Header list of 1w9r.pdb file
Complete list - r 25 2 Bytes
HEADER RECEPTOR 15-OCT-04 1W9R
TITLE SOLUTION STRUCTURE OF CHOLINE BINDING PROTEIN A, DOMAIN R2,
TITLE 2 THE MAJOR ADHESIN OF STREPTOCOCCUS PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINE BINDING PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ADHESION DOMAIN RESIDUES 329-443;
COMPND 5 SYNONYM: CBPA-R2;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE FIRST FOUR RESIDUES (N-TER-GSHM) DERIVE
COMPND 8 FROM THE PET28A EXPRESSION VECTOR. THE FOLLOWING RESIDUES
COMPND 9 CORRESPOND TO RESIDUES 329-443 OF CBPA FROM THE TIGR4
COMPND 10 STRAIN OF S. PNEUMONIAE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS RECEPTOR, CBPA, POLYMERIC IMMUNOGLOBULIN RECEPTOR, PIGR,
KEYWDS 2 ADHESION, INVASION, PATHOGENESIS
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR R.LUO,B.MANN,W.S.LEWIS,A.ROWE,R.HEATH,M.L.STEWART,
AUTHOR 2 A.E.HAMBURGER,P.J.BJORKMAN,S.SIVAKOLUNDU,E.R.LACY,
AUTHOR 3 E.TUOMANEN,R.W.KRIWACKI
REVDAT 2 24-FEB-09 1W9R 1 VERSN
REVDAT 1 22-FEB-05 1W9R 0
JRNL AUTH R.LUO,B.MANN,W.S.LEWIS,A.ROWE,R.HEATH,M.L.STEWART,
JRNL AUTH 2 A.E.HAMBURGER,S.SIVAKOLUNDU,E.R.LACY,P.J.BJORKMAN,
JRNL AUTH 3 E.TUOMANEN,R.W.KRIWACKI
JRNL TITL SOLUTION STRUCTURE OF CHOLINE BINDING PROTEIN A,
JRNL TITL 2 THE MAJOR ADHESIN OF STREPTOCOCCUS PNEUMONIAE
JRNL REF EMBO J. V. 24 34 2005
JRNL REFN ISSN 0261-4189
JRNL PMID 15616594
JRNL DOI 10.1038/SJ.EMBOJ.7600490
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 8.0
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: A TOTAL OF 2292 NOE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS, 83 PAIRS OF PSI AND PHI AND BACKBONE
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, AND 146 PAIRS OF H-BOND RESTRAINTS
REMARK 3 WERE USED TO CALCULATE AN ENSEMBLE OF STRUCTURES USING A
REMARK 3 MODIFIED VERSION OF THE ORIGINAL TORSION ANGLE DYNAMICS
REMARK 3 PROTOCOL ROUTINE WITHIN CNS. THE TAD PROTOCOL WAS AS FOLLOWS.
REMARK 3 75 PS HIGH-TEMPERATURE TAD 50000 K FOLLOWED BY COOLING TO 1000
REMARK 3 K OVER THE COURSE OF 75 PS AND RAMPING OF THE VAN DER WAALS
REMARK 3 SCALING TERM FROM 0.1 TO 1.0. THE MOLECULES WERE FURTHER
REMARK 3 COOLED TO 300 K OVER THE COURSE OF 20 PS USING CONVENTIONAL
REMARK 3 CARTESIAN DYNAMICS FOLLOWED FINALLY BY 10000 STEPS OF
REMARK 3 CONJUGATE GRADIENT ENERGY MINIMIZATION. THE NOE ENERGY TERM
REMARK 3 WAS 150 KCAL PER MOL FOR THE FIRST THREE STEPS AND 100 KCAL
REMARK 3 PER MOL FOR THE LAST. THE DIHEDRAL RESTRAINT TERM WAS 100 KCAL
REMARK 3 PER MOL FOR THE FIRST THREE STEPS AND 300 KCAL PER MOL FOR THE
REMARK 3 LAST. TWO HUNDRED STRUCTURES WERE CALCULATED, AND THE LOWEST
REMARK 3 40 STRUCTURES WERE FURTHER REFINED BY USING THE SANDER MODULE
REMARK 3 OF AMBER 8.0 MOLECULAR MODELING SUITE. THE SOLVENT WAS
REMARK 3 REPRESENTED BY GENERALIZED-BORN GB SOLVENT MODEL. THE
REMARK 3 STRUCTURES WERE FIRST ENERGY MINIMIZED FOR1 PS WITHOUT ANY
REMARK 3 RESTRAINTS FOLLOWED BY 40 PS SIMULATED ANNEALING FROM 400 K TO
REMARK 3 0 K WITH ALL THE RESTRAINTS. THE DISTANCE AND ANGLE RESTRAINTS
REMARK 3 WERE REPRESENTED BY A SQUARE-WELL PENALTY FUNCTION WITH FORCE
REMARK 3 CONSTANTS OF 20 KCAL PER MOL AND 2 KCAL PER MOL, RESPECTIVELY.
REMARK 4
REMARK 4 1W9R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-04.
REMARK 100 THE PDBE ID CODE IS EBI-21201.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : APPROX. 60 MM
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : 10 MM POTASSIUM PHOSPHATE
REMARK 210 BUFFER, PH 6.5, 50 MM
REMARK 210 NACL, 0.02 % (W/V) SODIUM
REMARK 210 AZIDE, AND 95% H2O/5 %
REMARK 210 2H2O (V/V)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D CT-HNCA, 3D CT-HNCOCA ,
REMARK 210 3D CT-HNCACB, 3D CT-
REMARK 210 HNCOCACB, 4D HNCOCA, 4D
REMARK 210 HNCACO, 3D CCONH-TOCSY, 3D
REMARK 210 HCCONH-TOCSY, 3D
REMARK 210 HBHACBCACONH, 3D HCCH-COSY,
REMARK 210 3D HCCH-TOSCY, 3D NOESY-
REMARK 210 1H-15N HSQC, 3D NOESY-1H-
REMARK 210 13 CHSQC, 4D 1H-15N HSQC-
REMARK 210 NOESY-1H-15N HSQC, 4D 1H-
REMARK 210 15N HSQC-NOESY-1H-13C HSQC,
REMARK 210 4D 1H-13C HSQC-NOESY-1H-
REMARK 210 13C HSQC.
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : UNITYINOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS
REMARK 210 METHOD USED : TAD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: CBPA-R2 STRUCTURES WERE CALCULATED USING NMR DATA
REMARK 210 COLLECTED AT 25 C. INTERPROTON DISTANCES WERE ESTIMATED
REMARK 210 FROM THE VOLUMES OF CROSS-PEAKS IN 3D AND 4D NOESY SPECTRA.
REMARK 210 THE RESTRAINT LOWER BOUNDS WERE SET TO THE VAN DER WAALS
REMARK 210 DISTANCE, AND UPPER BOUNDS WERE SET TO 2.5, 3.5, AND 6.0
REMARK 210 FOR STRONG, MEDIUM, AND WEAK RESONANCES, RESPECTIVELY.
REMARK 210 ESTIMATES OF BACKBONE DIHEDRAL ANGLES F AND Y WERE
REMARK 210 OBTAINED USING THE PROGRAM TALOS AND 1H , 15N, 13C , 13C ,
REMARK 210 AND 13CO CHEMICAL SHIFT VALUES. TALOS-BASED AND
REMARK 210 RESTRAINTS WERE USED ONLY WHEN A WELL-DEFINED PREDICTION
REMARK 210 WAS OBTAINED, AND THIS OCCURRED WITHIN THE HELICAL
REMARK 210 SEGMENTS OF CBPA-R2. IN ADDITION, H-BOND RESTRAINTS WERE
REMARK 210 USED WITHIN -HELICES IN THE FOLLOWING WAY. TWO DISTANCE
REMARK 210 RESTRAINTS WERE USED FOR EACH HYDROGEN BOND, ONE BETWEEN
REMARK 210 THE HYDROGEN AND THE ACCEPTOR ATOM 1.5-2.3 AND ONE BETWEEN
REMARK 210 THE DONOR HEAVY ATOM AND THE ACCEPTOR ATOM 2.4-3.3. THESE
REMARK 210 WERE INTRODUCED AFTER THE INITIAL SET OF STRUCTURE
REMARK 210 CALCULATIONS. AMIDE PROTONS INVOLVED IN H-BONDS WERE
REMARK 210 IDENTIFIED ON THE BASIS OF SLOW EXCHANGE WITH D2O. A TOTAL
REMARK 210 OF 2292 NOE INTERPROTON DISTANCE RESTRAINTS, 83 PAIRS OF
REMARK 210 AND BACKBONE DIHEDRAL ANGLE RESTRAINTS, AND 146 PAIRS OF
REMARK 210 H-BOND RESTRAINTS WERE USED TO CALCULATE AN ENSEMBLE OF
REMARK 210 STRUCTURES USING A MODIFIED VERSION OF THE ORIGINAL
REMARK 210 TORSION ANGLE DYNAMICS PROTOCOL ROUTINE WITHIN CNS. THE
REMARK 210 TAD PROTOCOL WAS AS FOLLOWS 75 PS HIGH-TEMPERATURE TAD 50
REMARK 210 000 K FOLLOWED BY COOLING TO 1000 K OVER THE COURSE OF 75
REMARK 210 PS AND RAMPING OF THE VAN DER WAALS SCALING TERM FROM 0.1
REMARK 210 TO 1.0. THE MOLECULES WERE FURTHER COOLED TO 300 K OVER
REMARK 210 THE COURSE OF 20 PS USING CONVENTIONAL CARTESIAN DYNAMICS
REMARK 210 FOLLOWED FINALLY BY 10000 STEPS OF CONJUGATE GRADIENT
REMARK 210 ENERGY MINIMIZATION. THE NOE ENERGY TERM WAS 150 FOR THE
REMARK 210 FIRST THREE STEPS AND 100 FOR THE LAST. THE DIHEDRAL
REMARK 210 RESTRAINT TERM WAS 100 FOR THE FIRST THREE STEPS AND 300
REMARK 210 FOR THE LAST. TWO HUNDRED STRUCTURES WERE CALCULATED, AND
REMARK 210 THE LOWEST 40 STRUCTURES WERE FURTHER REFINED BY USING THE
REMARK 210 SANDER MODULE OF AMBER 8.0 MOLECULAR MODELING SUITE.
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: 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 4 ARG A 69 CZ ARG A 69 NH1 2.504
REMARK 500 4 ASN A 70 CB ASN A 70 CG 2.357
REMARK 500 4 ASN A 70 N ASN A 70 CA 2.470
REMARK 500 4 GLU A 71 CA GLU A 71 CB 2.744
REMARK 500 4 GLU A 71 CA GLU A 71 C 2.674
REMARK 500 4 GLU A 71 CB GLU A 71 CG 0.649
REMARK 500 4 GLU A 71 N GLU A 71 CA 0.653
REMARK 500 4 GLU A 72 CA GLU A 72 C 4.195
REMARK 500 4 GLU A 72 CB GLU A 72 CG 5.109
REMARK 500 4 GLU A 71 C GLU A 72 N 4.264
REMARK 500 4 LYS A 73 CA LYS A 73 CB 3.968
REMARK 500 4 LYS A 73 CB LYS A 73 CG 1.630
REMARK 500 4 LYS A 73 CD LYS A 73 CE 4.081
REMARK 500 4 VAL A 74 CA VAL A 74 CB 3.308
REMARK 500 4 VAL A 74 CB VAL A 74 CG2 2.228
REMARK 500 4 VAL A 74 N VAL A 74 CA 1.174
REMARK 500 4 LYS A 75 CA LYS A 75 CB 5.173
REMARK 500 4 LYS A 75 CA LYS A 75 C 5.034
REMARK 500 4 GLN A 76 CA GLN A 76 C 5.823
REMARK 500 4 GLN A 76 CB GLN A 76 CG 4.718
REMARK 500 4 GLN A 76 CD GLN A 76 NE2 6.084
REMARK 500 4 GLN A 76 CD GLN A 76 OE1 6.142
REMARK 500 4 GLN A 76 N GLN A 76 CA 5.114
REMARK 500 4 ALA A 77 CA ALA A 77 CB 5.133
REMARK 500 4 ALA A 77 C ALA A 77 O 5.501
REMARK 500 4 ALA A 77 N ALA A 77 CA 3.505
REMARK 500 4 LYS A 78 CB LYS A 78 CG 6.057
REMARK 500 4 LYS A 78 CD LYS A 78 CE 5.679
REMARK 500 4 LYS A 78 CE LYS A 78 NZ 4.716
REMARK 500 4 LYS A 78 C LYS A 78 O 6.350
REMARK 500 4 ALA A 79 CA ALA A 79 CB 7.052
REMARK 500 4 ALA A 79 N ALA A 79 CA 4.987
REMARK 500 4 GLU A 80 CA GLU A 80 CB 5.498
REMARK 500 4 GLU A 80 CA GLU A 80 C 3.620
REMARK 500 4 GLU A 80 CB GLU A 80 CG 3.015
REMARK 500 4 GLU A 80 C GLU A 80 O 5.781
REMARK 500 4 VAL A 81 CA VAL A 81 CB 3.842
REMARK 500 4 VAL A 81 CA VAL A 81 C 4.967
REMARK 500 4 VAL A 81 CB VAL A 81 CG1 4.751
REMARK 500 4 VAL A 81 C VAL A 81 O 6.352
REMARK 500 4 GLU A 80 C VAL A 81 N 6.153
REMARK 500 4 GLU A 82 CA GLU A 82 C 6.464
REMARK 500 4 GLU A 82 CG GLU A 82 CD 7.630
REMARK 500 4 GLU A 82 N GLU A 82 CA 5.946
REMARK 500 4 SER A 83 CA SER A 83 C 6.380
REMARK 500 4 SER A 83 CB SER A 83 OG 5.113
REMARK 500 4 LYS A 84 CA LYS A 84 CB 4.405
REMARK 500 4 LYS A 84 CA LYS A 84 C 5.908
REMARK 500 4 LYS A 84 CE LYS A 84 NZ 4.714
REMARK 500 4 SER A 83 C LYS A 84 N 5.055
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 31 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 TYR A 34 CB - CG - CD1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 1 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 TYR A 34 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 ASN A 37 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 2 GLU A 67 N - CA - C ANGL. DEV. = 19.3 DEGREES
REMARK 500 3 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 TYR A 34 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 PRO A 68 C - N - CA ANGL. DEV. = -9.7 DEGREES
REMARK 500 3 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 4 TYR A 34 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 GLU A 67 N - CA - C ANGL. DEV. = 20.0 DEGREES
REMARK 500 4 ARG A 69 NE - CZ - NH1 ANGL. DEV. = -80.6 DEGREES
REMARK 500 4 ARG A 69 NH1 - CZ - NH2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 4 ASN A 70 CB - CG - OD1 ANGL. DEV. = -36.2 DEGREES
REMARK 500 4 ASN A 70 N - CA - C ANGL. DEV. = 46.9 DEGREES
REMARK 500 4 ASN A 70 N - CA - CB ANGL. DEV. = -27.3 DEGREES
REMARK 500 4 ASN A 70 C - N - CA ANGL. DEV. = -38.3 DEGREES
REMARK 500 4 GLU A 71 CA - CB - CG ANGL. DEV. = -87.9 DEGREES
REMARK 500 4 GLU A 71 CA - C - O ANGL. DEV. = 29.1 DEGREES
REMARK 500 4 GLU A 71 CB - CA - C ANGL. DEV. = -74.5 DEGREES
REMARK 500 4 GLU A 71 CB - CG - CD ANGL. DEV. = -53.4 DEGREES
REMARK 500 4 GLU A 71 N - CA - C ANGL. DEV. = -83.5 DEGREES
REMARK 500 4 GLU A 71 N - CA - CB ANGL. DEV. = -90.4 DEGREES
REMARK 500 4 GLU A 71 C - N - CA ANGL. DEV. = -82.6 DEGREES
REMARK 500 4 GLU A 72 CA - CB - CG ANGL. DEV. = -78.5 DEGREES
REMARK 500 4 GLU A 72 CA - C - O ANGL. DEV. = 20.8 DEGREES
REMARK 500 4 GLU A 72 CB - CA - C ANGL. DEV. = 60.3 DEGREES
REMARK 500 4 GLU A 72 CB - CG - CD ANGL. DEV. = -46.4 DEGREES
REMARK 500 4 GLU A 72 N - CA - C ANGL. DEV. = -31.1 DEGREES
REMARK 500 4 GLU A 71 CA - C - N ANGL. DEV. = -92.9 DEGREES
REMARK 500 4 GLU A 71 O - C - N ANGL. DEV. = 22.9 DEGREES
REMARK 500 4 LYS A 73 CA - CB - CG ANGL. DEV. = -97.7 DEGREES
REMARK 500 4 LYS A 73 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 4 LYS A 73 CD - CE - NZ ANGL. DEV. = 24.7 DEGREES
REMARK 500 4 LYS A 73 CG - CD - CE ANGL. DEV. = -27.7 DEGREES
REMARK 500 4 GLU A 72 CA - C - N ANGL. DEV. = -59.3 DEGREES
REMARK 500 4 VAL A 74 CA - CB - CG1 ANGL. DEV. = 40.5 DEGREES
REMARK 500 4 VAL A 74 CA - CB - CG2 ANGL. DEV. = -79.9 DEGREES
REMARK 500 4 VAL A 74 CG1 - CB - CG2 ANGL. DEV. = 61.9 DEGREES
REMARK 500 4 VAL A 74 N - CA - C ANGL. DEV. = -26.0 DEGREES
REMARK 500 4 VAL A 74 N - CA - CB ANGL. DEV. = -93.8 DEGREES
REMARK 500 4 VAL A 74 C - N - CA ANGL. DEV. = -74.2 DEGREES
REMARK 500 4 LYS A 75 CA - CB - CG ANGL. DEV. = -46.4 DEGREES
REMARK 500 4 LYS A 75 CA - C - O ANGL. DEV. = -44.2 DEGREES
REMARK 500 4 LYS A 75 CB - CA - C ANGL. DEV. = -88.6 DEGREES
REMARK 500 4 LYS A 75 N - CA - C ANGL. DEV. = -39.0 DEGREES
REMARK 500 4 LYS A 75 N - CA - CB ANGL. DEV. = -42.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 168 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 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 SER A 2 -162.81 54.56
REMARK 500 1 HIS A 3 -40.91 125.91
REMARK 500 1 MET A 4 -24.23 -142.80
REMARK 500 1 ASP A 30 21.36 -60.72
REMARK 500 1 ARG A 31 -12.75 -140.92
REMARK 500 1 PRO A 35 -44.49 -28.22
REMARK 500 1 TYR A 39 -47.99 -0.04
REMARK 500 1 GLU A 104 42.92 -71.81
REMARK 500 1 ALA A 109 16.42 57.95
REMARK 500 1 ALA A 110 14.88 -146.39
REMARK 500 1 GLU A 112 -35.97 66.00
REMARK 500 2 SER A 2 93.35 63.68
REMARK 500 2 HIS A 3 -75.90 -137.81
REMARK 500 2 ALA A 12 0.82 -67.79
REMARK 500 2 TYR A 39 -58.24 12.20
REMARK 500 2 THR A 41 85.66 19.71
REMARK 500 2 LEU A 42 -18.52 -48.95
REMARK 500 2 ARG A 69 11.81 57.47
REMARK 500 2 ASN A 70 36.17 -73.92
REMARK 500 2 GLU A 71 -28.47 72.57
REMARK 500 2 GLU A 103 -45.07 66.13
REMARK 500 2 ARG A 107 -120.08 -134.57
REMARK 500 2 GLU A 111 27.31 47.07
REMARK 500 3 HIS A 3 -82.17 -134.15
REMARK 500 3 MET A 4 82.49 -155.57
REMARK 500 3 PRO A 5 6.60 -61.12
REMARK 500 3 GLU A 6 -33.39 -38.44
REMARK 500 3 PRO A 35 -42.89 -28.14
REMARK 500 3 TYR A 39 -59.76 9.70
REMARK 500 3 THR A 41 84.83 36.30
REMARK 500 3 ARG A 69 63.44 25.24
REMARK 500 3 GLU A 71 -28.10 74.84
REMARK 500 3 GLU A 103 51.90 38.59
REMARK 500 3 GLU A 104 16.67 58.51
REMARK 500 3 ARG A 107 67.20 37.39
REMARK 500 3 ALA A 110 19.92 52.54
REMARK 500 4 HIS A 3 -97.08 -131.60
REMARK 500 4 PRO A 5 -2.53 -50.61
REMARK 500 4 GLU A 6 -37.49 -39.35
REMARK 500 4 ASP A 30 14.46 -53.97
REMARK 500 4 PRO A 35 -43.61 -29.10
REMARK 500 4 ASN A 37 52.29 36.71
REMARK 500 4 TYR A 39 -46.37 -4.18
REMARK 500 4 THR A 41 80.35 41.13
REMARK 500 4 GLU A 64 -76.58 -71.77
REMARK 500 4 ARG A 69 17.24 58.78
REMARK 500 4 ASN A 70 23.96 -32.69
REMARK 500 4 GLU A 72 -69.82 -9.79
REMARK 500 4 ALA A 77 73.24 2.92
REMARK 500 4 GLU A 80 99.22 103.66
REMARK 500 4 VAL A 81 -78.84 -48.86
REMARK 500 4 GLU A 82 63.81 -100.25
REMARK 500 4 SER A 83 -102.64 -47.50
REMARK 500 4 LYS A 84 -19.87 -12.50
REMARK 500 4 LYS A 85 -108.47 -87.49
REMARK 500 4 GLU A 104 -88.15 -129.57
REMARK 500 4 ALA A 105 -63.70 -160.48
REMARK 500 4 ALA A 110 -27.76 -156.86
REMARK 500 5 SER A 2 81.41 59.27
REMARK 500 5 HIS A 3 -75.05 -131.58
REMARK 500 5 PRO A 5 -0.68 -57.40
REMARK 500 5 ASP A 30 20.44 -73.65
REMARK 500 5 PRO A 35 -44.08 -26.85
REMARK 500 5 TYR A 39 -48.23 -4.79
REMARK 500 5 LYS A 40 45.15 -76.69
REMARK 500 5 GLU A 71 -25.49 75.38
REMARK 500 5 ARG A 107 62.42 36.92
REMARK 500 6 SER A 2 101.50 -163.05
REMARK 500 6 HIS A 3 -72.48 -140.23
REMARK 500 6 PRO A 5 3.34 -53.12
REMARK 500 6 ASP A 30 15.76 -56.22
REMARK 500 6 PRO A 35 -44.93 -28.16
REMARK 500 6 TYR A 39 -45.26 0.65
REMARK 500 6 LYS A 40 42.15 -80.57
REMARK 500 6 PRO A 68 56.92 -90.85
REMARK 500 6 ARG A 69 78.00 56.93
REMARK 500 6 GLU A 71 -37.14 80.06
REMARK 500 6 GLU A 103 88.15 47.96
REMARK 500 6 ARG A 107 71.29 41.10
REMARK 500 6 GLU A 117 -23.99 -143.60
REMARK 500 7 HIS A 3 -70.54 -72.98
REMARK 500 7 GLU A 6 -51.80 -20.57
REMARK 500 7 TYR A 39 -123.66 51.89
REMARK 500 7 LYS A 40 112.77 -170.88
REMARK 500 7 THR A 41 -74.02 -136.66
REMARK 500 7 GLU A 71 -26.86 -35.70
REMARK 500 7 LYS A 106 109.28 -56.79
REMARK 500 7 ARG A 107 65.04 39.89
REMARK 500 7 LYS A 108 -6.70 -59.81
REMARK 500 7 ALA A 110 17.57 56.52
REMARK 500 8 HIS A 3 -64.54 -136.17
REMARK 500 8 MET A 4 106.58 -161.27
REMARK 500 8 PRO A 5 -0.84 -55.85
REMARK 500 8 TYR A 39 -99.73 20.83
REMARK 500 8 THR A 41 -72.01 -103.39
REMARK 500 8 LYS A 66 -71.36 -51.64
REMARK 500 8 ARG A 69 -60.62 81.30
REMARK 500 8 ASN A 70 20.87 36.57
REMARK 500 8 GLU A 71 -7.06 64.33
REMARK 500 8 ALA A 105 37.71 -72.79
REMARK 500 8 ARG A 107 -40.22 -137.53
REMARK 500 8 ALA A 109 9.80 -153.06
REMARK 500 8 GLU A 112 -41.41 65.17
REMARK 500 8 ASP A 113 -12.74 104.87
REMARK 500 8 VAL A 115 34.42 36.87
REMARK 500 8 LYS A 116 36.83 38.92
REMARK 500 8 GLU A 117 -45.90 -153.28
REMARK 500 9 SER A 2 76.14 52.34
REMARK 500 9 HIS A 3 -73.60 -137.23
REMARK 500 9 PRO A 5 3.29 -57.89
REMARK 500 9 ASN A 37 47.35 39.34
REMARK 500 9 TYR A 39 -102.06 12.50
REMARK 500 9 LYS A 40 -68.66 -101.69
REMARK 500 9 THR A 41 -130.29 48.56
REMARK 500 9 GLU A 71 -34.99 78.30
REMARK 500 10 SER A 2 42.21 -76.84
REMARK 500 10 HIS A 3 -61.22 -123.08
REMARK 500 10 ASP A 30 -37.61 -38.14
REMARK 500 10 TYR A 39 -39.72 -12.38
REMARK 500 10 THR A 41 77.56 33.01
REMARK 500 10 ALA A 105 26.70 49.20
REMARK 500 11 SER A 2 48.92 -76.45
REMARK 500 11 HIS A 3 34.85 -142.13
REMARK 500 11 MET A 4 -55.54 -150.14
REMARK 500 11 ASP A 30 -52.28 -29.52
REMARK 500 11 TYR A 39 -41.21 -11.69
REMARK 500 11 THR A 41 75.09 33.30
REMARK 500 11 ARG A 69 47.31 36.67
REMARK 500 11 GLU A 71 -21.22 75.30
REMARK 500 11 GLU A 103 -43.98 68.24
REMARK 500 11 ALA A 109 6.99 53.78
REMARK 500 11 GLU A 112 -34.86 66.84
REMARK 500 12 HIS A 3 -71.64 -131.43
REMARK 500 12 PRO A 5 -7.14 -53.42
REMARK 500 12 ASP A 30 22.11 -68.42
REMARK 500 12 PRO A 35 -44.03 -27.83
REMARK 500 12 TYR A 39 -48.96 -1.70
REMARK 500 12 THR A 41 80.95 24.76
REMARK 500 12 ALA A 110 -51.83 -144.27
REMARK 500 12 GLU A 111 -36.87 70.86
REMARK 500 13 HIS A 3 51.64 -147.65
REMARK 500 13 MET A 4 -55.73 -166.31
REMARK 500 13 ASP A 30 11.11 -59.71
REMARK 500 13 PRO A 35 -78.59 -17.51
REMARK 500 13 TYR A 39 -44.02 0.64
REMARK 500 13 GLU A 64 -95.26 -53.80
REMARK 500 13 ASN A 70 29.46 -70.64
REMARK 500 13 GLU A 71 -33.47 74.55
REMARK 500 13 LYS A 106 -56.98 71.85
REMARK 500 13 ARG A 107 88.97 48.04
REMARK 500 13 ALA A 110 -38.57 -134.70
REMARK 500 14 HIS A 3 59.52 -145.04
REMARK 500 14 MET A 4 -57.69 -175.78
REMARK 500 14 ASP A 30 17.76 -62.19
REMARK 500 14 PRO A 35 -43.36 -29.42
REMARK 500 14 TYR A 39 -50.45 1.27
REMARK 500 14 THR A 41 72.53 36.24
REMARK 500 14 LYS A 66 1.79 -66.26
REMARK 500 14 GLU A 71 -18.01 79.45
REMARK 500 14 GLU A 102 0.10 -67.87
REMARK 500 14 LYS A 108 6.52 -61.65
REMARK 500 14 ALA A 109 9.40 54.25
REMARK 500 14 GLU A 111 -37.27 -135.74
REMARK 500 15 HIS A 3 -67.17 -122.29
REMARK 500 15 MET A 4 -51.14 -29.48
REMARK 500 15 PRO A 35 -46.64 -27.06
REMARK 500 15 TYR A 39 -36.35 -4.12
REMARK 500 15 ARG A 69 -26.68 63.76
REMARK 500 15 ASN A 70 15.88 36.59
REMARK 500 15 GLU A 71 -11.62 67.88
REMARK 500 15 ARG A 107 53.67 38.12
REMARK 500 15 LYS A 108 -9.02 -54.68
REMARK 500 15 GLU A 112 -32.12 66.16
REMARK 500 16 SER A 2 72.96 57.67
REMARK 500 16 HIS A 3 -81.59 -131.55
REMARK 500 16 ASP A 30 11.64 -62.04
REMARK 500 16 ARG A 31 31.55 -140.32
REMARK 500 16 THR A 36 -35.88 -149.48
REMARK 500 16 TYR A 39 -119.85 38.90
REMARK 500 16 LYS A 40 74.70 84.98
REMARK 500 16 THR A 41 -25.38 -148.14
REMARK 500 16 GLU A 71 -18.07 -39.65
REMARK 500 16 LYS A 106 106.37 -56.50
REMARK 500 16 ARG A 107 -129.63 -141.91
REMARK 500 16 GLU A 112 -18.10 57.83
REMARK 500 16 LYS A 118 63.61 31.41
REMARK 500 17 SER A 2 28.08 -145.59
REMARK 500 17 HIS A 3 -89.00 -94.50
REMARK 500 17 PRO A 5 -3.30 -52.51
REMARK 500 17 ARG A 31 -25.11 -162.81
REMARK 500 17 ASN A 33 -71.89 79.50
REMARK 500 17 ASN A 37 24.19 49.47
REMARK 500 17 TYR A 39 -71.56 28.73
REMARK 500 17 THR A 41 85.61 26.14
REMARK 500 17 LEU A 42 -17.91 -49.11
REMARK 500 17 GLU A 67 30.69 -87.55
REMARK 500 17 PRO A 68 73.62 -57.47
REMARK 500 17 ARG A 69 61.17 29.79
REMARK 500 17 GLU A 71 -20.92 83.18
REMARK 500 17 LYS A 108 6.79 -69.52
REMARK 500 17 ALA A 110 -48.50 -141.97
REMARK 500 18 MET A 4 -54.23 -178.51
REMARK 500 18 ASP A 30 20.18 -63.29
REMARK 500 18 ARG A 31 -35.91 -132.97
REMARK 500 18 PRO A 35 -44.02 -29.11
REMARK 500 18 TYR A 39 -49.16 -0.13
REMARK 500 18 GLU A 71 -30.26 -38.42
REMARK 500 18 ALA A 101 -40.97 61.73
REMARK 500 18 GLU A 102 -36.81 61.57
REMARK 500 18 ARG A 107 -65.83 -29.36
REMARK 500 19 HIS A 3 46.61 -150.46
REMARK 500 19 MET A 4 -54.38 -159.12
REMARK 500 19 PRO A 35 -43.91 -29.75
REMARK 500 19 TYR A 39 -34.38 -10.31
REMARK 500 19 GLU A 43 -57.17 -25.18
REMARK 500 19 GLU A 64 -87.05 -67.58
REMARK 500 19 ARG A 69 59.77 38.91
REMARK 500 19 GLU A 71 -36.84 75.34
REMARK 500 19 LYS A 106 46.77 -77.37
REMARK 500 19 ALA A 109 -28.95 61.82
REMARK 500 19 ALA A 110 -43.02 -159.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 3 MET A 4 1 141.64
REMARK 500 LYS A 66 GLU A 67 1 -115.88
REMARK 500 HIS A 3 MET A 4 2 145.46
REMARK 500 ASN A 33 TYR A 34 2 143.61
REMARK 500 LYS A 66 GLU A 67 2 -141.94
REMARK 500 PRO A 68 ARG A 69 2 126.55
REMARK 500 HIS A 3 MET A 4 3 124.06
REMARK 500 PRO A 5 GLU A 6 3 146.90
REMARK 500 ASN A 37 THR A 38 3 148.53
REMARK 500 ALA A 65 LYS A 66 3 -142.71
REMARK 500 GLU A 67 PRO A 68 3 -76.61
REMARK 500 GLU A 63 GLU A 64 4 140.21
REMARK 500 GLU A 64 ALA A 65 4 -142.54
REMARK 500 LYS A 66 GLU A 67 4 -131.01
REMARK 500 PRO A 68 ARG A 69 4 125.99
REMARK 500 ASN A 70 GLU A 71 4 -39.57
REMARK 500 GLU A 72 LYS A 73 4 -125.24
REMARK 500 LYS A 73 VAL A 74 4 -43.88
REMARK 500 LYS A 78 ALA A 79 4 -145.27
REMARK 500 GLU A 80 VAL A 81 4 81.77
REMARK 500 GLU A 82 SER A 83 4 100.27
REMARK 500 LYS A 85 ALA A 86 4 -55.48
REMARK 500 ASN A 37 THR A 38 5 149.55
REMARK 500 LYS A 66 GLU A 67 5 -139.32
REMARK 500 GLU A 67 PRO A 68 5 -149.55
REMARK 500 HIS A 3 MET A 4 6 122.32
REMARK 500 PRO A 5 GLU A 6 6 146.78
REMARK 500 HIS A 3 MET A 4 7 94.03
REMARK 500 PRO A 5 GLU A 6 7 146.68
REMARK 500 ASN A 33 TYR A 34 7 140.49
REMARK 500 ASN A 37 THR A 38 7 146.09
REMARK 500 LYS A 40 THR A 41 7 -139.45
REMARK 500 LYS A 40 THR A 41 8 -44.40
REMARK 500 LYS A 66 GLU A 67 8 -144.80
REMARK 500 PRO A 68 ARG A 69 8 139.66
REMARK 500 ARG A 107 LYS A 108 8 -39.86
REMARK 500 HIS A 3 MET A 4 9 131.50
REMARK 500 LYS A 66 GLU A 67 9 -144.34
REMARK 500 PRO A 68 ARG A 69 10 148.07
REMARK 500 LYS A 75 GLN A 76 10 149.57
REMARK 500 ASN A 33 TYR A 34 13 142.83
REMARK 500 TYR A 34 PRO A 35 13 64.62
REMARK 500 ASN A 37 THR A 38 13 146.80
REMARK 500 GLU A 63 GLU A 64 13 137.85
REMARK 500 GLU A 64 ALA A 65 13 -139.69
REMARK 500 LYS A 66 GLU A 67 13 -140.42
REMARK 500 PRO A 68 ARG A 69 13 127.50
REMARK 500 LYS A 66 GLU A 67 14 -127.46
REMARK 500 GLU A 67 PRO A 68 14 -148.30
REMARK 500 PRO A 68 ARG A 69 15 140.00
REMARK 500 HIS A 3 MET A 4 16 144.22
REMARK 500 ASP A 30 ARG A 31 16 148.37
REMARK 500 ARG A 31 ARG A 32 16 136.54
REMARK 500 ASN A 37 THR A 38 16 134.78
REMARK 500 LYS A 40 THR A 41 16 -148.58
REMARK 500 LYS A 66 GLU A 67 16 -127.48
REMARK 500 HIS A 3 MET A 4 17 146.22
REMARK 500 ARG A 31 ARG A 32 17 136.91
REMARK 500 TYR A 34 PRO A 35 17 142.82
REMARK 500 ASN A 37 THR A 38 17 145.89
REMARK 500 GLU A 67 PRO A 68 17 -61.07
REMARK 500 GLU A 63 GLU A 64 19 145.71
REMARK 500 LYS A 66 GLU A 67 19 -129.61
REMARK 500 PRO A 68 ARG A 69 19 93.76
REMARK 500 ARG A 107 LYS A 108 19 148.23
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 2 TYR A 34 0.13 SIDE CHAIN
REMARK 500 4 ARG A 69 0.25 SIDE CHAIN
REMARK 500 4 ASN A 70 0.24 SIDE CHAIN
REMARK 500 4 GLN A 76 0.09 SIDE CHAIN
REMARK 500 4 GLU A 82 0.11 SIDE CHAIN
REMARK 500 4 GLU A 87 0.17 SIDE CHAIN
REMARK 500 10 ARG A 32 0.08 SIDE CHAIN
REMARK 500 13 ARG A 32 0.08 SIDE CHAIN
REMARK 500 13 TYR A 34 0.08 SIDE CHAIN
REMARK 500 18 ARG A 32 0.08 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 4 GLU A 72 24.84
REMARK 500 4 GLN A 76 18.09
REMARK 500 4 ALA A 77 62.59
REMARK 500 4 GLU A 80 -118.77
REMARK 500 4 VAL A 81 88.98
REMARK 500 4 GLU A 82 -39.01
REMARK 500 4 SER A 83 10.21
REMARK 500 4 LYS A 85 53.25
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 1 ASN A 37 23.1 L L OUTSIDE RANGE
REMARK 500 2 ASN A 37 22.8 L L OUTSIDE RANGE
REMARK 500 2 GLU A 67 17.5 L L OUTSIDE RANGE
REMARK 500 3 ASN A 37 23.0 L L OUTSIDE RANGE
REMARK 500 3 PRO A 68 24.5 L L OUTSIDE RANGE
REMARK 500 4 ASN A 37 23.6 L L OUTSIDE RANGE
REMARK 500 4 GLU A 67 16.7 L L OUTSIDE RANGE
REMARK 500 4 ASN A 70 14.6 L L OUTSIDE RANGE
REMARK 500 4 GLU A 71 -15.8 L D OUTSIDE RANGE
REMARK 500 4 GLU A 72 -15.8 L D OUTSIDE RANGE
REMARK 500 4 VAL A 74 -147.0 L D OUTSIDE RANGE
REMARK 500 4 LYS A 75 12.8 L L OUTSIDE RANGE
REMARK 500 4 GLN A 76 52.6 L L OUTSIDE RANGE
REMARK 500 4 ALA A 77 146.6 L L OUTSIDE RANGE
REMARK 500 4 ALA A 79 56.6 L L OUTSIDE RANGE
REMARK 500 4 GLU A 80 -20.2 L D OUTSIDE RANGE
REMARK 500 4 VAL A 81 -2.8 L D EXPECTING SP3
REMARK 500 4 GLU A 82 87.2 L L OUTSIDE RANGE
REMARK 500 4 SER A 83 49.1 L L OUTSIDE RANGE
REMARK 500 4 LYS A 84 8.8 L D EXPECTING SP3
REMARK 500 4 ALA A 86 65.9 L L OUTSIDE RANGE
REMARK 500 4 GLU A 87 -12.1 L D OUTSIDE RANGE
REMARK 500 5 ASN A 37 22.7 L L OUTSIDE RANGE
REMARK 500 6 ASN A 37 22.8 L L OUTSIDE RANGE
REMARK 500 6 GLU A 67 22.2 L L OUTSIDE RANGE
REMARK 500 7 ASN A 37 22.8 L L OUTSIDE RANGE
REMARK 500 8 ASN A 37 22.7 L L OUTSIDE RANGE
REMARK 500 8 GLU A 67 15.7 L L OUTSIDE RANGE
REMARK 500 9 ASN A 37 23.5 L L OUTSIDE RANGE
REMARK 500 10 ASN A 37 22.2 L L OUTSIDE RANGE
REMARK 500 10 GLU A 67 17.3 L L OUTSIDE RANGE
REMARK 500 11 ASN A 37 22.7 L L OUTSIDE RANGE
REMARK 500 11 GLU A 67 17.0 L L OUTSIDE RANGE
REMARK 500 12 ASN A 37 22.6 L L OUTSIDE RANGE
REMARK 500 12 GLU A 67 17.6 L L OUTSIDE RANGE
REMARK 500 13 TYR A 34 22.3 L L OUTSIDE RANGE
REMARK 500 13 ASN A 37 20.0 L L OUTSIDE RANGE
REMARK 500 13 GLU A 67 15.1 L L OUTSIDE RANGE
REMARK 500 14 ASN A 37 22.1 L L OUTSIDE RANGE
REMARK 500 15 ASN A 37 21.1 L L OUTSIDE RANGE
REMARK 500 15 GLU A 67 18.8 L L OUTSIDE RANGE
REMARK 500 16 ASN A 37 24.3 L L OUTSIDE RANGE
REMARK 500 17 TYR A 34 25.0 L L OUTSIDE RANGE
REMARK 500 18 ASN A 37 22.7 L L OUTSIDE RANGE
REMARK 500 19 ASN A 37 21.9 L L OUTSIDE RANGE
REMARK 500 19 GLU A 67 12.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PRIMARY ACCESSION NUMBER CORRESPONDS TO THE CBPA
REMARK 999 PROTEIN SEQUENCE. THIS IS DERIVED FROM THE GENOME
REMARK 999 SEQUENCE DETERMINED BY TIGR. THAT ENTRY HAS ACCESSION
REMARK 999 NUMBER AE007507.
DBREF 1W9R A 1 4 PDB 1W9R 1W9R 1 4
DBREF 1W9R A 5 119 UNP Q97N74 Q97N74 329 443
SEQRES 1 A 119 GLY SER HIS MET PRO GLU LYS LYS VAL ALA GLU ALA GLU
SEQRES 2 A 119 LYS LYS VAL GLU GLU ALA LYS LYS LYS ALA GLU ASP GLN
SEQRES 3 A 119 LYS GLU GLU ASP ARG ARG ASN TYR PRO THR ASN THR TYR
SEQRES 4 A 119 LYS THR LEU GLU LEU GLU ILE ALA GLU SER ASP VAL GLU
SEQRES 5 A 119 VAL LYS LYS ALA GLU LEU GLU LEU VAL LYS GLU GLU ALA
SEQRES 6 A 119 LYS GLU PRO ARG ASN GLU GLU LYS VAL LYS GLN ALA LYS
SEQRES 7 A 119 ALA GLU VAL GLU SER LYS LYS ALA GLU ALA THR ARG LEU
SEQRES 8 A 119 GLU LYS ILE LYS THR ASP ARG LYS LYS ALA GLU GLU GLU
SEQRES 9 A 119 ALA LYS ARG LYS ALA ALA GLU GLU ASP LYS VAL LYS GLU
SEQRES 10 A 119 LYS PRO
HELIX 1 1 PRO A 5 ASN A 33 1 29
HELIX 2 2 THR A 41 LYS A 66 1 26
HELIX 3 3 GLU A 71 GLU A 102 1 32
HELIX 4 4 GLU A 112 GLU A 117 5 6
CISPEP 1 MET A 4 PRO A 5 1 2.93
CISPEP 2 GLU A 67 PRO A 68 2 -27.05
CISPEP 3 GLU A 67 PRO A 68 4 -24.39
CISPEP 4 GLN A 76 ALA A 77 4 -25.65
CISPEP 5 VAL A 81 GLU A 82 4 -28.33
CISPEP 6 GLY A 1 SER A 2 5 6.64
CISPEP 7 GLU A 67 PRO A 68 6 -7.72
CISPEP 8 GLU A 67 PRO A 68 8 -19.73
CISPEP 9 GLU A 67 PRO A 68 10 -11.56
CISPEP 10 GLU A 67 PRO A 68 11 -1.82
CISPEP 11 GLU A 67 PRO A 68 12 -8.66
CISPEP 12 GLY A 1 SER A 2 13 2.18
CISPEP 13 GLU A 67 PRO A 68 13 -22.34
CISPEP 14 GLU A 67 PRO A 68 15 -7.21
CISPEP 15 GLU A 67 PRO A 68 19 -21.58
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