HEADER ANTIBODY 27-NOV-00 1HEZ
TITLE STRUCTURE OF P. MAGNUS PROTEIN L BOUND TO A HUMAN IGM FAB.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KAPPA LIGHT CHAIN OF IG;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: 1-214;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEAVY CHAIN OF IG;
COMPND 7 CHAIN: B, D;
COMPND 8 FRAGMENT: 501-724;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PROTEIN L;
COMPND 11 CHAIN: E;
COMPND 12 FRAGMENT: 820-880
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: B-LYMPHOCYTE;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 CELL: B-LYMPHOCYTE;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: FINEGOLDIA MAGNA;
SOURCE 13 ORGANISM_TAXID: 1260;
SOURCE 14 STRAIN: 3316;
SOURCE 15 PLASMID: PKK223-3
KEYWDS ANTIBODY, SUPERANTIGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GRAILLE,E.A.STURA,N.G.HOUSDEN,S.P.BOTTOMLEY,M.J.TAUSSIG,B.J.SUTTON,
AUTHOR 2 M.G.GORE,J.B.CHARBONNIER
REVDAT 6 13-DEC-23 1HEZ 1 REMARK
REVDAT 5 17-MAR-21 1HEZ 1 TITLE REMARK
REVDAT 4 18-APR-18 1HEZ 1 JRNL
REVDAT 3 24-FEB-09 1HEZ 1 VERSN
REVDAT 2 18-JUL-03 1HEZ 1 REMARK
REVDAT 1 10-AUG-01 1HEZ 0
JRNL AUTH M.GRAILLE,E.A.STURA,N.G.HOUSDEN,J.A.BECKINGHAM,
JRNL AUTH 2 S.P.BOTTOMLEY,D.BEALE,M.J.TAUSSIG,B.J.SUTTON,M.G.GORE,
JRNL AUTH 3 J.B.CHARBONNIER
JRNL TITL COMPLEX BETWEEN PEPTOSTREPTOCOCCUS MAGNUS PROTEIN L AND A
JRNL TITL 2 HUMAN ANTIBODY REVEALS STRUCTURAL CONVERGENCE IN THE
JRNL TITL 3 INTERACTION MODES OF FAB BINDING MODES
JRNL REF STRUCTURE V. 9 679 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11587642
JRNL DOI 10.1016/S0969-2126(01)00630-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.BECKINGHAM,S.P.BOTTOMLEY,R.HINTON,B.J.SUTTON,M.G.GORE
REMARK 1 TITL INTERACTIONS BETWEEN A SINGLE IMMUNOGLOBULIN-BINDING DOMAIN
REMARK 1 TITL 2 OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS AND A HUMAN
REMARK 1 TITL 3 KAPPA LIGHT CHAIN
REMARK 1 REF BIOCHEM.J. V. 340 193 1999
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 10229674
REMARK 1 DOI 10.1042/0264-6021:3400193
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.GRAILLE,E.A.STURA,A.L.CORPER,B.J.SUTTON,M.J.TAUSSIG,
REMARK 1 AUTH 2 J.B.CHARBONNIER,G.J.SILVERMAN
REMARK 1 TITL CRYSTAL STRUCTURE OF A STAPHYLOCOCCUS AUREUS PROTEIN A
REMARK 1 TITL 2 DOMAIN COMPLEXED WITH THE FAB FRAGMENT OF A HUMAN IGM
REMARK 1 TITL 3 ANTIBODY: STRUCTURAL BASIS FOR RECOGNITION OF B-CELL
REMARK 1 TITL 4 RECEPTORS AND SUPERANTIGEN ACTIVITY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 97 5399 2000
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 10805799
REMARK 1 DOI 10.1073/PNAS.97.10.5399
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.P.BOTTOMLEY,J.A.BECKINGHAM,J.P.MURPHY,M.ATKINSON,
REMARK 1 AUTH 2 T.ATKINSON,R.J.HINTON,M.G.GORE
REMARK 1 TITL CLONING, EXPRESSION AND PURIFICATION OF PPL-1, A KAPPA-CHAIN
REMARK 1 TITL 2 BINDING PROTEIN, BASED UPON PROTEIN L FROM
REMARK 1 TITL 3 PEPTOSTREPTOCOCCUS MAGNUS.
REMARK 1 REF BIOSEPARATION V. 5 359 1995
REMARK 1 REFN ISSN 0923-179X
REMARK 1 PMID 8767928
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.5
REMARK 3 NUMBER OF REFLECTIONS : 24298
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1192
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 23
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 819
REMARK 3 BIN R VALUE (WORKING SET) : 0.3132
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 42
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 112
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.423
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 22.38
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : IMIDAZOLE.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIDE CHAIN ATOMS FROM RESIDUES LYS A
REMARK 3 45, LYS A 169, GLU B 89, LEU C 54, LYS C 107, GLU D 89, GLN D
REMARK 3 113, GLU D 136, ARG D 181, LYS E 833 AND LYS E 878 ARE NOT
REMARK 3 DEFINED BY ELECTRONIC DENSITY
REMARK 4
REMARK 4 1HEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1290005583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : DW32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.962
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26811
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 4.660
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1DEE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-16% MPEG 5000, 100MM IMIDAZOLE
REMARK 280 MALATE, PH8.5, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.59250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.26900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.66750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.26900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.59250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.66750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 11780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU B 136
REMARK 465 ASN B 137
REMARK 465 SER B 138
REMARK 465 ASN B 139
REMARK 465 PRO B 140
REMARK 465 SER B 141
REMARK 465 SER B 142
REMARK 465 THR B 143
REMARK 465 LYS B 196
REMARK 465 ASP B 197
REMARK 465 VAL B 198
REMARK 465 ALA B 199
REMARK 465 GLN B 200
REMARK 465 GLY B 201
REMARK 465 THR B 202
REMARK 465 ASN B 203
REMARK 465 GLU B 204
REMARK 465 SER D 138
REMARK 465 ASN D 139
REMARK 465 PRO D 140
REMARK 465 SER D 141
REMARK 465 LYS D 196
REMARK 465 ASP D 197
REMARK 465 VAL D 198
REMARK 465 ALA D 199
REMARK 465 GLN D 200
REMARK 465 GLY D 201
REMARK 465 THR D 202
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 45 CG CD CE NZ
REMARK 470 LYS A 169 CG CD CE NZ
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 LEU C 154 CG CD1 CD2
REMARK 470 LYS C 207 CG CD CE NZ
REMARK 470 GLU D 89 CG CD OE1 OE2
REMARK 470 GLN D 113 CG CD OE1 NE2
REMARK 470 GLU D 136 CG CD OE1 OE2
REMARK 470 ARG D 181 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 833 CG CD CE NZ
REMARK 470 LYS E 878 CG CD CE NZ
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 PRO B 224 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO D 222 C - N - CA ANGL. DEV. = 9.3 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
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 VAL A 15 122.58 -35.70
REMARK 500 ILE A 29 15.86 -141.94
REMARK 500 SER A 30 -109.04 59.75
REMARK 500 PRO A 40 124.84 -38.29
REMARK 500 ALA A 51 -29.91 70.23
REMARK 500 SER A 60 -9.82 -43.70
REMARK 500 ALA A 84 -162.12 -178.81
REMARK 500 ARG A 108 -161.24 -129.11
REMARK 500 ASN A 138 84.93 22.78
REMARK 500 PRO A 141 -179.64 -68.48
REMARK 500 ASN A 158 15.59 -149.64
REMARK 500 PHE A 209 125.15 -179.36
REMARK 500 ARG B 16 -162.99 -65.38
REMARK 500 ALA B 49 -176.88 176.31
REMARK 500 ASN B 77 66.97 32.80
REMARK 500 GLU B 89 -8.28 -59.86
REMARK 500 ALA B 106 142.16 -39.23
REMARK 500 SER B 134 -176.56 -65.07
REMARK 500 ASP B 152 73.28 36.24
REMARK 500 SER B 157 76.15 -153.67
REMARK 500 ASN B 167 86.33 -16.95
REMARK 500 SER B 172 63.48 -62.73
REMARK 500 CYS C 23 115.54 -170.84
REMARK 500 SER C 30 -108.42 63.12
REMARK 500 ALA C 51 -30.44 71.45
REMARK 500 SER C 52 11.17 -148.68
REMARK 500 PRO C 59 148.92 -35.80
REMARK 500 PRO C 80 -35.41 -38.67
REMARK 500 ALA C 84 -156.08 -170.23
REMARK 500 PRO C 141 -155.67 -59.01
REMARK 500 SER C 171 17.74 49.44
REMARK 500 LYS C 190 -60.39 -107.75
REMARK 500 ARG C 211 137.80 -37.65
REMARK 500 SER D 7 166.41 179.54
REMARK 500 ALA D 92 177.50 176.07
REMARK 500 GLU D 136 159.02 164.58
REMARK 500 SER D 157 76.05 -154.46
REMARK 500 ASN D 166 27.62 -77.99
REMARK 500 ASN D 167 28.07 46.08
REMARK 500 ASP D 169 133.44 -33.65
REMARK 500 SER D 172 23.82 -161.26
REMARK 500 ARG D 174 -68.73 -122.54
REMARK 500 PRO D 194 -141.14 -83.34
REMARK 500 ASP E 831 42.83 -65.92
REMARK 500 VAL E 860 -4.00 -148.31
REMARK 500 GLU E 863 157.95 -49.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C 401
DBREF 1HEZ A 1 214 PDB 1HEZ 1HEZ 1 214
DBREF 1HEZ B 1 224 PDB 1HEZ 1HEZ 1 224
DBREF 1HEZ C 1 214 PDB 1HEZ 1HEZ 1 214
DBREF 1HEZ D 1 224 PDB 1HEZ 1HEZ 1 224
DBREF 1HEZ E 820 880 UNP Q51918 Q51918 476 536
SEQADV 1HEZ ILE E 834 UNP Q51918 THR 490 CONFLICT
SEQADV 1HEZ ASN E 873 UNP Q51918 TYR 529 CONFLICT
SEQADV 1HEZ HIS E 874 UNP Q51918 THR 530 CONFLICT
SEQADV 1HEZ MET E 875 UNP Q51918 ILE 531 CONFLICT
SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 A 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER
SEQRES 3 A 214 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS
SEQRES 4 A 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER
SEQRES 5 A 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU
SEQRES 7 A 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER
SEQRES 8 A 214 TYR SER THR PRO ARG THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 A 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 B 224 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 B 224 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 B 224 PHE THR PHE SER GLY TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 B 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE SER
SEQRES 5 B 224 TYR ASP GLU SER ASN LYS TYR TYR ALA ASP SER VAL LYS
SEQRES 6 B 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 B 224 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 B 224 ALA VAL TYR TYR CYS ALA LYS VAL LYS PHE TYR ASP PRO
SEQRES 9 B 224 THR ALA PRO ASN ASP TYR TRP GLY GLN GLY THR LEU VAL
SEQRES 10 B 224 THR VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE
SEQRES 11 B 224 PRO LEU VAL SER CYS GLU ASN SER ASN PRO SER SER THR
SEQRES 12 B 224 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP
SEQRES 13 B 224 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP
SEQRES 14 B 224 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY
SEQRES 15 B 224 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER
SEQRES 16 B 224 LYS ASP VAL ALA GLN GLY THR ASN GLU HIS VAL VAL CYS
SEQRES 17 B 224 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASP VAL
SEQRES 18 B 224 PRO LEU PRO
SEQRES 1 C 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 C 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER
SEQRES 3 C 214 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS
SEQRES 4 C 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER
SEQRES 5 C 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 C 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU
SEQRES 7 C 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER
SEQRES 8 C 214 TYR SER THR PRO ARG THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 C 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 D 224 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 D 224 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 D 224 PHE THR PHE SER GLY TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 D 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE SER
SEQRES 5 D 224 TYR ASP GLU SER ASN LYS TYR TYR ALA ASP SER VAL LYS
SEQRES 6 D 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 D 224 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 D 224 ALA VAL TYR TYR CYS ALA LYS VAL LYS PHE TYR ASP PRO
SEQRES 9 D 224 THR ALA PRO ASN ASP TYR TRP GLY GLN GLY THR LEU VAL
SEQRES 10 D 224 THR VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE
SEQRES 11 D 224 PRO LEU VAL SER CYS GLU ASN SER ASN PRO SER SER THR
SEQRES 12 D 224 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP
SEQRES 13 D 224 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP
SEQRES 14 D 224 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY
SEQRES 15 D 224 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER
SEQRES 16 D 224 LYS ASP VAL ALA GLN GLY THR ASN GLU HIS VAL VAL CYS
SEQRES 17 D 224 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASP VAL
SEQRES 18 D 224 PRO LEU PRO
SEQRES 1 E 61 GLU VAL THR ILE LYS VAL ASN LEU ILE PHE ALA ASP GLY
SEQRES 2 E 61 LYS ILE GLN THR ALA GLU PHE LYS GLY THR PHE GLU GLU
SEQRES 3 E 61 ALA THR ALA GLU ALA TYR ARG TYR ALA ASP LEU LEU ALA
SEQRES 4 E 61 LYS VAL ASN GLY GLU TYR THR ALA ASP LEU GLU ASP GLY
SEQRES 5 E 61 GLY ASN HIS MET ASN ILE LYS PHE ALA
HET IMD A 401 5
HET IMD C 401 5
HETNAM IMD IMIDAZOLE
FORMUL 6 IMD 2(C3 H5 N2 1+)
FORMUL 8 HOH *112(H2 O)
HELIX 1 1 GLN A 79 PHE A 83 5 5
HELIX 2 2 SER A 121 LYS A 126 1 6
HELIX 3 3 SER A 182 GLU A 187 1 6
HELIX 4 4 ASN B 74 LYS B 76 5 3
HELIX 5 5 ARG B 87 THR B 91 5 5
HELIX 6 6 GLN C 79 PHE C 83 5 5
HELIX 7 7 SER C 121 SER C 127 1 7
HELIX 8 8 SER C 182 GLU C 187 1 6
HELIX 9 9 ASN D 74 LYS D 76 5 3
HELIX 10 10 ARG D 87 THR D 91 5 5
HELIX 11 11 THR E 842 ALA E 858 1 17
SHEET 1 AA 4 MET A 4 SER A 7 0
SHEET 2 AA 4 VAL A 19 THR A 25 -1 O THR A 22 N SER A 7
SHEET 3 AA 4 ASP A 70 ILE A 75 -1 O PHE A 71 N CYS A 23
SHEET 4 AA 4 PHE A 62 SER A 63 -1 O SER A 63 N THR A 74
SHEET 1 AB12 SER A 53 LEU A 54 0
SHEET 2 AB12 LYS A 45 TYR A 49 -1 O TYR A 49 N SER A 53
SHEET 3 AB12 LEU A 33 GLN A 38 -1 O TRP A 35 N LEU A 47
SHEET 4 AB12 ALA A 84 GLN A 90 -1 O THR A 85 N GLN A 38
SHEET 5 AB12 LYS A 103 ILE A 106 -1 O VAL A 104 N ALA A 84
SHEET 6 AB12 SER A 10 ALA A 13 1 O LEU A 11 N GLU A 105
SHEET 7 AB12 ILE E 834 PHE E 839 -1 O THR E 836 N SER A 12
SHEET 8 AB12 ILE E 823 ILE E 828 -1 O ILE E 823 N PHE E 839
SHEET 9 AB12 HIS E 874 PHE E 879 1 O MET E 875 N ASN E 826
SHEET 10 AB12 TYR E 864 GLU E 869 -1 O THR E 865 N LYS E 878
SHEET 11 AB12 SER C 10 ALA C 13 1 O SER C 10 N ALA E 866
SHEET 12 AB12 LYS C 103 ILE C 106 1 O LYS C 103 N LEU C 11
SHEET 1 AC 4 SER A 114 PHE A 118 0
SHEET 2 AC 4 ALA A 130 PHE A 139 -1 O VAL A 133 N PHE A 118
SHEET 3 AC 4 TYR A 173 LEU A 181 -1 O TYR A 173 N PHE A 139
SHEET 4 AC 4 SER A 159 VAL A 163 -1 O GLN A 160 N THR A 178
SHEET 1 AD 4 ALA A 153 LEU A 154 0
SHEET 2 AD 4 ALA A 144 VAL A 150 -1 O VAL A 150 N ALA A 153
SHEET 3 AD 4 VAL A 191 HIS A 198 -1 O ALA A 193 N LYS A 149
SHEET 4 AD 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196
SHEET 1 BA 4 GLN B 3 SER B 7 0
SHEET 2 BA 4 SER B 17 SER B 25 -1 O SER B 21 N SER B 7
SHEET 3 BA 4 THR B 78 ASN B 84 -1 O LEU B 79 N CYS B 22
SHEET 4 BA 4 PHE B 68 ASP B 73 -1 O THR B 69 N GLN B 82
SHEET 1 BB 5 LYS B 58 TYR B 60 0
SHEET 2 BB 5 GLU B 46 ILE B 51 -1 O LEU B 50 N TYR B 59
SHEET 3 BB 5 HIS B 35 GLN B 39 -1 O TRP B 36 N VAL B 48
SHEET 4 BB 5 ALA B 92 ALA B 97 -1 O VAL B 93 N GLN B 39
SHEET 5 BB 5 LEU B 116 VAL B 117 -1 O VAL B 117 N ALA B 92
SHEET 1 BC 4 THR B 128 PHE B 130 0
SHEET 2 BC 4 ALA B 145 PHE B 153 -1 O LEU B 149 N PHE B 130
SHEET 3 BC 4 TYR B 185 LEU B 192 -1 O TYR B 185 N PHE B 153
SHEET 4 BC 4 THR B 173 ARG B 174 -1 O ARG B 174 N GLN B 190
SHEET 1 BD 3 THR B 128 PHE B 130 0
SHEET 2 BD 3 ALA B 145 PHE B 153 -1 O LEU B 149 N PHE B 130
SHEET 3 BD 3 TYR B 185 LEU B 192 -1 O TYR B 185 N PHE B 153
SHEET 1 BE 3 THR B 159 LYS B 163 0
SHEET 2 BE 3 VAL B 206 GLN B 211 -1 O VAL B 207 N LYS B 163
SHEET 3 BE 3 LYS B 217 VAL B 221 -1 O LYS B 217 N VAL B 210
SHEET 1 CA 4 MET C 4 SER C 7 0
SHEET 2 CA 4 VAL C 19 THR C 25 -1 O THR C 22 N SER C 7
SHEET 3 CA 4 ASP C 70 ILE C 75 -1 O PHE C 71 N CYS C 23
SHEET 4 CA 4 PHE C 62 SER C 63 -1 O SER C 63 N THR C 74
SHEET 1 CB 4 SER C 53 LEU C 54 0
SHEET 2 CB 4 LYS C 45 TYR C 49 -1 O TYR C 49 N SER C 53
SHEET 3 CB 4 LEU C 33 GLN C 38 -1 O TRP C 35 N LEU C 47
SHEET 4 CB 4 THR C 85 GLN C 90 -1 O THR C 85 N GLN C 38
SHEET 1 CC 4 ILE C 117 PHE C 118 0
SHEET 2 CC 4 ALA C 130 PHE C 139 -1 O VAL C 133 N PHE C 118
SHEET 3 CC 4 TYR C 173 LEU C 181 -1 O TYR C 173 N PHE C 139
SHEET 4 CC 4 SER C 159 GLN C 160 -1 O GLN C 160 N THR C 178
SHEET 1 CD 3 LYS C 145 VAL C 150 0
SHEET 2 CD 3 VAL C 191 THR C 197 -1 O ALA C 193 N LYS C 149
SHEET 3 CD 3 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196
SHEET 1 DA 4 GLN D 3 SER D 7 0
SHEET 2 DA 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7
SHEET 3 DA 4 THR D 78 MET D 83 -1 O LEU D 79 N CYS D 22
SHEET 4 DA 4 PHE D 68 ASP D 73 -1 O THR D 69 N GLN D 82
SHEET 1 DB 5 LYS D 58 TYR D 60 0
SHEET 2 DB 5 GLU D 46 ILE D 51 -1 O LEU D 50 N TYR D 59
SHEET 3 DB 5 HIS D 35 GLN D 39 -1 O TRP D 36 N VAL D 48
SHEET 4 DB 5 ALA D 92 VAL D 99 -1 O VAL D 93 N GLN D 39
SHEET 5 DB 5 LEU D 116 VAL D 117 -1 O VAL D 117 N ALA D 92
SHEET 1 DC 4 LYS D 58 TYR D 60 0
SHEET 2 DC 4 GLU D 46 ILE D 51 -1 O LEU D 50 N TYR D 59
SHEET 3 DC 4 HIS D 35 GLN D 39 -1 O TRP D 36 N VAL D 48
SHEET 4 DC 4 ALA D 92 VAL D 99 -1 O VAL D 93 N GLN D 39
SHEET 1 DD 4 THR D 128 PHE D 130 0
SHEET 2 DD 4 ALA D 145 PHE D 153 -1 O LEU D 149 N PHE D 130
SHEET 3 DD 4 TYR D 185 LEU D 192 -1 O TYR D 185 N PHE D 153
SHEET 4 DD 4 VAL D 179 LEU D 180 -1 O VAL D 179 N ALA D 186
SHEET 1 DE 3 THR D 159 LYS D 163 0
SHEET 2 DE 3 HIS D 205 GLN D 211 -1 O VAL D 207 N LYS D 163
SHEET 3 DE 3 LYS D 217 PRO D 222 -1 O LYS D 217 N VAL D 210
SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.03
SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.03
SSBOND 3 CYS A 214 CYS B 135 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 148 CYS B 208 1555 1555 2.03
SSBOND 6 CYS C 23 CYS C 88 1555 1555 2.04
SSBOND 7 CYS C 134 CYS C 194 1555 1555 2.03
SSBOND 8 CYS C 214 CYS D 135 1555 1555 2.03
SSBOND 9 CYS D 22 CYS D 96 1555 1555 2.02
SSBOND 10 CYS D 148 CYS D 208 1555 1555 2.03
CISPEP 1 SER A 7 PRO A 8 0 0.21
CISPEP 2 THR A 94 PRO A 95 0 -0.20
CISPEP 3 TYR A 140 PRO A 141 0 -0.13
CISPEP 4 LEU B 154 PRO B 155 0 0.36
CISPEP 5 SER C 7 PRO C 8 0 -0.43
CISPEP 6 THR C 94 PRO C 95 0 0.02
CISPEP 7 TYR C 140 PRO C 141 0 -0.19
CISPEP 8 LEU D 154 PRO D 155 0 0.09
SITE 1 AC1 6 ARG A 96 THR A 97 PHE A 98 LEU B 45
SITE 2 AC1 6 GLU B 46 TRP B 47
SITE 1 AC2 5 ARG C 96 THR C 97 PHE C 98 LEU D 45
SITE 2 AC2 5 TRP D 47
CRYST1 55.185 87.335 210.538 90.00 90.00 90.00 P 21 21 21 8
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 0.018121 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011450 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004750 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
