Header list of 1xee.pdb file
Complete list - r 2 2 Bytes
HEADER IMMUNE SYSTEM 10-SEP-04 1XEE
TITLE SOLUTION STRUCTURE OF THE CHEMOTAXIS INHIBITORY PROTEIN OF
TITLE 2 STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS-INHIBITING PROTEIN CHIPS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 31-121;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: CHP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS CHEMOTAXIS INHIBITORY PROTEIN, STAPHYLOCOCCUS AUREUS, SUPERANTIGEN,
KEYWDS 2 C5A, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.J.HAAS,C.J.DE HAAS,M.J.POPPELIER,K.P.VAN KESSEL,J.A.VAN STRIJP,
AUTHOR 2 K.DIJKSTRA,R.M.SCHEEK,H.FAN,J.A.KRUIJTZER,R.M.LISKAMP,J.KEMMINK
REVDAT 4 02-MAR-22 1XEE 1 REMARK
REVDAT 3 24-FEB-09 1XEE 1 VERSN
REVDAT 2 24-JAN-06 1XEE 1 JRNL
REVDAT 1 27-SEP-05 1XEE 0
JRNL AUTH P.J.HAAS,C.J.DE HAAS,M.J.POPPELIER,K.P.VAN KESSEL,
JRNL AUTH 2 J.A.VAN STRIJP,K.DIJKSTRA,R.M.SCHEEK,H.FAN,J.A.KRUIJTZER,
JRNL AUTH 3 R.M.LISKAMP,J.KEMMINK
JRNL TITL THE STRUCTURE OF THE C5A RECEPTOR-BLOCKING DOMAIN OF
JRNL TITL 2 CHEMOTAXIS INHIBITORY PROTEIN OF STAPHYLOCOCCUS AUREUS IS
JRNL TITL 3 RELATED TO A GROUP OF IMMUNE EVASIVE MOLECULES
JRNL REF J.MOL.BIOL. V. 353 859 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16213522
JRNL DOI 10.1016/J.JMB.2005.09.014
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, ARIA 1.2
REMARK 3 AUTHORS : BRUNGER ET AL. (CNS), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XEE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030268.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1-2MM 15N OR 13C,15N LABELED
REMARK 210 PROTEIN, 20MM SODIUM PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 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 48 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 TYR A 97 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 TYR A 71 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 3 MET A 62 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 3 TYR A 108 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 TYR A 119 CA - C - N ANGL. DEV. = 13.7 DEGREES
REMARK 500 3 ALA A 120 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 4 GLY A 33 O - C - N ANGL. DEV. = -11.7 DEGREES
REMARK 500 4 TYR A 48 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 ASN A 55 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 4 MET A 62 N - CA - CB ANGL. DEV. = 11.8 DEGREES
REMARK 500 4 TYR A 72 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 PHE A 99 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 LYS A 54 CA - C - N ANGL. DEV. = -17.6 DEGREES
REMARK 500 5 LYS A 61 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 5 LYS A 61 CA - C - N ANGL. DEV. = -16.9 DEGREES
REMARK 500 5 MET A 62 N - CA - CB ANGL. DEV. = 13.1 DEGREES
REMARK 500 5 TYR A 72 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 TYR A 72 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 PHE A 99 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 5 GLU A 118 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 6 ASP A 42 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 6 ASP A 42 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 6 LYS A 61 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 6 MET A 62 N - CA - CB ANGL. DEV. = 12.1 DEGREES
REMARK 500 6 TYR A 75 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 6 LYS A 101 CA - C - N ANGL. DEV. = -19.8 DEGREES
REMARK 500 7 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 7 TYR A 75 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 TYR A 97 CB - CG - CD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 7 LYS A 101 CA - C - N ANGL. DEV. = -13.1 DEGREES
REMARK 500 7 TYR A 108 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 8 LYS A 54 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 8 LYS A 61 CA - C - N ANGL. DEV. = -14.3 DEGREES
REMARK 500 8 MET A 62 N - CA - CB ANGL. DEV. = 12.1 DEGREES
REMARK 500 8 TYR A 75 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 8 PHE A 99 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 9 TYR A 72 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 9 TYR A 72 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 TYR A 75 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 PHE A 98 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 10 LEU A 38 CB - CG - CD1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 10 LYS A 61 CA - C - N ANGL. DEV. = -14.4 DEGREES
REMARK 500 10 MET A 62 N - CA - CB ANGL. DEV. = 13.6 DEGREES
REMARK 500 10 ARG A 84 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 10 LEU A 90 CB - CG - CD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 10 TYR A 97 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 11 ASN A 55 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 11 PHE A 59 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 11 MET A 62 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 113 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 THR A 36 -156.31 -86.52
REMARK 500 1 THR A 53 -160.37 -129.25
REMARK 500 1 SER A 56 -35.37 -39.88
REMARK 500 1 ASN A 68 -83.47 85.97
REMARK 500 1 LYS A 69 35.39 -162.81
REMARK 500 1 LEU A 76 -19.61 -43.93
REMARK 500 1 LEU A 90 32.12 -47.68
REMARK 500 1 LYS A 105 116.65 -163.37
REMARK 500 1 SER A 106 61.82 -69.79
REMARK 500 1 PRO A 113 22.27 -76.99
REMARK 500 1 LYS A 115 -41.91 95.02
REMARK 500 1 GLU A 118 -165.44 -119.38
REMARK 500 2 SER A 32 55.88 -168.75
REMARK 500 2 PRO A 35 93.79 -62.32
REMARK 500 2 LYS A 54 -87.83 -41.39
REMARK 500 2 ASN A 55 61.45 -49.96
REMARK 500 2 ASN A 68 -77.31 76.35
REMARK 500 2 LYS A 69 45.72 -173.16
REMARK 500 2 LEU A 76 -16.01 -39.32
REMARK 500 2 GLU A 118 -82.19 -103.70
REMARK 500 2 ALA A 120 24.20 -55.16
REMARK 500 3 LEU A 34 80.60 85.52
REMARK 500 3 LYS A 54 10.54 -69.54
REMARK 500 3 ASN A 55 74.82 -119.08
REMARK 500 3 GLU A 67 -171.58 -67.18
REMARK 500 3 ASN A 68 -86.33 47.61
REMARK 500 3 LYS A 69 28.07 -153.29
REMARK 500 3 LEU A 76 -26.32 -37.98
REMARK 500 3 LEU A 90 39.58 -51.69
REMARK 500 4 LEU A 34 97.08 -42.71
REMARK 500 4 ASN A 68 -83.42 66.44
REMARK 500 4 LYS A 69 29.77 -168.13
REMARK 500 4 LEU A 76 -24.31 -32.95
REMARK 500 4 LEU A 90 35.13 -46.45
REMARK 500 4 TYR A 119 -152.14 -106.88
REMARK 500 4 ALA A 120 63.96 170.64
REMARK 500 5 SER A 32 55.24 -110.65
REMARK 500 5 LEU A 34 139.94 -27.11
REMARK 500 5 ASN A 55 63.32 -47.35
REMARK 500 5 GLU A 60 -73.55 -86.26
REMARK 500 5 GLU A 67 -172.35 -66.56
REMARK 500 5 ASN A 68 -96.13 66.77
REMARK 500 5 LYS A 69 38.00 -159.65
REMARK 500 5 LEU A 90 -25.02 -30.48
REMARK 500 5 GLU A 118 -155.65 -115.37
REMARK 500 6 SER A 56 -35.54 -29.89
REMARK 500 6 ASN A 68 -86.78 83.42
REMARK 500 6 LYS A 69 24.22 -153.62
REMARK 500 6 LEU A 76 -22.51 -29.97
REMARK 500 6 LEU A 90 42.54 -55.10
REMARK 500
REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS.
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 ALA A 120 TYR A 121 20 -148.72
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 8 GLU A 60 0.07 SIDE CHAIN
REMARK 500 9 ARG A 84 0.12 SIDE CHAIN
REMARK 500 9 TYR A 94 0.08 SIDE CHAIN
REMARK 500 9 PHE A 98 0.08 SIDE CHAIN
REMARK 500 10 TYR A 48 0.07 SIDE CHAIN
REMARK 500 10 ARG A 84 0.11 SIDE CHAIN
REMARK 500 10 TYR A 94 0.09 SIDE CHAIN
REMARK 500 11 ARG A 84 0.12 SIDE CHAIN
REMARK 500 12 TYR A 48 0.08 SIDE CHAIN
REMARK 500 12 ARG A 84 0.13 SIDE CHAIN
REMARK 500 13 ARG A 84 0.14 SIDE CHAIN
REMARK 500 13 TYR A 108 0.07 SIDE CHAIN
REMARK 500 13 TYR A 119 0.08 SIDE CHAIN
REMARK 500 17 ARG A 84 0.14 SIDE CHAIN
REMARK 500 18 TYR A 48 0.08 SIDE CHAIN
REMARK 500 18 TYR A 75 0.11 SIDE CHAIN
REMARK 500 18 TYR A 94 0.23 SIDE CHAIN
REMARK 500 19 ARG A 84 0.15 SIDE CHAIN
REMARK 500 20 ARG A 84 0.11 SIDE CHAIN
REMARK 500 20 TYR A 97 0.08 SIDE CHAIN
REMARK 500 20 TYR A 121 0.07 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 ANGLE, 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 GLY A 33 -22.17
REMARK 500 1 LYS A 51 11.36
REMARK 500 1 THR A 53 -20.23
REMARK 500 1 ASN A 55 11.22
REMARK 500 1 TYR A 75 19.05
REMARK 500 1 ASN A 77 -13.10
REMARK 500 1 ALA A 81 -11.64
REMARK 500 1 ASN A 86 -17.94
REMARK 500 1 LEU A 89 13.50
REMARK 500 1 LEU A 90 -14.03
REMARK 500 1 SER A 104 -17.50
REMARK 500 1 SER A 106 12.00
REMARK 500 1 GLY A 114 13.82
REMARK 500 2 SER A 32 12.74
REMARK 500 2 GLY A 33 -11.24
REMARK 500 2 ARG A 44 -11.35
REMARK 500 2 LYS A 54 17.82
REMARK 500 2 ASN A 68 -10.45
REMARK 500 2 LYS A 85 -10.03
REMARK 500 2 LEU A 89 -19.37
REMARK 500 2 PRO A 113 11.98
REMARK 500 2 TYR A 119 10.80
REMARK 500 3 GLY A 33 13.96
REMARK 500 3 GLY A 52 12.53
REMARK 500 3 LYS A 54 -12.92
REMARK 500 3 ASN A 55 -14.41
REMARK 500 3 ASN A 68 -10.99
REMARK 500 3 GLY A 70 -17.04
REMARK 500 3 TYR A 75 17.27
REMARK 500 3 PRO A 79 13.18
REMARK 500 3 LEU A 89 16.12
REMARK 500 3 LEU A 90 -12.78
REMARK 500 3 LYS A 101 11.17
REMARK 500 4 SER A 32 15.47
REMARK 500 4 GLY A 33 23.67
REMARK 500 4 ASN A 55 -19.63
REMARK 500 4 PHE A 59 17.58
REMARK 500 4 THR A 73 -10.37
REMARK 500 4 TYR A 75 14.12
REMARK 500 4 ASN A 86 -12.06
REMARK 500 4 LEU A 89 11.84
REMARK 500 4 LEU A 90 -10.90
REMARK 500 4 PRO A 113 12.23
REMARK 500 4 LYS A 115 14.02
REMARK 500 4 TYR A 119 -10.24
REMARK 500 4 ALA A 120 12.03
REMARK 500 5 GLY A 33 20.23
REMARK 500 5 LEU A 45 -12.77
REMARK 500 5 LYS A 50 12.43
REMARK 500 5 LYS A 54 21.03
REMARK 500
REMARK 500 THIS ENTRY HAS 231 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XEE A 31 121 UNP Q7WUJ0 Q7WUJ0_STAAU 59 149
SEQRES 1 A 91 ASN SER GLY LEU PRO THR THR LEU GLY LYS LEU ASP GLU
SEQRES 2 A 91 ARG LEU ARG ASN TYR LEU LYS LYS GLY THR LYS ASN SER
SEQRES 3 A 91 ALA GLN PHE GLU LYS MET VAL ILE LEU THR GLU ASN LYS
SEQRES 4 A 91 GLY TYR TYR THR VAL TYR LEU ASN THR PRO LEU ALA GLU
SEQRES 5 A 91 ASP ARG LYS ASN VAL GLU LEU LEU GLY LYS MET TYR LYS
SEQRES 6 A 91 THR TYR PHE PHE LYS LYS GLY GLU SER LYS SER SER TYR
SEQRES 7 A 91 VAL ILE ASN GLY PRO GLY LYS THR ASN GLU TYR ALA TYR
HELIX 1 1 THR A 37 LYS A 51 1 15
HELIX 2 2 ASN A 55 ALA A 57 5 3
HELIX 3 3 ALA A 81 ASN A 86 1 6
SHEET 1 A 4 TYR A 71 TYR A 75 0
SHEET 2 A 4 PHE A 59 THR A 66 -1 N ILE A 64 O TYR A 72
SHEET 3 A 4 MET A 93 LYS A 100 -1 O PHE A 99 N LYS A 61
SHEET 4 A 4 TYR A 108 ASN A 111 -1 O TYR A 108 N PHE A 98
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 2 2 Bytes