HEADER CELL ADHESION/TOXIN 16-MAY-08 3D5R
TITLE CRYSTAL STRUCTURE OF EFB-C (N138A) / C3D COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT C3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: COMPLEMENT C3D FRAGMENT, UNP RESIDUES 996-1287;
COMPND 5 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING
COMPND 6 PROTEIN 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: FIBRINOGEN-BINDING PROTEIN;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 101-165;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: C3, CPAMD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PT7;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS STR.
SOURCE 11 NEWMAN;
SOURCE 12 ORGANISM_TAXID: 426430;
SOURCE 13 STRAIN: MU50;
SOURCE 14 GENE: FIB, EFB, FIB, EFB, NWMN_1069;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR: PT7HMT
KEYWDS PROTEIN-PROTEIN COMPLEX, CELL ADHESION-TOXIN COMPLEX, SITE-DIRECTED
KEYWDS 2 MUTATION, AGE-RELATED MACULAR DEGENERATION, CLEAVAGE ON PAIR OF
KEYWDS 3 BASIC RESIDUES, COMPLEMENT ALTERNATE PATHWAY, COMPLEMENT PATHWAY,
KEYWDS 4 DISEASE MUTATION, GLYCOPROTEIN, IMMUNE RESPONSE, INFLAMMATORY
KEYWDS 5 RESPONSE, INNATE IMMUNITY, PHOSPHOPROTEIN, POLYMORPHISM, SECRETED,
KEYWDS 6 THIOESTER BOND
EXPDTA X-RAY DIFFRACTION
AUTHOR B.V.GEISBRECHT
REVDAT 6 30-AUG-23 3D5R 1 REMARK
REVDAT 5 20-OCT-21 3D5R 1 SEQADV
REVDAT 4 25-OCT-17 3D5R 1 REMARK
REVDAT 3 24-FEB-09 3D5R 1 VERSN
REVDAT 2 11-NOV-08 3D5R 1 JRNL
REVDAT 1 09-SEP-08 3D5R 0
JRNL AUTH N.HASPEL,D.RICKLIN,B.V.GEISBRECHT,L.E.KAVRAKI,J.D.LAMBRIS
JRNL TITL ELECTROSTATIC CONTRIBUTIONS DRIVE THE INTERACTION BETWEEN
JRNL TITL 2 STAPHYLOCOCCUS AUREUS PROTEIN EFB-C AND ITS COMPLEMENT
JRNL TITL 3 TARGET C3D.
JRNL REF PROTEIN SCI. V. 17 1894 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18687868
JRNL DOI 10.1110/PS.036624.108
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
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,
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 53911
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) : 0.218
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2727
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 5718
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.05
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.174
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 : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3D5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56794
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2GOX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% (V/V) TACSIMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.26000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.13000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.39000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 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 ARG C 75 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 75 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 OE2 GLU A 46 CB ARG C 75 2.13
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 ALA A 21 -157.79 -87.98
REMARK 500 LYS A 47 45.89 -79.83
REMARK 500 PHE A 48 -29.24 -168.62
REMARK 500 SER A 75 0.78 92.05
REMARK 500 LYS A 228 19.66 57.54
REMARK 500 LYS A 255 31.39 73.40
REMARK 500 ASP A 296 -61.30 -91.37
REMARK 500 ALA A 297 135.58 -28.27
REMARK 500 ALA B 21 -158.67 -89.37
REMARK 500 LYS B 47 44.98 -75.53
REMARK 500 PHE B 48 -32.29 -167.96
REMARK 500 SER B 75 -1.05 90.54
REMARK 500 ALA B 297 136.37 -32.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GOX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EFB-C (WILD-TYPE) / C3D COMPLEX
REMARK 900 RELATED ID: 2GOM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EFB-C (UNBOUND)
REMARK 900 RELATED ID: 2NOJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EHP (N63E) / C3D COMPLEX
REMARK 900 RELATED ID: 3D5S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EFB-C (R131A) / C3D COMPLEX
DBREF 3D5R A 7 298 UNP P01024 CO3_HUMAN 996 1287
DBREF 3D5R C 11 75 UNP A6QG59 FIB_STAAU 101 165
DBREF 3D5R B 7 298 UNP P01024 CO3_HUMAN 996 1287
DBREF 3D5R D 11 75 UNP A6QG59 FIB_STAAU 101 165
SEQADV 3D5R GLY A 2 UNP P01024 EXPRESSION TAG
SEQADV 3D5R SER A 3 UNP P01024 EXPRESSION TAG
SEQADV 3D5R ARG A 4 UNP P01024 EXPRESSION TAG
SEQADV 3D5R SER A 5 UNP P01024 EXPRESSION TAG
SEQADV 3D5R THR A 6 UNP P01024 EXPRESSION TAG
SEQADV 3D5R ALA A 21 UNP P01024 CYS 1010 ENGINEERED MUTATION
SEQADV 3D5R ALA C 48 UNP A6QG59 ASN 138 ENGINEERED MUTATION
SEQADV 3D5R GLY B 2 UNP P01024 EXPRESSION TAG
SEQADV 3D5R SER B 3 UNP P01024 EXPRESSION TAG
SEQADV 3D5R ARG B 4 UNP P01024 EXPRESSION TAG
SEQADV 3D5R SER B 5 UNP P01024 EXPRESSION TAG
SEQADV 3D5R THR B 6 UNP P01024 EXPRESSION TAG
SEQADV 3D5R ALA B 21 UNP P01024 CYS 1010 ENGINEERED MUTATION
SEQADV 3D5R ALA D 48 UNP A6QG59 ASN 138 ENGINEERED MUTATION
SEQRES 1 A 297 GLY SER ARG SER THR ASP ALA GLU ARG LEU LYS HIS LEU
SEQRES 2 A 297 ILE VAL THR PRO SER GLY ALA GLY GLU GLN ASN MET ILE
SEQRES 3 A 297 GLY MET THR PRO THR VAL ILE ALA VAL HIS TYR LEU ASP
SEQRES 4 A 297 GLU THR GLU GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG
SEQRES 5 A 297 GLN GLY ALA LEU GLU LEU ILE LYS LYS GLY TYR THR GLN
SEQRES 6 A 297 GLN LEU ALA PHE ARG GLN PRO SER SER ALA PHE ALA ALA
SEQRES 7 A 297 PHE VAL LYS ARG ALA PRO SER THR TRP LEU THR ALA TYR
SEQRES 8 A 297 VAL VAL LYS VAL PHE SER LEU ALA VAL ASN LEU ILE ALA
SEQRES 9 A 297 ILE ASP SER GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU
SEQRES 10 A 297 ILE LEU GLU LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU
SEQRES 11 A 297 ASP ALA PRO VAL ILE HIS GLN GLU MET ILE GLY GLY LEU
SEQRES 12 A 297 ARG ASN ASN ASN GLU LYS ASP MET ALA LEU THR ALA PHE
SEQRES 13 A 297 VAL LEU ILE SER LEU GLN GLU ALA LYS ASP ILE CYS GLU
SEQRES 14 A 297 GLU GLN VAL ASN SER LEU PRO GLY SER ILE THR LYS ALA
SEQRES 15 A 297 GLY ASP PHE LEU GLU ALA ASN TYR MET ASN LEU GLN ARG
SEQRES 16 A 297 SER TYR THR VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN
SEQRES 17 A 297 MET GLY ARG LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU
SEQRES 18 A 297 THR THR ALA LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY
SEQRES 19 A 297 LYS GLN LEU TYR ASN VAL GLU ALA THR SER TYR ALA LEU
SEQRES 20 A 297 LEU ALA LEU LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO
SEQRES 21 A 297 PRO VAL VAL ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY
SEQRES 22 A 297 GLY GLY TYR GLY SER THR GLN ALA THR PHE MET VAL PHE
SEQRES 23 A 297 GLN ALA LEU ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 C 65 THR ASP ALA THR ILE LYS LYS GLU GLN LYS LEU ILE GLN
SEQRES 2 C 65 ALA GLN ASN LEU VAL ARG GLU PHE GLU LYS THR HIS THR
SEQRES 3 C 65 VAL SER ALA HIS ARG LYS ALA GLN LYS ALA VAL ALA LEU
SEQRES 4 C 65 VAL SER PHE GLU TYR LYS VAL LYS LYS MET VAL LEU GLN
SEQRES 5 C 65 GLU ARG ILE ASP ASN VAL LEU LYS GLN GLY LEU VAL ARG
SEQRES 1 B 297 GLY SER ARG SER THR ASP ALA GLU ARG LEU LYS HIS LEU
SEQRES 2 B 297 ILE VAL THR PRO SER GLY ALA GLY GLU GLN ASN MET ILE
SEQRES 3 B 297 GLY MET THR PRO THR VAL ILE ALA VAL HIS TYR LEU ASP
SEQRES 4 B 297 GLU THR GLU GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG
SEQRES 5 B 297 GLN GLY ALA LEU GLU LEU ILE LYS LYS GLY TYR THR GLN
SEQRES 6 B 297 GLN LEU ALA PHE ARG GLN PRO SER SER ALA PHE ALA ALA
SEQRES 7 B 297 PHE VAL LYS ARG ALA PRO SER THR TRP LEU THR ALA TYR
SEQRES 8 B 297 VAL VAL LYS VAL PHE SER LEU ALA VAL ASN LEU ILE ALA
SEQRES 9 B 297 ILE ASP SER GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU
SEQRES 10 B 297 ILE LEU GLU LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU
SEQRES 11 B 297 ASP ALA PRO VAL ILE HIS GLN GLU MET ILE GLY GLY LEU
SEQRES 12 B 297 ARG ASN ASN ASN GLU LYS ASP MET ALA LEU THR ALA PHE
SEQRES 13 B 297 VAL LEU ILE SER LEU GLN GLU ALA LYS ASP ILE CYS GLU
SEQRES 14 B 297 GLU GLN VAL ASN SER LEU PRO GLY SER ILE THR LYS ALA
SEQRES 15 B 297 GLY ASP PHE LEU GLU ALA ASN TYR MET ASN LEU GLN ARG
SEQRES 16 B 297 SER TYR THR VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN
SEQRES 17 B 297 MET GLY ARG LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU
SEQRES 18 B 297 THR THR ALA LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY
SEQRES 19 B 297 LYS GLN LEU TYR ASN VAL GLU ALA THR SER TYR ALA LEU
SEQRES 20 B 297 LEU ALA LEU LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO
SEQRES 21 B 297 PRO VAL VAL ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY
SEQRES 22 B 297 GLY GLY TYR GLY SER THR GLN ALA THR PHE MET VAL PHE
SEQRES 23 B 297 GLN ALA LEU ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 D 65 THR ASP ALA THR ILE LYS LYS GLU GLN LYS LEU ILE GLN
SEQRES 2 D 65 ALA GLN ASN LEU VAL ARG GLU PHE GLU LYS THR HIS THR
SEQRES 3 D 65 VAL SER ALA HIS ARG LYS ALA GLN LYS ALA VAL ALA LEU
SEQRES 4 D 65 VAL SER PHE GLU TYR LYS VAL LYS LYS MET VAL LEU GLN
SEQRES 5 D 65 GLU ARG ILE ASP ASN VAL LEU LYS GLN GLY LEU VAL ARG
FORMUL 5 HOH *150(H2 O)
HELIX 1 1 ASP A 7 ILE A 15 5 9
HELIX 2 2 GLU A 23 THR A 42 1 20
HELIX 3 3 GLY A 49 ALA A 69 1 21
HELIX 4 4 SER A 86 ALA A 100 1 15
HELIX 5 5 VAL A 101 LEU A 103 5 3
HELIX 6 6 ASP A 107 GLN A 123 1 17
HELIX 7 7 HIS A 137 ASN A 146 5 10
HELIX 8 8 GLU A 149 GLU A 170 1 22
HELIX 9 9 GLU A 171 VAL A 173 5 3
HELIX 10 10 SER A 175 MET A 192 1 18
HELIX 11 11 ARG A 196 MET A 210 1 15
HELIX 12 12 LYS A 214 ALA A 225 1 12
HELIX 13 13 LYS A 236 LYS A 255 1 20
HELIX 14 14 PHE A 259 GLN A 270 1 12
HELIX 15 15 SER A 279 ALA A 297 1 19
HELIX 16 16 THR C 11 HIS C 35 1 25
HELIX 17 17 THR C 36 LEU C 49 1 14
HELIX 18 18 VAL C 50 GLU C 53 5 4
HELIX 19 19 TYR C 54 GLY C 72 1 19
HELIX 20 20 ASP B 7 ILE B 15 5 9
HELIX 21 21 GLU B 23 THR B 42 1 20
HELIX 22 22 GLY B 49 ALA B 69 1 21
HELIX 23 23 SER B 86 ALA B 100 1 15
HELIX 24 24 VAL B 101 LEU B 103 5 3
HELIX 25 25 ASP B 107 GLN B 123 1 17
HELIX 26 26 HIS B 137 ASN B 146 5 10
HELIX 27 27 GLU B 149 GLU B 170 1 22
HELIX 28 28 GLU B 171 VAL B 173 5 3
HELIX 29 29 SER B 175 TYR B 191 1 17
HELIX 30 30 MET B 192 LEU B 194 5 3
HELIX 31 31 ARG B 196 MET B 210 1 15
HELIX 32 32 LYS B 214 ALA B 225 1 12
HELIX 33 33 LYS B 236 LYS B 255 1 20
HELIX 34 34 PHE B 259 GLN B 270 1 12
HELIX 35 35 SER B 279 ALA B 297 1 19
HELIX 36 36 THR D 11 HIS D 35 1 25
HELIX 37 37 THR D 36 VAL D 50 1 15
HELIX 38 38 SER D 51 GLU D 53 5 3
HELIX 39 39 TYR D 54 GLY D 72 1 19
SSBOND 1 CYS A 112 CYS A 169 1555 1555 2.04
SSBOND 2 CYS B 112 CYS B 169 1555 1555 2.04
CRYST1 91.010 91.010 120.520 90.00 90.00 90.00 P 41 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 0.010988 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008297 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
