HEADER HYDROLASE 24-JUN-08 3DKB
TITLE CRYSTAL STRUCTURE OF A20, 2.5 ANGSTROM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR, ALPHA-INDUCED PROTEIN 3;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 1-370;
COMPND 5 SYNONYM: DNA-BINDING PROTEIN A20, ZINC FINGER PROTEIN A20;
COMPND 6 EC: 3.-.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TNFAIP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS OTU DOMAIN, DUB DOMAIN, APOPTOSIS, CYTOPLASM, DNA-BINDING, HYDROLASE,
KEYWDS 2 METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, PROTEASE,
KEYWDS 3 THIOL PROTEASE, UBL CONJUGATION PATHWAY, ZINC, ZINC-FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-C.LIN,J.Y.CHUNG,Y.-C.LO,H.WU
REVDAT 4 21-FEB-24 3DKB 1 SEQADV
REVDAT 3 25-OCT-17 3DKB 1 REMARK
REVDAT 2 24-FEB-09 3DKB 1 VERSN
REVDAT 1 08-JUL-08 3DKB 0
JRNL AUTH S.-C.LIN,J.Y.CHUNG,B.LAMOTHE,K.RAJASHANKAR,M.LU,Y.-C.LO,
JRNL AUTH 2 A.Y.LAM,B.G.DARNAY,H.WU
JRNL TITL MOLECULAR BASIS FOR THE UNIQUE DEUBIQUITINATING ACTIVITY OF
JRNL TITL 2 THE NF-KAPPAB INHIBITOR A20
JRNL REF J.MOL.BIOL. V. 376 526 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18164316
JRNL DOI 10.1016/J.JMB.2007.11.092
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 79018
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) : 0.200
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7644
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3235
REMARK 3 BIN FREE R VALUE : 0.3316
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 784
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 : 17550
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.14600
REMARK 3 B22 (A**2) : 8.14600
REMARK 3 B33 (A**2) : -16.29100
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) : 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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 : 62.03
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000048144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-06; 01-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 97; NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; NSLS
REMARK 200 BEAMLINE : 24-ID-C; X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97922,
REMARK 200 0.97942,0.97166,0.98714; 0.97563
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84504
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE 2.06, RESOLVE 2.13
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM SULFATE, 300 MM NA
REMARK 280 THIOCYANATE, 5 MM MGSO4, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.36200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.68100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 MET A 5981
REMARK 465 GLY A 5982
REMARK 465 SER A 5983
REMARK 465 SER A 5984
REMARK 465 HIS A 5985
REMARK 465 HIS A 5986
REMARK 465 HIS A 5987
REMARK 465 HIS A 5988
REMARK 465 HIS A 5989
REMARK 465 HIS A 5990
REMARK 465 SER A 5991
REMARK 465 SER A 5992
REMARK 465 GLY A 5993
REMARK 465 LEU A 5994
REMARK 465 VAL A 5995
REMARK 465 PRO A 5996
REMARK 465 ARG A 5997
REMARK 465 GLY A 5998
REMARK 465 SER A 5999
REMARK 465 HIS A 6000
REMARK 465 MET A 6001
REMARK 465 ALA A 6002
REMARK 465 THR A 6155
REMARK 465 GLY A 6156
REMARK 465 LEU A 6157
REMARK 465 CYS A 6158
REMARK 465 SER A 6222
REMARK 465 ASN A 6223
REMARK 465 PHE A 6224
REMARK 465 ALA A 6225
REMARK 465 GLY A 6363
REMARK 465 ARG A 6364
REMARK 465 ARG A 6365
REMARK 465 GLU A 6366
REMARK 465 GLY A 6367
REMARK 465 HIS A 6368
REMARK 465 ALA A 6369
REMARK 465 GLN A 6370
REMARK 465 MET B 981
REMARK 465 GLY B 982
REMARK 465 SER B 983
REMARK 465 SER B 984
REMARK 465 HIS B 985
REMARK 465 HIS B 986
REMARK 465 HIS B 987
REMARK 465 HIS B 988
REMARK 465 HIS B 989
REMARK 465 HIS B 990
REMARK 465 SER B 991
REMARK 465 SER B 992
REMARK 465 GLY B 993
REMARK 465 LEU B 994
REMARK 465 VAL B 995
REMARK 465 PRO B 996
REMARK 465 ARG B 997
REMARK 465 GLY B 998
REMARK 465 SER B 999
REMARK 465 HIS B 1000
REMARK 465 MET B 1001
REMARK 465 ALA B 1002
REMARK 465 THR B 1155
REMARK 465 GLY B 1156
REMARK 465 LEU B 1157
REMARK 465 CYS B 1158
REMARK 465 SER B 1222
REMARK 465 ASN B 1223
REMARK 465 PHE B 1224
REMARK 465 ALA B 1225
REMARK 465 GLY B 1363
REMARK 465 ARG B 1364
REMARK 465 ARG B 1365
REMARK 465 GLU B 1366
REMARK 465 GLY B 1367
REMARK 465 HIS B 1368
REMARK 465 ALA B 1369
REMARK 465 GLN B 1370
REMARK 465 MET C 1981
REMARK 465 GLY C 1982
REMARK 465 SER C 1983
REMARK 465 SER C 1984
REMARK 465 HIS C 1985
REMARK 465 HIS C 1986
REMARK 465 HIS C 1987
REMARK 465 HIS C 1988
REMARK 465 HIS C 1989
REMARK 465 HIS C 1990
REMARK 465 SER C 1991
REMARK 465 SER C 1992
REMARK 465 GLY C 1993
REMARK 465 LEU C 1994
REMARK 465 VAL C 1995
REMARK 465 PRO C 1996
REMARK 465 ARG C 1997
REMARK 465 GLY C 1998
REMARK 465 SER C 1999
REMARK 465 HIS C 2000
REMARK 465 MET C 2001
REMARK 465 ALA C 2002
REMARK 465 THR C 2155
REMARK 465 GLY C 2156
REMARK 465 LEU C 2157
REMARK 465 CYS C 2158
REMARK 465 SER C 2222
REMARK 465 ASN C 2223
REMARK 465 PHE C 2224
REMARK 465 ALA C 2225
REMARK 465 GLY C 2363
REMARK 465 ARG C 2364
REMARK 465 ARG C 2365
REMARK 465 GLU C 2366
REMARK 465 GLY C 2367
REMARK 465 HIS C 2368
REMARK 465 ALA C 2369
REMARK 465 GLN C 2370
REMARK 465 MET D 2981
REMARK 465 GLY D 2982
REMARK 465 SER D 2983
REMARK 465 SER D 2984
REMARK 465 HIS D 2985
REMARK 465 HIS D 2986
REMARK 465 HIS D 2987
REMARK 465 HIS D 2988
REMARK 465 HIS D 2989
REMARK 465 HIS D 2990
REMARK 465 SER D 2991
REMARK 465 SER D 2992
REMARK 465 GLY D 2993
REMARK 465 LEU D 2994
REMARK 465 VAL D 2995
REMARK 465 PRO D 2996
REMARK 465 ARG D 2997
REMARK 465 GLY D 2998
REMARK 465 SER D 2999
REMARK 465 HIS D 3000
REMARK 465 MET D 3001
REMARK 465 ALA D 3002
REMARK 465 THR D 3155
REMARK 465 GLY D 3156
REMARK 465 LEU D 3157
REMARK 465 CYS D 3158
REMARK 465 SER D 3222
REMARK 465 ASN D 3223
REMARK 465 PHE D 3224
REMARK 465 ALA D 3225
REMARK 465 GLY D 3363
REMARK 465 ARG D 3364
REMARK 465 ARG D 3365
REMARK 465 GLU D 3366
REMARK 465 GLY D 3367
REMARK 465 HIS D 3368
REMARK 465 ALA D 3369
REMARK 465 GLN D 3370
REMARK 465 MET E 3981
REMARK 465 GLY E 3982
REMARK 465 SER E 3983
REMARK 465 SER E 3984
REMARK 465 HIS E 3985
REMARK 465 HIS E 3986
REMARK 465 HIS E 3987
REMARK 465 HIS E 3988
REMARK 465 HIS E 3989
REMARK 465 HIS E 3990
REMARK 465 SER E 3991
REMARK 465 SER E 3992
REMARK 465 GLY E 3993
REMARK 465 LEU E 3994
REMARK 465 VAL E 3995
REMARK 465 PRO E 3996
REMARK 465 ARG E 3997
REMARK 465 GLY E 3998
REMARK 465 SER E 3999
REMARK 465 HIS E 4000
REMARK 465 MET E 4001
REMARK 465 ALA E 4002
REMARK 465 THR E 4155
REMARK 465 GLY E 4156
REMARK 465 LEU E 4157
REMARK 465 CYS E 4158
REMARK 465 SER E 4222
REMARK 465 ASN E 4223
REMARK 465 PHE E 4224
REMARK 465 ALA E 4225
REMARK 465 GLY E 4363
REMARK 465 ARG E 4364
REMARK 465 ARG E 4365
REMARK 465 GLU E 4366
REMARK 465 GLY E 4367
REMARK 465 HIS E 4368
REMARK 465 ALA E 4369
REMARK 465 GLN E 4370
REMARK 465 MET F 4981
REMARK 465 GLY F 4982
REMARK 465 SER F 4983
REMARK 465 SER F 4984
REMARK 465 HIS F 4985
REMARK 465 HIS F 4986
REMARK 465 HIS F 4987
REMARK 465 HIS F 4988
REMARK 465 HIS F 4989
REMARK 465 HIS F 4990
REMARK 465 SER F 4991
REMARK 465 SER F 4992
REMARK 465 GLY F 4993
REMARK 465 LEU F 4994
REMARK 465 VAL F 4995
REMARK 465 PRO F 4996
REMARK 465 ARG F 4997
REMARK 465 GLY F 4998
REMARK 465 SER F 4999
REMARK 465 HIS F 5000
REMARK 465 MET F 5001
REMARK 465 ALA F 5002
REMARK 465 THR F 5155
REMARK 465 GLY F 5156
REMARK 465 LEU F 5157
REMARK 465 CYS F 5158
REMARK 465 SER F 5222
REMARK 465 ASN F 5223
REMARK 465 PHE F 5224
REMARK 465 ALA F 5225
REMARK 465 GLY F 5363
REMARK 465 ARG F 5364
REMARK 465 ARG F 5365
REMARK 465 GLU F 5366
REMARK 465 GLY F 5367
REMARK 465 HIS F 5368
REMARK 465 ALA F 5369
REMARK 465 GLN F 5370
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 O VAL B 1229 OH TYR B 1233 2.03
REMARK 500 O TRP C 2238 OH TYR C 2306 2.14
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 GLN A6004 92.06 -43.40
REMARK 500 PRO A6007 146.93 -35.62
REMARK 500 ASN A6014 82.14 -168.97
REMARK 500 LYS A6031 57.69 -106.45
REMARK 500 THR A6042 -24.00 -151.10
REMARK 500 ASN A6084 29.56 44.38
REMARK 500 LYS A6148 115.84 72.68
REMARK 500 SER A6149 81.67 -158.69
REMARK 500 GLN A6150 -155.50 -143.09
REMARK 500 VAL A6153 103.82 -169.92
REMARK 500 ASP A6160 -93.69 -167.22
REMARK 500 THR A6161 84.71 -168.20
REMARK 500 ARG A6162 101.39 74.53
REMARK 500 ASN A6163 78.80 -175.80
REMARK 500 ASN A6165 -34.40 -141.68
REMARK 500 SER A6184 -15.89 -152.83
REMARK 500 MET A6214 90.87 -54.95
REMARK 500 LEU A6215 47.72 -149.81
REMARK 500 GLU A6219 56.55 -140.98
REMARK 500 SER A6220 41.70 -96.28
REMARK 500 LEU A6227 76.88 70.99
REMARK 500 ALA A6240 -19.34 -49.32
REMARK 500 ASP A6253 -118.62 -116.77
REMARK 500 HIS A6255 51.22 -158.68
REMARK 500 LEU A6260 79.61 -113.67
REMARK 500 ASP A6265 -87.67 -119.42
REMARK 500 SER A6266 147.39 -5.61
REMARK 500 ASP A6279 -168.15 -57.17
REMARK 500 TRP A6317 69.11 -103.81
REMARK 500 HIS A6319 65.23 -172.23
REMARK 500 SER A6360 19.92 -65.44
REMARK 500 GLN B1004 91.26 -42.99
REMARK 500 PRO B1007 145.99 -35.20
REMARK 500 ASN B1014 77.41 -168.01
REMARK 500 LYS B1031 59.23 -107.00
REMARK 500 THR B1042 -29.37 -149.85
REMARK 500 CYS B1054 10.94 -69.01
REMARK 500 ASN B1084 26.06 48.23
REMARK 500 LYS B1148 116.07 71.58
REMARK 500 SER B1149 82.03 -158.28
REMARK 500 GLN B1150 -155.06 -143.30
REMARK 500 VAL B1153 102.76 -169.34
REMARK 500 ASP B1160 -150.80 -139.85
REMARK 500 ARG B1162 120.10 71.72
REMARK 500 ASN B1163 -12.22 -179.51
REMARK 500 ASN B1165 -39.21 -29.38
REMARK 500 SER B1184 -17.70 -153.02
REMARK 500 MET B1214 90.33 -54.91
REMARK 500 LEU B1215 50.02 -150.23
REMARK 500 GLU B1219 54.53 -140.46
REMARK 500
REMARK 500 THIS ENTRY HAS 186 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3DKB A 6001 6370 UNP P21580 TNAP3_HUMAN 1 370
DBREF 3DKB B 1001 1370 UNP P21580 TNAP3_HUMAN 1 370
DBREF 3DKB C 2001 2370 UNP P21580 TNAP3_HUMAN 1 370
DBREF 3DKB D 3001 3370 UNP P21580 TNAP3_HUMAN 1 370
DBREF 3DKB E 4001 4370 UNP P21580 TNAP3_HUMAN 1 370
DBREF 3DKB F 5001 5370 UNP P21580 TNAP3_HUMAN 1 370
SEQADV 3DKB MET A 5981 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY A 5982 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER A 5983 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER A 5984 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 5985 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 5986 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 5987 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 5988 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 5989 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 5990 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER A 5991 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER A 5992 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY A 5993 UNP P21580 EXPRESSION TAG
SEQADV 3DKB LEU A 5994 UNP P21580 EXPRESSION TAG
SEQADV 3DKB VAL A 5995 UNP P21580 EXPRESSION TAG
SEQADV 3DKB PRO A 5996 UNP P21580 EXPRESSION TAG
SEQADV 3DKB ARG A 5997 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY A 5998 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER A 5999 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS A 6000 UNP P21580 EXPRESSION TAG
SEQADV 3DKB MET B 981 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY B 982 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER B 983 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER B 984 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 985 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 986 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 987 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 988 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 989 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 990 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER B 991 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER B 992 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY B 993 UNP P21580 EXPRESSION TAG
SEQADV 3DKB LEU B 994 UNP P21580 EXPRESSION TAG
SEQADV 3DKB VAL B 995 UNP P21580 EXPRESSION TAG
SEQADV 3DKB PRO B 996 UNP P21580 EXPRESSION TAG
SEQADV 3DKB ARG B 997 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY B 998 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER B 999 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS B 1000 UNP P21580 EXPRESSION TAG
SEQADV 3DKB MET C 1981 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY C 1982 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER C 1983 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER C 1984 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 1985 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 1986 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 1987 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 1988 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 1989 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 1990 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER C 1991 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER C 1992 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY C 1993 UNP P21580 EXPRESSION TAG
SEQADV 3DKB LEU C 1994 UNP P21580 EXPRESSION TAG
SEQADV 3DKB VAL C 1995 UNP P21580 EXPRESSION TAG
SEQADV 3DKB PRO C 1996 UNP P21580 EXPRESSION TAG
SEQADV 3DKB ARG C 1997 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY C 1998 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER C 1999 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS C 2000 UNP P21580 EXPRESSION TAG
SEQADV 3DKB MET D 2981 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY D 2982 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER D 2983 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER D 2984 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 2985 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 2986 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 2987 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 2988 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 2989 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 2990 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER D 2991 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER D 2992 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY D 2993 UNP P21580 EXPRESSION TAG
SEQADV 3DKB LEU D 2994 UNP P21580 EXPRESSION TAG
SEQADV 3DKB VAL D 2995 UNP P21580 EXPRESSION TAG
SEQADV 3DKB PRO D 2996 UNP P21580 EXPRESSION TAG
SEQADV 3DKB ARG D 2997 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY D 2998 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER D 2999 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS D 3000 UNP P21580 EXPRESSION TAG
SEQADV 3DKB MET E 3981 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY E 3982 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER E 3983 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER E 3984 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 3985 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 3986 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 3987 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 3988 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 3989 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 3990 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER E 3991 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER E 3992 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY E 3993 UNP P21580 EXPRESSION TAG
SEQADV 3DKB LEU E 3994 UNP P21580 EXPRESSION TAG
SEQADV 3DKB VAL E 3995 UNP P21580 EXPRESSION TAG
SEQADV 3DKB PRO E 3996 UNP P21580 EXPRESSION TAG
SEQADV 3DKB ARG E 3997 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY E 3998 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER E 3999 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS E 4000 UNP P21580 EXPRESSION TAG
SEQADV 3DKB MET F 4981 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY F 4982 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER F 4983 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER F 4984 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 4985 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 4986 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 4987 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 4988 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 4989 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 4990 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER F 4991 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER F 4992 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY F 4993 UNP P21580 EXPRESSION TAG
SEQADV 3DKB LEU F 4994 UNP P21580 EXPRESSION TAG
SEQADV 3DKB VAL F 4995 UNP P21580 EXPRESSION TAG
SEQADV 3DKB PRO F 4996 UNP P21580 EXPRESSION TAG
SEQADV 3DKB ARG F 4997 UNP P21580 EXPRESSION TAG
SEQADV 3DKB GLY F 4998 UNP P21580 EXPRESSION TAG
SEQADV 3DKB SER F 4999 UNP P21580 EXPRESSION TAG
SEQADV 3DKB HIS F 5000 UNP P21580 EXPRESSION TAG
SEQRES 1 A 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 390 LEU VAL PRO ARG GLY SER HIS MET ALA GLU GLN VAL LEU
SEQRES 3 A 390 PRO GLN ALA LEU TYR LEU SER ASN MET ARG LYS ALA VAL
SEQRES 4 A 390 LYS ILE ARG GLU ARG THR PRO GLU ASP ILE PHE LYS PRO
SEQRES 5 A 390 THR ASN GLY ILE ILE HIS HIS PHE LYS THR MET HIS ARG
SEQRES 6 A 390 TYR THR LEU GLU MET PHE ARG THR CYS GLN PHE CYS PRO
SEQRES 7 A 390 GLN PHE ARG GLU ILE ILE HIS LYS ALA LEU ILE ASP ARG
SEQRES 8 A 390 ASN ILE GLN ALA THR LEU GLU SER GLN LYS LYS LEU ASN
SEQRES 9 A 390 TRP CYS ARG GLU VAL ARG LYS LEU VAL ALA LEU LYS THR
SEQRES 10 A 390 ASN GLY ASP GLY ASN CYS LEU MET HIS ALA THR SER GLN
SEQRES 11 A 390 TYR MET TRP GLY VAL GLN ASP THR ASP LEU VAL LEU ARG
SEQRES 12 A 390 LYS ALA LEU PHE SER THR LEU LYS GLU THR ASP THR ARG
SEQRES 13 A 390 ASN PHE LYS PHE ARG TRP GLN LEU GLU SER LEU LYS SER
SEQRES 14 A 390 GLN GLU PHE VAL GLU THR GLY LEU CYS TYR ASP THR ARG
SEQRES 15 A 390 ASN TRP ASN ASP GLU TRP ASP ASN LEU ILE LYS MET ALA
SEQRES 16 A 390 SER THR ASP THR PRO MET ALA ARG SER GLY LEU GLN TYR
SEQRES 17 A 390 ASN SER LEU GLU GLU ILE HIS ILE PHE VAL LEU CYS ASN
SEQRES 18 A 390 ILE LEU ARG ARG PRO ILE ILE VAL ILE SER ASP LYS MET
SEQRES 19 A 390 LEU ARG SER LEU GLU SER GLY SER ASN PHE ALA PRO LEU
SEQRES 20 A 390 LYS VAL GLY GLY ILE TYR LEU PRO LEU HIS TRP PRO ALA
SEQRES 21 A 390 GLN GLU CYS TYR ARG TYR PRO ILE VAL LEU GLY TYR ASP
SEQRES 22 A 390 SER HIS HIS PHE VAL PRO LEU VAL THR LEU LYS ASP SER
SEQRES 23 A 390 GLY PRO GLU ILE ARG ALA VAL PRO LEU VAL ASN ARG ASP
SEQRES 24 A 390 ARG GLY ARG PHE GLU ASP LEU LYS VAL HIS PHE LEU THR
SEQRES 25 A 390 ASP PRO GLU ASN GLU MET LYS GLU LYS LEU LEU LYS GLU
SEQRES 26 A 390 TYR LEU MET VAL ILE GLU ILE PRO VAL GLN GLY TRP ASP
SEQRES 27 A 390 HIS GLY THR THR HIS LEU ILE ASN ALA ALA LYS LEU ASP
SEQRES 28 A 390 GLU ALA ASN LEU PRO LYS GLU ILE ASN LEU VAL ASP ASP
SEQRES 29 A 390 TYR PHE GLU LEU VAL GLN HIS GLU TYR LYS LYS TRP GLN
SEQRES 30 A 390 GLU ASN SER GLU GLN GLY ARG ARG GLU GLY HIS ALA GLN
SEQRES 1 B 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 390 LEU VAL PRO ARG GLY SER HIS MET ALA GLU GLN VAL LEU
SEQRES 3 B 390 PRO GLN ALA LEU TYR LEU SER ASN MET ARG LYS ALA VAL
SEQRES 4 B 390 LYS ILE ARG GLU ARG THR PRO GLU ASP ILE PHE LYS PRO
SEQRES 5 B 390 THR ASN GLY ILE ILE HIS HIS PHE LYS THR MET HIS ARG
SEQRES 6 B 390 TYR THR LEU GLU MET PHE ARG THR CYS GLN PHE CYS PRO
SEQRES 7 B 390 GLN PHE ARG GLU ILE ILE HIS LYS ALA LEU ILE ASP ARG
SEQRES 8 B 390 ASN ILE GLN ALA THR LEU GLU SER GLN LYS LYS LEU ASN
SEQRES 9 B 390 TRP CYS ARG GLU VAL ARG LYS LEU VAL ALA LEU LYS THR
SEQRES 10 B 390 ASN GLY ASP GLY ASN CYS LEU MET HIS ALA THR SER GLN
SEQRES 11 B 390 TYR MET TRP GLY VAL GLN ASP THR ASP LEU VAL LEU ARG
SEQRES 12 B 390 LYS ALA LEU PHE SER THR LEU LYS GLU THR ASP THR ARG
SEQRES 13 B 390 ASN PHE LYS PHE ARG TRP GLN LEU GLU SER LEU LYS SER
SEQRES 14 B 390 GLN GLU PHE VAL GLU THR GLY LEU CYS TYR ASP THR ARG
SEQRES 15 B 390 ASN TRP ASN ASP GLU TRP ASP ASN LEU ILE LYS MET ALA
SEQRES 16 B 390 SER THR ASP THR PRO MET ALA ARG SER GLY LEU GLN TYR
SEQRES 17 B 390 ASN SER LEU GLU GLU ILE HIS ILE PHE VAL LEU CYS ASN
SEQRES 18 B 390 ILE LEU ARG ARG PRO ILE ILE VAL ILE SER ASP LYS MET
SEQRES 19 B 390 LEU ARG SER LEU GLU SER GLY SER ASN PHE ALA PRO LEU
SEQRES 20 B 390 LYS VAL GLY GLY ILE TYR LEU PRO LEU HIS TRP PRO ALA
SEQRES 21 B 390 GLN GLU CYS TYR ARG TYR PRO ILE VAL LEU GLY TYR ASP
SEQRES 22 B 390 SER HIS HIS PHE VAL PRO LEU VAL THR LEU LYS ASP SER
SEQRES 23 B 390 GLY PRO GLU ILE ARG ALA VAL PRO LEU VAL ASN ARG ASP
SEQRES 24 B 390 ARG GLY ARG PHE GLU ASP LEU LYS VAL HIS PHE LEU THR
SEQRES 25 B 390 ASP PRO GLU ASN GLU MET LYS GLU LYS LEU LEU LYS GLU
SEQRES 26 B 390 TYR LEU MET VAL ILE GLU ILE PRO VAL GLN GLY TRP ASP
SEQRES 27 B 390 HIS GLY THR THR HIS LEU ILE ASN ALA ALA LYS LEU ASP
SEQRES 28 B 390 GLU ALA ASN LEU PRO LYS GLU ILE ASN LEU VAL ASP ASP
SEQRES 29 B 390 TYR PHE GLU LEU VAL GLN HIS GLU TYR LYS LYS TRP GLN
SEQRES 30 B 390 GLU ASN SER GLU GLN GLY ARG ARG GLU GLY HIS ALA GLN
SEQRES 1 C 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 390 LEU VAL PRO ARG GLY SER HIS MET ALA GLU GLN VAL LEU
SEQRES 3 C 390 PRO GLN ALA LEU TYR LEU SER ASN MET ARG LYS ALA VAL
SEQRES 4 C 390 LYS ILE ARG GLU ARG THR PRO GLU ASP ILE PHE LYS PRO
SEQRES 5 C 390 THR ASN GLY ILE ILE HIS HIS PHE LYS THR MET HIS ARG
SEQRES 6 C 390 TYR THR LEU GLU MET PHE ARG THR CYS GLN PHE CYS PRO
SEQRES 7 C 390 GLN PHE ARG GLU ILE ILE HIS LYS ALA LEU ILE ASP ARG
SEQRES 8 C 390 ASN ILE GLN ALA THR LEU GLU SER GLN LYS LYS LEU ASN
SEQRES 9 C 390 TRP CYS ARG GLU VAL ARG LYS LEU VAL ALA LEU LYS THR
SEQRES 10 C 390 ASN GLY ASP GLY ASN CYS LEU MET HIS ALA THR SER GLN
SEQRES 11 C 390 TYR MET TRP GLY VAL GLN ASP THR ASP LEU VAL LEU ARG
SEQRES 12 C 390 LYS ALA LEU PHE SER THR LEU LYS GLU THR ASP THR ARG
SEQRES 13 C 390 ASN PHE LYS PHE ARG TRP GLN LEU GLU SER LEU LYS SER
SEQRES 14 C 390 GLN GLU PHE VAL GLU THR GLY LEU CYS TYR ASP THR ARG
SEQRES 15 C 390 ASN TRP ASN ASP GLU TRP ASP ASN LEU ILE LYS MET ALA
SEQRES 16 C 390 SER THR ASP THR PRO MET ALA ARG SER GLY LEU GLN TYR
SEQRES 17 C 390 ASN SER LEU GLU GLU ILE HIS ILE PHE VAL LEU CYS ASN
SEQRES 18 C 390 ILE LEU ARG ARG PRO ILE ILE VAL ILE SER ASP LYS MET
SEQRES 19 C 390 LEU ARG SER LEU GLU SER GLY SER ASN PHE ALA PRO LEU
SEQRES 20 C 390 LYS VAL GLY GLY ILE TYR LEU PRO LEU HIS TRP PRO ALA
SEQRES 21 C 390 GLN GLU CYS TYR ARG TYR PRO ILE VAL LEU GLY TYR ASP
SEQRES 22 C 390 SER HIS HIS PHE VAL PRO LEU VAL THR LEU LYS ASP SER
SEQRES 23 C 390 GLY PRO GLU ILE ARG ALA VAL PRO LEU VAL ASN ARG ASP
SEQRES 24 C 390 ARG GLY ARG PHE GLU ASP LEU LYS VAL HIS PHE LEU THR
SEQRES 25 C 390 ASP PRO GLU ASN GLU MET LYS GLU LYS LEU LEU LYS GLU
SEQRES 26 C 390 TYR LEU MET VAL ILE GLU ILE PRO VAL GLN GLY TRP ASP
SEQRES 27 C 390 HIS GLY THR THR HIS LEU ILE ASN ALA ALA LYS LEU ASP
SEQRES 28 C 390 GLU ALA ASN LEU PRO LYS GLU ILE ASN LEU VAL ASP ASP
SEQRES 29 C 390 TYR PHE GLU LEU VAL GLN HIS GLU TYR LYS LYS TRP GLN
SEQRES 30 C 390 GLU ASN SER GLU GLN GLY ARG ARG GLU GLY HIS ALA GLN
SEQRES 1 D 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 390 LEU VAL PRO ARG GLY SER HIS MET ALA GLU GLN VAL LEU
SEQRES 3 D 390 PRO GLN ALA LEU TYR LEU SER ASN MET ARG LYS ALA VAL
SEQRES 4 D 390 LYS ILE ARG GLU ARG THR PRO GLU ASP ILE PHE LYS PRO
SEQRES 5 D 390 THR ASN GLY ILE ILE HIS HIS PHE LYS THR MET HIS ARG
SEQRES 6 D 390 TYR THR LEU GLU MET PHE ARG THR CYS GLN PHE CYS PRO
SEQRES 7 D 390 GLN PHE ARG GLU ILE ILE HIS LYS ALA LEU ILE ASP ARG
SEQRES 8 D 390 ASN ILE GLN ALA THR LEU GLU SER GLN LYS LYS LEU ASN
SEQRES 9 D 390 TRP CYS ARG GLU VAL ARG LYS LEU VAL ALA LEU LYS THR
SEQRES 10 D 390 ASN GLY ASP GLY ASN CYS LEU MET HIS ALA THR SER GLN
SEQRES 11 D 390 TYR MET TRP GLY VAL GLN ASP THR ASP LEU VAL LEU ARG
SEQRES 12 D 390 LYS ALA LEU PHE SER THR LEU LYS GLU THR ASP THR ARG
SEQRES 13 D 390 ASN PHE LYS PHE ARG TRP GLN LEU GLU SER LEU LYS SER
SEQRES 14 D 390 GLN GLU PHE VAL GLU THR GLY LEU CYS TYR ASP THR ARG
SEQRES 15 D 390 ASN TRP ASN ASP GLU TRP ASP ASN LEU ILE LYS MET ALA
SEQRES 16 D 390 SER THR ASP THR PRO MET ALA ARG SER GLY LEU GLN TYR
SEQRES 17 D 390 ASN SER LEU GLU GLU ILE HIS ILE PHE VAL LEU CYS ASN
SEQRES 18 D 390 ILE LEU ARG ARG PRO ILE ILE VAL ILE SER ASP LYS MET
SEQRES 19 D 390 LEU ARG SER LEU GLU SER GLY SER ASN PHE ALA PRO LEU
SEQRES 20 D 390 LYS VAL GLY GLY ILE TYR LEU PRO LEU HIS TRP PRO ALA
SEQRES 21 D 390 GLN GLU CYS TYR ARG TYR PRO ILE VAL LEU GLY TYR ASP
SEQRES 22 D 390 SER HIS HIS PHE VAL PRO LEU VAL THR LEU LYS ASP SER
SEQRES 23 D 390 GLY PRO GLU ILE ARG ALA VAL PRO LEU VAL ASN ARG ASP
SEQRES 24 D 390 ARG GLY ARG PHE GLU ASP LEU LYS VAL HIS PHE LEU THR
SEQRES 25 D 390 ASP PRO GLU ASN GLU MET LYS GLU LYS LEU LEU LYS GLU
SEQRES 26 D 390 TYR LEU MET VAL ILE GLU ILE PRO VAL GLN GLY TRP ASP
SEQRES 27 D 390 HIS GLY THR THR HIS LEU ILE ASN ALA ALA LYS LEU ASP
SEQRES 28 D 390 GLU ALA ASN LEU PRO LYS GLU ILE ASN LEU VAL ASP ASP
SEQRES 29 D 390 TYR PHE GLU LEU VAL GLN HIS GLU TYR LYS LYS TRP GLN
SEQRES 30 D 390 GLU ASN SER GLU GLN GLY ARG ARG GLU GLY HIS ALA GLN
SEQRES 1 E 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 390 LEU VAL PRO ARG GLY SER HIS MET ALA GLU GLN VAL LEU
SEQRES 3 E 390 PRO GLN ALA LEU TYR LEU SER ASN MET ARG LYS ALA VAL
SEQRES 4 E 390 LYS ILE ARG GLU ARG THR PRO GLU ASP ILE PHE LYS PRO
SEQRES 5 E 390 THR ASN GLY ILE ILE HIS HIS PHE LYS THR MET HIS ARG
SEQRES 6 E 390 TYR THR LEU GLU MET PHE ARG THR CYS GLN PHE CYS PRO
SEQRES 7 E 390 GLN PHE ARG GLU ILE ILE HIS LYS ALA LEU ILE ASP ARG
SEQRES 8 E 390 ASN ILE GLN ALA THR LEU GLU SER GLN LYS LYS LEU ASN
SEQRES 9 E 390 TRP CYS ARG GLU VAL ARG LYS LEU VAL ALA LEU LYS THR
SEQRES 10 E 390 ASN GLY ASP GLY ASN CYS LEU MET HIS ALA THR SER GLN
SEQRES 11 E 390 TYR MET TRP GLY VAL GLN ASP THR ASP LEU VAL LEU ARG
SEQRES 12 E 390 LYS ALA LEU PHE SER THR LEU LYS GLU THR ASP THR ARG
SEQRES 13 E 390 ASN PHE LYS PHE ARG TRP GLN LEU GLU SER LEU LYS SER
SEQRES 14 E 390 GLN GLU PHE VAL GLU THR GLY LEU CYS TYR ASP THR ARG
SEQRES 15 E 390 ASN TRP ASN ASP GLU TRP ASP ASN LEU ILE LYS MET ALA
SEQRES 16 E 390 SER THR ASP THR PRO MET ALA ARG SER GLY LEU GLN TYR
SEQRES 17 E 390 ASN SER LEU GLU GLU ILE HIS ILE PHE VAL LEU CYS ASN
SEQRES 18 E 390 ILE LEU ARG ARG PRO ILE ILE VAL ILE SER ASP LYS MET
SEQRES 19 E 390 LEU ARG SER LEU GLU SER GLY SER ASN PHE ALA PRO LEU
SEQRES 20 E 390 LYS VAL GLY GLY ILE TYR LEU PRO LEU HIS TRP PRO ALA
SEQRES 21 E 390 GLN GLU CYS TYR ARG TYR PRO ILE VAL LEU GLY TYR ASP
SEQRES 22 E 390 SER HIS HIS PHE VAL PRO LEU VAL THR LEU LYS ASP SER
SEQRES 23 E 390 GLY PRO GLU ILE ARG ALA VAL PRO LEU VAL ASN ARG ASP
SEQRES 24 E 390 ARG GLY ARG PHE GLU ASP LEU LYS VAL HIS PHE LEU THR
SEQRES 25 E 390 ASP PRO GLU ASN GLU MET LYS GLU LYS LEU LEU LYS GLU
SEQRES 26 E 390 TYR LEU MET VAL ILE GLU ILE PRO VAL GLN GLY TRP ASP
SEQRES 27 E 390 HIS GLY THR THR HIS LEU ILE ASN ALA ALA LYS LEU ASP
SEQRES 28 E 390 GLU ALA ASN LEU PRO LYS GLU ILE ASN LEU VAL ASP ASP
SEQRES 29 E 390 TYR PHE GLU LEU VAL GLN HIS GLU TYR LYS LYS TRP GLN
SEQRES 30 E 390 GLU ASN SER GLU GLN GLY ARG ARG GLU GLY HIS ALA GLN
SEQRES 1 F 390 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 390 LEU VAL PRO ARG GLY SER HIS MET ALA GLU GLN VAL LEU
SEQRES 3 F 390 PRO GLN ALA LEU TYR LEU SER ASN MET ARG LYS ALA VAL
SEQRES 4 F 390 LYS ILE ARG GLU ARG THR PRO GLU ASP ILE PHE LYS PRO
SEQRES 5 F 390 THR ASN GLY ILE ILE HIS HIS PHE LYS THR MET HIS ARG
SEQRES 6 F 390 TYR THR LEU GLU MET PHE ARG THR CYS GLN PHE CYS PRO
SEQRES 7 F 390 GLN PHE ARG GLU ILE ILE HIS LYS ALA LEU ILE ASP ARG
SEQRES 8 F 390 ASN ILE GLN ALA THR LEU GLU SER GLN LYS LYS LEU ASN
SEQRES 9 F 390 TRP CYS ARG GLU VAL ARG LYS LEU VAL ALA LEU LYS THR
SEQRES 10 F 390 ASN GLY ASP GLY ASN CYS LEU MET HIS ALA THR SER GLN
SEQRES 11 F 390 TYR MET TRP GLY VAL GLN ASP THR ASP LEU VAL LEU ARG
SEQRES 12 F 390 LYS ALA LEU PHE SER THR LEU LYS GLU THR ASP THR ARG
SEQRES 13 F 390 ASN PHE LYS PHE ARG TRP GLN LEU GLU SER LEU LYS SER
SEQRES 14 F 390 GLN GLU PHE VAL GLU THR GLY LEU CYS TYR ASP THR ARG
SEQRES 15 F 390 ASN TRP ASN ASP GLU TRP ASP ASN LEU ILE LYS MET ALA
SEQRES 16 F 390 SER THR ASP THR PRO MET ALA ARG SER GLY LEU GLN TYR
SEQRES 17 F 390 ASN SER LEU GLU GLU ILE HIS ILE PHE VAL LEU CYS ASN
SEQRES 18 F 390 ILE LEU ARG ARG PRO ILE ILE VAL ILE SER ASP LYS MET
SEQRES 19 F 390 LEU ARG SER LEU GLU SER GLY SER ASN PHE ALA PRO LEU
SEQRES 20 F 390 LYS VAL GLY GLY ILE TYR LEU PRO LEU HIS TRP PRO ALA
SEQRES 21 F 390 GLN GLU CYS TYR ARG TYR PRO ILE VAL LEU GLY TYR ASP
SEQRES 22 F 390 SER HIS HIS PHE VAL PRO LEU VAL THR LEU LYS ASP SER
SEQRES 23 F 390 GLY PRO GLU ILE ARG ALA VAL PRO LEU VAL ASN ARG ASP
SEQRES 24 F 390 ARG GLY ARG PHE GLU ASP LEU LYS VAL HIS PHE LEU THR
SEQRES 25 F 390 ASP PRO GLU ASN GLU MET LYS GLU LYS LEU LEU LYS GLU
SEQRES 26 F 390 TYR LEU MET VAL ILE GLU ILE PRO VAL GLN GLY TRP ASP
SEQRES 27 F 390 HIS GLY THR THR HIS LEU ILE ASN ALA ALA LYS LEU ASP
SEQRES 28 F 390 GLU ALA ASN LEU PRO LYS GLU ILE ASN LEU VAL ASP ASP
SEQRES 29 F 390 TYR PHE GLU LEU VAL GLN HIS GLU TYR LYS LYS TRP GLN
SEQRES 30 F 390 GLU ASN SER GLU GLN GLY ARG ARG GLU GLY HIS ALA GLN
HELIX 1 1 ALA A 6009 SER A 6013 5 5
HELIX 2 2 ASN A 6014 ASP A 6028 1 15
HELIX 3 3 THR A 6042 TYR A 6046 5 5
HELIX 4 4 CYS A 6057 ILE A 6069 1 13
HELIX 5 5 ASP A 6070 GLN A 6080 1 11
HELIX 6 6 ASN A 6102 GLY A 6114 1 13
HELIX 7 7 LEU A 6120 THR A 6133 1 14
HELIX 8 8 THR A 6135 LYS A 6148 1 14
HELIX 9 9 ASN A 6165 ALA A 6175 1 11
HELIX 10 10 GLU A 6192 LEU A 6203 1 12
HELIX 11 11 THR A 6292 MET A 6298 1 7
HELIX 12 12 MET A 6298 LEU A 6307 1 10
HELIX 13 13 PRO A 6336 ILE A 6339 5 4
HELIX 14 14 ASN A 6340 GLU A 6358 1 19
HELIX 15 15 ASN A 6359 GLN A 6362 5 4
HELIX 16 16 ALA B 1009 SER B 1013 5 5
HELIX 17 17 ASN B 1014 ASP B 1028 1 15
HELIX 18 18 THR B 1042 TYR B 1046 5 5
HELIX 19 19 CYS B 1057 ILE B 1069 1 13
HELIX 20 20 ASP B 1070 GLN B 1080 1 11
HELIX 21 21 ASN B 1102 GLY B 1114 1 13
HELIX 22 22 LEU B 1120 THR B 1133 1 14
HELIX 23 23 THR B 1135 LYS B 1148 1 14
HELIX 24 24 ASN B 1163 ALA B 1175 1 13
HELIX 25 25 GLU B 1192 LEU B 1203 1 12
HELIX 26 26 THR B 1292 MET B 1298 1 7
HELIX 27 27 MET B 1298 LEU B 1307 1 10
HELIX 28 28 PRO B 1336 ILE B 1339 5 4
HELIX 29 29 ASN B 1340 GLU B 1358 1 19
HELIX 30 30 ASN B 1359 GLN B 1362 5 4
HELIX 31 31 ALA C 2009 SER C 2013 5 5
HELIX 32 32 ASN C 2014 ASP C 2028 1 15
HELIX 33 33 THR C 2042 TYR C 2046 5 5
HELIX 34 34 CYS C 2057 ILE C 2069 1 13
HELIX 35 35 ASP C 2070 GLN C 2080 1 11
HELIX 36 36 ASN C 2102 GLY C 2114 1 13
HELIX 37 37 LEU C 2120 THR C 2133 1 14
HELIX 38 38 THR C 2135 LYS C 2148 1 14
HELIX 39 39 ASN C 2163 ALA C 2175 1 13
HELIX 40 40 GLU C 2192 ARG C 2204 1 13
HELIX 41 41 THR C 2292 MET C 2298 1 7
HELIX 42 42 MET C 2298 LEU C 2307 1 10
HELIX 43 43 PRO C 2336 ILE C 2339 5 4
HELIX 44 44 ASN C 2340 GLU C 2358 1 19
HELIX 45 45 ASN C 2359 GLN C 2362 5 4
HELIX 46 46 ALA D 3009 SER D 3013 5 5
HELIX 47 47 ASN D 3014 ASP D 3028 1 15
HELIX 48 48 THR D 3042 TYR D 3046 5 5
HELIX 49 49 CYS D 3057 ILE D 3069 1 13
HELIX 50 50 ASP D 3070 GLN D 3080 1 11
HELIX 51 51 ASN D 3102 GLY D 3114 1 13
HELIX 52 52 LEU D 3120 THR D 3133 1 14
HELIX 53 53 THR D 3135 LYS D 3148 1 14
HELIX 54 54 ASN D 3163 ALA D 3175 1 13
HELIX 55 55 GLU D 3192 LEU D 3203 1 12
HELIX 56 56 THR D 3292 MET D 3298 1 7
HELIX 57 57 MET D 3298 LEU D 3307 1 10
HELIX 58 58 PRO D 3336 ILE D 3339 5 4
HELIX 59 59 ASN D 3340 GLU D 3358 1 19
HELIX 60 60 ASN D 3359 GLN D 3362 5 4
HELIX 61 61 ALA E 4009 SER E 4013 5 5
HELIX 62 62 ASN E 4014 ASP E 4028 1 15
HELIX 63 63 THR E 4042 TYR E 4046 5 5
HELIX 64 64 CYS E 4057 ILE E 4069 1 13
HELIX 65 65 ASP E 4070 GLN E 4080 1 11
HELIX 66 66 ASN E 4102 GLY E 4114 1 13
HELIX 67 67 LEU E 4120 THR E 4133 1 14
HELIX 68 68 THR E 4135 LYS E 4148 1 14
HELIX 69 69 ASP E 4166 ALA E 4175 1 10
HELIX 70 70 GLU E 4192 ARG E 4204 1 13
HELIX 71 71 THR E 4292 MET E 4298 1 7
HELIX 72 72 MET E 4298 LEU E 4307 1 10
HELIX 73 73 PRO E 4336 ILE E 4339 5 4
HELIX 74 74 ASN E 4340 GLU E 4358 1 19
HELIX 75 75 ASN E 4359 GLN E 4362 5 4
HELIX 76 76 ALA F 5009 SER F 5013 5 5
HELIX 77 77 ASN F 5014 ASP F 5028 1 15
HELIX 78 78 THR F 5042 TYR F 5046 5 5
HELIX 79 79 CYS F 5057 ILE F 5069 1 13
HELIX 80 80 ASP F 5070 GLN F 5080 1 11
HELIX 81 81 ASN F 5102 GLY F 5114 1 13
HELIX 82 82 LEU F 5120 THR F 5133 1 14
HELIX 83 83 THR F 5135 LYS F 5148 1 14
HELIX 84 84 ASP F 5166 ALA F 5175 1 10
HELIX 85 85 GLU F 5192 ARG F 5204 1 13
HELIX 86 86 THR F 5292 MET F 5298 1 7
HELIX 87 87 MET F 5298 LEU F 5307 1 10
HELIX 88 88 PRO F 5336 ILE F 5339 5 4
HELIX 89 89 ASN F 5340 GLU F 5358 1 19
HELIX 90 90 ASN F 5359 GLN F 5362 5 4
SHEET 1 A 2 ILE A6029 PHE A6030 0
SHEET 2 A 2 HIS A6039 PHE A6040 -1 O HIS A6039 N PHE A6030
SHEET 1 B 5 LEU A6092 ALA A6094 0
SHEET 2 B 5 PHE A6257 THR A6262 -1 O VAL A6261 N VAL A6093
SHEET 3 B 5 ILE A6248 TYR A6252 -1 N GLY A6251 O VAL A6258
SHEET 4 B 5 ILE A6207 SER A6211 1 N ILE A6210 O LEU A6250
SHEET 5 B 5 GLY A6231 TYR A6233 -1 O TYR A6233 N ILE A6207
SHEET 1 C 3 ALA A6272 PRO A6274 0
SHEET 2 C 3 THR A6322 LYS A6329 -1 O ALA A6328 N VAL A6273
SHEET 3 C 3 VAL A6309 GLN A6315 -1 N ILE A6312 O ILE A6325
SHEET 1 D 2 VAL A6276 ARG A6278 0
SHEET 2 D 2 PHE A6283 ASP A6285 -1 O GLU A6284 N ASN A6277
SHEET 1 E 2 ILE B1029 PHE B1030 0
SHEET 2 E 2 HIS B1039 PHE B1040 -1 O HIS B1039 N PHE B1030
SHEET 1 F 5 LEU B1092 ALA B1094 0
SHEET 2 F 5 PHE B1257 THR B1262 -1 O VAL B1261 N VAL B1093
SHEET 3 F 5 ILE B1248 TYR B1252 -1 N GLY B1251 O VAL B1258
SHEET 4 F 5 ILE B1207 SER B1211 1 N ILE B1208 O ILE B1248
SHEET 5 F 5 GLY B1231 TYR B1233 -1 O TYR B1233 N ILE B1207
SHEET 1 G 3 ALA B1272 PRO B1274 0
SHEET 2 G 3 THR B1322 LYS B1329 -1 O ALA B1328 N VAL B1273
SHEET 3 G 3 VAL B1309 GLN B1315 -1 N ILE B1312 O ILE B1325
SHEET 1 H 2 VAL B1276 ARG B1278 0
SHEET 2 H 2 PHE B1283 ASP B1285 -1 O GLU B1284 N ASN B1277
SHEET 1 I 2 ILE C2029 PHE C2030 0
SHEET 2 I 2 HIS C2039 PHE C2040 -1 O HIS C2039 N PHE C2030
SHEET 1 J 5 LEU C2092 ALA C2094 0
SHEET 2 J 5 PHE C2257 THR C2262 -1 O VAL C2261 N VAL C2093
SHEET 3 J 5 ILE C2248 TYR C2252 -1 N GLY C2251 O VAL C2258
SHEET 4 J 5 ILE C2207 SER C2211 1 N ILE C2208 O ILE C2248
SHEET 5 J 5 GLY C2231 TYR C2233 -1 O TYR C2233 N ILE C2207
SHEET 1 K 3 ALA C2272 PRO C2274 0
SHEET 2 K 3 THR C2322 LYS C2329 -1 O ALA C2328 N VAL C2273
SHEET 3 K 3 VAL C2309 GLN C2315 -1 N ILE C2312 O ILE C2325
SHEET 1 L 2 VAL C2276 ARG C2278 0
SHEET 2 L 2 PHE C2283 ASP C2285 -1 O GLU C2284 N ASN C2277
SHEET 1 M 2 ILE D3029 PHE D3030 0
SHEET 2 M 2 HIS D3039 PHE D3040 -1 O HIS D3039 N PHE D3030
SHEET 1 N 5 LEU D3092 ALA D3094 0
SHEET 2 N 5 PHE D3257 THR D3262 -1 O VAL D3261 N VAL D3093
SHEET 3 N 5 ILE D3248 TYR D3252 -1 N GLY D3251 O VAL D3258
SHEET 4 N 5 ILE D3207 SER D3211 1 N ILE D3210 O LEU D3250
SHEET 5 N 5 GLY D3231 TYR D3233 -1 O TYR D3233 N ILE D3207
SHEET 1 O 3 ALA D3272 PRO D3274 0
SHEET 2 O 3 THR D3322 LYS D3329 -1 O ALA D3328 N VAL D3273
SHEET 3 O 3 VAL D3309 GLN D3315 -1 N VAL D3314 O HIS D3323
SHEET 1 P 2 VAL D3276 ARG D3278 0
SHEET 2 P 2 PHE D3283 ASP D3285 -1 O GLU D3284 N ASN D3277
SHEET 1 Q 2 ILE E4029 PHE E4030 0
SHEET 2 Q 2 HIS E4039 PHE E4040 -1 O HIS E4039 N PHE E4030
SHEET 1 R 5 LEU E4092 ALA E4094 0
SHEET 2 R 5 PHE E4257 THR E4262 -1 O VAL E4261 N VAL E4093
SHEET 3 R 5 ILE E4248 TYR E4252 -1 N GLY E4251 O VAL E4258
SHEET 4 R 5 ILE E4207 SER E4211 1 N ILE E4208 O ILE E4248
SHEET 5 R 5 GLY E4231 TYR E4233 -1 O TYR E4233 N ILE E4207
SHEET 1 S 3 ALA E4272 PRO E4274 0
SHEET 2 S 3 THR E4322 LYS E4329 -1 O ALA E4328 N VAL E4273
SHEET 3 S 3 VAL E4309 GLN E4315 -1 N ILE E4312 O ILE E4325
SHEET 1 T 2 VAL E4276 ARG E4278 0
SHEET 2 T 2 PHE E4283 ASP E4285 -1 O GLU E4284 N ASN E4277
SHEET 1 U 2 ILE F5029 PHE F5030 0
SHEET 2 U 2 HIS F5039 PHE F5040 -1 O HIS F5039 N PHE F5030
SHEET 1 V 5 LEU F5092 ALA F5094 0
SHEET 2 V 5 PHE F5257 THR F5262 -1 O VAL F5261 N VAL F5093
SHEET 3 V 5 ILE F5248 TYR F5252 -1 N GLY F5251 O VAL F5258
SHEET 4 V 5 ILE F5207 SER F5211 1 N ILE F5208 O ILE F5248
SHEET 5 V 5 GLY F5231 TYR F5233 -1 O TYR F5233 N ILE F5207
SHEET 1 W 3 ALA F5272 PRO F5274 0
SHEET 2 W 3 THR F5322 LYS F5329 -1 O ALA F5328 N VAL F5273
SHEET 3 W 3 VAL F5309 GLN F5315 -1 N ILE F5312 O ILE F5325
SHEET 1 X 2 VAL F5276 ARG F5278 0
SHEET 2 X 2 PHE F5283 ASP F5285 -1 O GLU F5284 N ASN F5277
CRYST1 123.636 123.636 143.043 90.00 90.00 120.00 P 32 18
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 0.008088 0.004670 0.000000 0.00000
SCALE2 0.000000 0.009340 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006991 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
