HEADER IMMUNE SYSTEM/BLOOD CLOTTING 25-JUL-03 1UJ3
TITLE CRYSTAL STRUCTURE OF A HUMANIZED FAB FRAGMENT OF ANTI-TISSUE-FACTOR
TITLE 2 ANTIBODY IN COMPLEX WITH TISSUE FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGG FAB LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ANTI-TISSUE-FACTOR ANTIBODY HATR-5 FAB;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: IGG FAB HEAVY CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: ANTI-TISSUE-FACTOR ANTIBODY HATR-5 FAB;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: TISSUE FACTOR;
COMPND 13 CHAIN: C;
COMPND 14 FRAGMENT: RESIDUES 606-810;
COMPND 15 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN,
COMPND 16 BLOOD COAGULATION FACTOR;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TISSUE FACTOR, ANTIGEN, ANTIBODY, FAB, IMMUNE SYSTEM-BLOOD CLOTTING
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR U.OHTO,R.MIZUTANI,M.NAKAMURA,H.ADACHI,Y.SATOW
REVDAT 4 25-OCT-23 1UJ3 1 REMARK
REVDAT 3 06-NOV-19 1UJ3 1 JRNL
REVDAT 2 24-FEB-09 1UJ3 1 VERSN
REVDAT 1 25-JUL-04 1UJ3 0
JRNL AUTH U.OHTO,R.MIZUTANI,M.NAKAMURA,H.ADACHI,Y.SATOW
JRNL TITL CRYSTAL STRUCTURE OF A HUMANIZED FAB FRAGMENT OF
JRNL TITL 2 ANTI-TISSUE-FACTOR ANTIBODY IN COMPLEX WITH TISSUE FACTOR.
JRNL REF J.SYNCHROTRON RADIAT. V. 11 105 2004
JRNL REFN ISSN 0909-0495
JRNL PMID 14646147
JRNL DOI 10.1107/S0909049503023513
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1947766.140
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 62792
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) : 0.196
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6352
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7659
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 926
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4913
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 464
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.43000
REMARK 3 B22 (A**2) : 1.86000
REMARK 3 B33 (A**2) : -3.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.980
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.360 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.640 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.890 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 44.95
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000005879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64872
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 37.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: CNS 1.1
REMARK 200 STARTING MODEL: PDB ENTRIES 2HFT AND 1JPT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-PROPANOL, PEG4000, HEPES-NA, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 51.52700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 132.99800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.52700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 132.99800
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 THR A 215
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 LEU B 482 CA - CB - CG ANGL. DEV. = 14.5 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 ALA A 51 -40.02 65.78
REMARK 500 ALA A 84 -172.82 -179.27
REMARK 500 HIS A 91 34.57 -141.73
REMARK 500 SER B 434 -98.71 -19.40
REMARK 500 THR B 435 132.00 52.69
REMARK 500 ASP B 448 60.59 63.67
REMARK 500 PHE C 619 -13.40 77.80
REMARK 500 THR C 640 42.47 -74.95
REMARK 500 LYS C 641 -1.26 53.07
REMARK 500 ASP C 644 102.79 -33.23
REMARK 500 TYR C 651 58.24 35.28
REMARK 500 ASP C 666 87.70 -170.70
REMARK 500 GLU C 684 -120.72 -74.65
REMARK 500 SER C 685 108.04 176.41
REMARK 500 TYR C 694 -164.93 -120.21
REMARK 500 GLU C 695 133.50 -179.14
REMARK 500 ASN C 737 -39.73 68.22
REMARK 500 ASN C 738 -12.32 161.98
REMARK 500 THR C 772 -151.75 -113.88
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 TYR A 36 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1UJ3 C 606 810 UNP P13726 TF_HUMAN 38 242
DBREF 1UJ3 A 1 215 PDB 1UJ3 1UJ3 1 215
DBREF 1UJ3 B 301 517 PDB 1UJ3 1UJ3 301 517
SEQRES 1 A 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 A 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER
SEQRES 3 A 215 GLN ASP ILE LYS SER PHE LEU SER TRP TYR GLN GLN LYS
SEQRES 4 A 215 PRO GLU LYS ALA PRO LYS SER LEU ILE TYR TYR ALA THR
SEQRES 5 A 215 SER LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 A 215 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU
SEQRES 7 A 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS LEU GLN HIS
SEQRES 8 A 215 GLY GLU SER PRO TYR THR PHE GLY GLY GLY THR LYS VAL
SEQRES 9 A 215 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 A 215 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 A 215 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 A 215 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 A 215 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 A 215 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 A 215 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 A 215 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 A 215 PHE ASN ARG GLY GLU CYS THR
SEQRES 1 B 217 GLN VAL GLN LEU LEU GLU SER GLY ALA VAL LEU ALA ARG
SEQRES 2 B 217 PRO GLY THR SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 B 217 PHE ASN ILE LYS ASP TYR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 B 217 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLY ASN ASP
SEQRES 5 B 217 PRO ALA ASN GLY HIS SER MET TYR ASP PRO LYS PHE GLN
SEQRES 6 B 217 GLY ARG VAL THR ILE THR ALA ASP THR SER THR SER THR
SEQRES 7 B 217 VAL PHE MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 B 217 ALA VAL TYR TYR CYS ALA ARG ASP SER GLY TYR ALA MET
SEQRES 9 B 217 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 10 B 217 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 B 217 CYS SER ARG SER THR SER GLU SER THR ALA ALA LEU GLY
SEQRES 12 B 217 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 B 217 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 B 217 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 B 217 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 B 217 LYS THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER ASN
SEQRES 17 B 217 THR LYS VAL ASP LYS ARG VAL GLU SER
SEQRES 1 C 205 THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER THR ASN
SEQRES 2 C 205 PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO VAL ASN
SEQRES 3 C 205 GLN VAL TYR THR VAL GLN ILE SER THR LYS SER GLY ASP
SEQRES 4 C 205 TRP LYS SER LYS CYS PHE TYR THR THR ASP THR GLU CYS
SEQRES 5 C 205 ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS GLN THR
SEQRES 6 C 205 TYR LEU ALA ARG VAL PHE SER TYR PRO ALA GLY ASN VAL
SEQRES 7 C 205 GLU SER THR GLY SER ALA GLY GLU PRO LEU TYR GLU ASN
SEQRES 8 C 205 SER PRO GLU PHE THR PRO TYR LEU GLU THR ASN LEU GLY
SEQRES 9 C 205 GLN PRO THR ILE GLN SER PHE GLU GLN VAL GLY THR LYS
SEQRES 10 C 205 VAL ASN VAL THR VAL GLU ASP GLU ARG THR LEU VAL ARG
SEQRES 11 C 205 ARG ASN ASN THR PHE LEU SER LEU ARG ASP VAL PHE GLY
SEQRES 12 C 205 LYS ASP LEU ILE TYR THR LEU TYR TYR TRP LYS SER SER
SEQRES 13 C 205 SER SER GLY LYS LYS THR ALA LYS THR ASN THR ASN GLU
SEQRES 14 C 205 PHE LEU ILE ASP VAL ASP LYS GLY GLU ASN TYR CYS PHE
SEQRES 15 C 205 SER VAL GLN ALA VAL ILE PRO SER ARG THR VAL ASN ARG
SEQRES 16 C 205 LYS SER THR ASP SER PRO VAL GLU CYS MET
FORMUL 4 HOH *464(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 LYS A 183 LYS A 188 1 6
HELIX 4 4 ASN B 328 TYR B 332 5 5
HELIX 5 5 ARG B 387 THR B 391 5 5
HELIX 6 6 SER B 460 ALA B 462 5 3
HELIX 7 7 SER B 491 LEU B 493 5 3
HELIX 8 8 LEU C 659 VAL C 664 1 6
HELIX 9 9 THR C 701 THR C 706 1 6
HELIX 10 10 LEU C 743 GLY C 748 1 6
HELIX 11 11 LYS C 749 LEU C 751 5 3
SHEET 1 A 4 MET A 4 SER A 7 0
SHEET 2 A 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7
SHEET 3 A 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21
SHEET 4 A 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74
SHEET 1 B 6 SER A 10 ALA A 13 0
SHEET 2 B 6 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11
SHEET 3 B 6 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 102
SHEET 4 B 6 LEU A 33 GLN A 38 -1 N GLN A 38 O THR A 85
SHEET 5 B 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35
SHEET 6 B 6 SER A 53 LEU A 54 -1 O SER A 53 N TYR A 49
SHEET 1 C 4 SER A 10 ALA A 13 0
SHEET 2 C 4 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11
SHEET 3 C 4 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 102
SHEET 4 C 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90
SHEET 1 D 4 SER A 114 PHE A 118 0
SHEET 2 D 4 THR A 129 PHE A 139 -1 O ASN A 137 N SER A 114
SHEET 3 D 4 TYR A 173 SER A 182 -1 O LEU A 181 N ALA A 130
SHEET 4 D 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178
SHEET 1 E 4 ALA A 153 LEU A 154 0
SHEET 2 E 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153
SHEET 3 E 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147
SHEET 4 E 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196
SHEET 1 F 4 GLN B 303 GLU B 306 0
SHEET 2 F 4 VAL B 318 SER B 325 -1 O LYS B 323 N LEU B 305
SHEET 3 F 4 THR B 378 LEU B 383 -1 O MET B 381 N ILE B 320
SHEET 4 F 4 VAL B 368 ASP B 373 -1 N THR B 369 O GLU B 382
SHEET 1 G 6 VAL B 310 ALA B 312 0
SHEET 2 G 6 THR B 411 VAL B 415 1 O THR B 414 N ALA B 312
SHEET 3 G 6 ALA B 392 ASP B 399 -1 N ALA B 392 O VAL B 413
SHEET 4 G 6 TYR B 333 GLN B 339 -1 N VAL B 337 O TYR B 395
SHEET 5 G 6 LEU B 345 ASN B 351 -1 O GLU B 346 N LYS B 338
SHEET 6 G 6 SER B 358 TYR B 360 -1 O MET B 359 N GLY B 350
SHEET 1 H 4 VAL B 310 ALA B 312 0
SHEET 2 H 4 THR B 411 VAL B 415 1 O THR B 414 N ALA B 312
SHEET 3 H 4 ALA B 392 ASP B 399 -1 N ALA B 392 O VAL B 413
SHEET 4 H 4 MET B 404 TRP B 407 -1 O TYR B 406 N ARG B 398
SHEET 1 I 4 SER B 424 LEU B 428 0
SHEET 2 I 4 THR B 439 TYR B 449 -1 O LEU B 445 N PHE B 426
SHEET 3 I 4 TYR B 480 PRO B 489 -1 O LEU B 482 N VAL B 446
SHEET 4 I 4 VAL B 467 THR B 469 -1 N HIS B 468 O VAL B 485
SHEET 1 J 4 SER B 424 LEU B 428 0
SHEET 2 J 4 THR B 439 TYR B 449 -1 O LEU B 445 N PHE B 426
SHEET 3 J 4 TYR B 480 PRO B 489 -1 O LEU B 482 N VAL B 446
SHEET 4 J 4 VAL B 473 LEU B 474 -1 N VAL B 473 O SER B 481
SHEET 1 K 3 THR B 455 TRP B 458 0
SHEET 2 K 3 THR B 499 HIS B 504 -1 O ASN B 501 N SER B 457
SHEET 3 K 3 THR B 509 ARG B 514 -1 O VAL B 511 N VAL B 502
SHEET 1 L 3 TYR C 610 THR C 617 0
SHEET 2 L 3 LYS C 620 GLU C 626 -1 O GLU C 626 N TYR C 610
SHEET 3 L 3 GLU C 656 ASP C 658 -1 O CYS C 657 N LEU C 623
SHEET 1 M 3 TRP C 645 THR C 652 0
SHEET 2 M 3 GLN C 632 SER C 639 -1 N VAL C 636 O LYS C 648
SHEET 3 M 3 LEU C 672 PRO C 679 -1 O PHE C 676 N THR C 635
SHEET 1 N 3 ILE C 713 VAL C 719 0
SHEET 2 N 3 LYS C 722 VAL C 727 -1 O ASN C 724 N GLU C 717
SHEET 3 N 3 GLU C 774 ILE C 777 -1 O ILE C 777 N VAL C 723
SHEET 1 O 2 ARG C 731 ARG C 736 0
SHEET 2 O 2 THR C 739 SER C 742 -1 N THR C 739 O ARG C 736
SHEET 1 P 4 LYS C 765 THR C 770 0
SHEET 2 P 4 ILE C 752 LYS C 759 -1 N LEU C 755 O ALA C 768
SHEET 3 P 4 TYR C 785 VAL C 792 -1 O VAL C 792 N ILE C 752
SHEET 4 P 4 GLU C 808 CYS C 809 -1 O GLU C 808 N PHE C 787
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 431 1555 1555 2.04
SSBOND 4 CYS B 322 CYS B 396 1555 1555 2.04
SSBOND 5 CYS B 444 CYS B 500 1555 1555 2.04
SSBOND 6 CYS C 649 CYS C 657 1555 1555 2.06
SSBOND 7 CYS C 786 CYS C 809 1555 1555 2.04
CISPEP 1 SER A 7 PRO A 8 0 -0.53
CISPEP 2 SER A 94 PRO A 95 0 -0.35
CISPEP 3 TYR A 140 PRO A 141 0 0.45
CISPEP 4 PHE B 450 PRO B 451 0 -0.38
CISPEP 5 GLU B 452 PRO B 453 0 0.33
CISPEP 6 GLU C 626 PRO C 627 0 -0.16
CRYST1 103.054 265.996 42.254 90.00 90.00 90.00 P 21 21 2 4
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 0.009704 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023666 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
