ASP A 51 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 310 ANGLE DEVIATIONS.
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
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 ARG A 14 87.54 68.07
REMARK 500 1 ARG A 16 -74.55 -96.50
REMARK 500 1 GLU A 45 69.62 -69.00
REMARK 500 1 SER A 46 -37.00 173.65
REMARK 500 1 ARG A 54 83.05 -159.87
REMARK 500 1 PRO A 55 -72.43 -75.86
REMARK 500 2 GLN A 12 70.07 -100.14
REMARK 500 2 ARG A 13 -64.52 72.90
REMARK 500 2 PRO A 15 86.49 -68.57
REMARK 500 2 SER A 46 57.59 -103.10
REMARK 500 2 ASP A 51 143.65 65.02
REMARK 500 2 LEU A 52 -67.11 -156.21
REMARK 500 2 PRO A 55 -151.85 -73.68
REMARK 500 2 LYS A 71 95.19 71.07
REMARK 500 3 ARG A 14 80.32 81.22
REMARK 500 3 ARG A 16 -87.82 -107.72
REMARK 500 3 ARG A 39 -48.63 -135.38
REMARK 500 3 GLU A 45 68.12 -68.75
REMARK 500 3 SER A 46 -27.44 175.28
REMARK 500 4 ARG A 14 95.31 79.07
REMARK 500 4 ARG A 16 -74.97 -84.06
REMARK 500 4 GLU A 27 30.53 -87.58
REMARK 500 4 SER A 46 -28.89 170.95
REMARK 500 4 LEU A 52 98.47 -64.67
REMARK 500 4 LYS A 71 -175.28 72.15
REMARK 500 5 ARG A 16 -78.55 -121.88
REMARK 500 5 SER A 46 -27.32 155.48
REMARK 500 5 LEU A 52 -67.29 -139.93
REMARK 500 5 VAL A 56 78.51 68.17
REMARK 500 6 ARG A 14 126.82 74.89
REMARK 500 6 SER A 46 44.85 -93.27
REMARK 500 6 ASP A 51 -49.59 78.52
REMARK 500 6 PRO A 55 -152.71 -83.32
REMARK 500 6 ARG A 63 159.72 62.33
REMARK 500 6 ASN A 66 -65.83 -98.60
REMARK 500 6 LYS A 69 -66.30 77.18
REMARK 500 6 ALA A 70 -58.03 68.44
REMARK 500 7 TYR A 2 157.74 77.22
REMARK 500 7 ARG A 13 -73.54 65.69
REMARK 500 7 ARG A 16 -76.79 -69.12
REMARK 500 7 SER A 17 20.94 -154.07
REMARK 500 7 LEU A 18 -51.86 66.62
REMARK 500 7 SER A 46 55.67 -103.71
REMARK 500 7 LYS A 68 88.21 62.75
REMARK 500 8 TYR A 2 98.15 75.42
REMARK 500 8 ARG A 16 -169.18 -111.93
REMARK 500 8 ASP A 37 -76.78 -88.47
REMARK 500 8 ARG A 39 -60.41 168.62
REMARK 500 8 SER A 46 -41.83 168.10
REMARK 500 8 LEU A 52 87.82 -68.18
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5539 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS DATA
DBREF 1PM6 A 1 72 UNP P68927 VXIS_BPHK0 1 72
SEQADV 1PM6 SER A 28 UNP P68927 CYS 28 ENGINEERED MUTATION
SEQRES 1 A 72 MET TYR LEU THR LEU GLN GLU TRP ASN ALA ARG GLN ARG
SEQRES 2 A 72 ARG PRO ARG SER LEU GLU THR VAL ARG ARG TRP VAL ARG
SEQRES 3 A 72 GLU SER ARG ILE PHE PRO PRO PRO VAL LYS ASP GLY ARG
SEQRES 4 A 72 GLU TYR LEU PHE HIS GLU SER ALA VAL LYS VAL ASP LEU
SEQRES 5 A 72 ASN ARG PRO VAL THR GLY SER LEU LEU LYS ARG ILE ARG
SEQRES 6 A 72 ASN GLY LYS LYS ALA LYS SER
HELIX 1 1 LEU A 5 GLN A 12 1 8
HELIX 2 2 SER A 17 SER A 28 1 12
SHEET 1 A 3 TYR A 2 THR A 4 0
SHEET 2 A 3 TYR A 41 HIS A 44 -1 O PHE A 43 N LEU A 3
SHEET 3 A 3 VAL A 35 LYS A 36 -1 N VAL A 35 O LEU A 42
SHEET 1 B 2 ILE A 30 PHE A 31 0
SHEET 2 B 2 VAL A 48 LYS A 49 -1 O VAL A 48 N PHE A 31
CISPEP 1 PHE A 31 PRO A 32 1 -6.21
CISPEP 2 PHE A 31 PRO A 32 2 -5.27
CISPEP 3 PHE A 31 PRO A 32 3 -3.53
CISPEP 4 PHE A 31 PRO A 32 4 -4.95
CISPEP 5 PHE A 31 PRO A 32 5 -5.97
CISPEP 6 PHE A 31 PRO A 32 6 -3.74
CISPEP 7 PHE A 31 PRO A 32 7 -8.09
CISPEP 8 PHE A 31 PRO A 32 8 0.35
CISPEP 9 PHE A 31 PRO A 32 9 -5.45
CISPEP 10 PHE A 31 PRO A 32 10 -4.79
CISPEP 11 PHE A 31 PRO A 32 11 -0.08
CISPEP 12 PHE A 31 PRO A 32 12 -5.99
CISPEP 13 PHE A 31 PRO A 32 13 -0.19
CISPEP 14 PHE A 31 PRO A 32 14 -6.76
CISPEP 15 PHE A 31 PRO A 32 15 -3.10
CISPEP 16 PHE A 31 PRO A 32 16 -5.40
CISPEP 17 PHE A 31 PRO A 32 17 -1.40
CISPEP 18 PHE A 31 PRO A 32 18 1.63
CISPEP 19 PHE A 31 PRO A 32 19 -5.48
CISPEP 20 PHE A 31 PRO A 32 20 -2.35
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 - t 27 2 Bytes