HEADER HYDROLASE 21-FEB-06 2G49
TITLE CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME IN COMPLEX WITH
TITLE 2 GLUCAGON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-DEGRADING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: INSULYSIN, INSULINASE, INSULIN PROTEASE;
COMPND 5 EC: 3.4.24.56;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GLUCAGON PREPROPROTEIN;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: RESIDUES 53-81;
COMPND 12 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: IDE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO SAPIENS
SOURCE 14 (HUMAN).
KEYWDS PROTEIN-PEPTIDE COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SHEN,W.-J.TANG
REVDAT 4 14-FEB-24 2G49 1 REMARK
REVDAT 3 20-OCT-21 2G49 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2G49 1 VERSN
REVDAT 1 24-OCT-06 2G49 0
JRNL AUTH Y.SHEN,A.JOACHIMIAK,M.R.ROSNER,W.J.TANG
JRNL TITL STRUCTURES OF HUMAN INSULIN-DEGRADING ENZYME REVEAL A NEW
JRNL TITL 2 SUBSTRATE RECOGNITION MECHANISM.
JRNL REF NATURE V. 443 870 2006
JRNL REFN ISSN 0028-0836
JRNL PMID 17051221
JRNL DOI 10.1038/NATURE05143
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 78511.370
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 119984
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) : 0.198
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11969
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 16626
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1829
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15931
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 695
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.37000
REMARK 3 B22 (A**2) : -1.37000
REMARK 3 B33 (A**2) : 2.74000
REMARK 3 B12 (A**2) : 3.65000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 1.190 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.200 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.350 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 35.94
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 : DOX.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : DOX.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2G49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123701
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.6000
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) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME5000, DIOXANE, TACISMATE, HEPES,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 60.52533
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 30.26267
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.39400
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 15.13133
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.65667
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
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 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 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 GLY A 39
REMARK 465 ILE A 40
REMARK 465 PRO A 41
REMARK 465 MET A 42
REMARK 465 PHE A 972
REMARK 465 PRO A 973
REMARK 465 CYS A 974
REMARK 465 GLN A 975
REMARK 465 ALA A 1017
REMARK 465 LYS A 1018
REMARK 465 LEU A 1019
REMARK 465 MET B 30
REMARK 465 HIS B 31
REMARK 465 HIS B 32
REMARK 465 HIS B 33
REMARK 465 HIS B 34
REMARK 465 HIS B 35
REMARK 465 HIS B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 GLY B 39
REMARK 465 ILE B 40
REMARK 465 PRO B 41
REMARK 465 MET B 42
REMARK 465 ASN B 43
REMARK 465 PRO B 973
REMARK 465 CYS B 974
REMARK 465 GLN B 975
REMARK 465 ASN B 976
REMARK 465 ASP B 977
REMARK 465 MET B 1015
REMARK 465 ALA B 1016
REMARK 465 ALA B 1017
REMARK 465 LYS B 1018
REMARK 465 LEU B 1019
REMARK 465 THR C 5
REMARK 465 PHE C 6
REMARK 465 THR C 7
REMARK 465 SER C 8
REMARK 465 ASP C 9
REMARK 465 TYR C 10
REMARK 465 SER C 11
REMARK 465 LYS C 12
REMARK 465 TYR C 13
REMARK 465 LEU C 14
REMARK 465 ASP C 15
REMARK 465 SER C 16
REMARK 465 ARG C 17
REMARK 465 ARG C 18
REMARK 465 ALA C 19
REMARK 465 GLN C 20
REMARK 465 ASP C 21
REMARK 465 THR C 29
REMARK 465 GLY D 4
REMARK 465 THR D 5
REMARK 465 PHE D 6
REMARK 465 THR D 7
REMARK 465 SER D 8
REMARK 465 ASP D 9
REMARK 465 TYR D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 TYR D 13
REMARK 465 LEU D 14
REMARK 465 ASP D 15
REMARK 465 SER D 16
REMARK 465 ARG D 17
REMARK 465 ARG D 18
REMARK 465 ALA D 19
REMARK 465 GLN D 20
REMARK 465 ASP D 21
REMARK 465 ASN D 28
REMARK 465 THR D 29
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 ASP A 964 CG OD1 OD2
REMARK 470 SER A 965 OG
REMARK 470 GLU A 971 CG CD OE1 OE2
REMARK 470 ASN A 976 CG OD1 ND2
REMARK 470 ASP A 977 CG OD1 OD2
REMARK 470 ILE A 978 CG1 CG2 CD1
REMARK 470 ASN A 979 CG OD1 ND2
REMARK 470 ILE A1012 CG1 CG2 CD1
REMARK 470 PHE A1014 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A1015 CG SD CE
REMARK 470 ASN B 44 CG OD1 ND2
REMARK 470 ASP B 964 CG OD1 OD2
REMARK 470 SER B 965 OG
REMARK 470 GLU B 971 CG CD OE1 OE2
REMARK 470 ILE B 978 CG1 CG2 CD1
REMARK 470 ASN B 979 CG OD1 ND2
REMARK 470 ILE B1012 CG1 CG2 CD1
REMARK 470 ASN B1013 CG OD1 ND2
REMARK 470 PHE B1014 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE C 22 CD1 PHE C 22 CE1 -0.134
REMARK 500 PHE C 22 CZ PHE C 22 CE2 -0.122
REMARK 500 PHE C 22 CE2 PHE C 22 CD2 -0.144
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 122 C - N - CA ANGL. DEV. = 10.1 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 ASN A 44 109.52 -57.89
REMARK 500 HIS A 93 48.97 -81.29
REMARK 500 LEU A 170 -51.21 -124.36
REMARK 500 CYS A 171 56.72 -144.60
REMARK 500 ASP A 175 138.98 -39.95
REMARK 500 GLU A 227 -73.10 -130.35
REMARK 500 THR A 228 -74.55 -42.50
REMARK 500 GLN A 232 33.50 -80.04
REMARK 500 GLU A 233 21.27 -156.67
REMARK 500 GLU A 341 -167.60 -115.23
REMARK 500 PRO A 343 127.05 -39.66
REMARK 500 ARG A 368 107.07 -48.20
REMARK 500 GLU A 457 -37.51 -132.32
REMARK 500 SER A 484 -7.74 -58.80
REMARK 500 LYS A 566 -22.62 -159.51
REMARK 500 TYR A 584 18.50 -140.91
REMARK 500 THR A 651 24.85 -142.63
REMARK 500 ASN A 672 -9.12 -58.46
REMARK 500 ASN A 787 48.39 -97.94
REMARK 500 THR A 797 -90.76 -104.55
REMARK 500 ARG A 824 -67.85 -106.07
REMARK 500 ASN A 917 74.26 -103.75
REMARK 500 GLU A 962 41.13 -85.59
REMARK 500 CYS A 966 131.95 178.91
REMARK 500 ASN A 979 7.24 50.77
REMARK 500 PRO A1010 179.61 -59.03
REMARK 500 MET A1015 140.65 162.91
REMARK 500 HIS B 93 48.72 -71.97
REMARK 500 SER B 143 -166.44 -120.88
REMARK 500 LEU B 170 -48.09 -143.02
REMARK 500 CYS B 171 50.99 -142.96
REMARK 500 GLU B 227 -63.33 -143.88
REMARK 500 GLU B 262 162.70 -48.79
REMARK 500 GLU B 453 34.32 -89.30
REMARK 500 TYR B 454 -46.69 -141.51
REMARK 500 GLU B 457 -78.47 -112.85
REMARK 500 SER B 484 -8.52 -54.79
REMARK 500 LYS B 566 -40.18 -140.58
REMARK 500 PRO B 570 55.51 -69.30
REMARK 500 ALA B 694 112.87 -163.34
REMARK 500 ASN B 787 50.90 -92.16
REMARK 500 THR B 797 -89.62 -105.74
REMARK 500 GLU B 962 32.30 -91.97
REMARK 500 ASP B 964 -151.42 -104.08
REMARK 500 SER B 965 141.20 -21.41
REMARK 500 VAL D 23 114.96 -165.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE D 22 VAL D 23 -132.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G47 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME IN COMPLEX WITH
REMARK 900 AMYLOID-BETA (1-40)
REMARK 900 RELATED ID: 2G48 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME ENZYME IN COMPLEX WITH AMYLIN
REMARK 900 RELATED ID: 2G54 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ZN-BOUND HUMAN INSULIN-DEGRADING ENZYME IN
REMARK 900 COMPLEX WITH INSULIN B CHAIN
REMARK 900 RELATED ID: 2G56 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME ENZYME IN COMPLEX WITH INSULIN B CHAIN
DBREF 2G49 A 42 1019 UNP Q5T5N2 Q5T5N2_HUMAN 42 1019
DBREF 2G49 B 42 1019 UNP Q5T5N2 Q5T5N2_HUMAN 42 1019
DBREF 2G49 C 1 29 GB 4503945 NP_002045 53 81
DBREF 2G49 D 1 29 GB 4503945 NP_002045 53 81
SEQADV 2G49 MET A 30 UNP Q5T5N2 INITIATING METHIONINE
SEQADV 2G49 HIS A 31 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS A 32 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS A 33 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS A 34 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS A 35 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS A 36 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 ALA A 37 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 ALA A 38 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 GLY A 39 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 ILE A 40 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 PRO A 41 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 GLN A 111 UNP Q5T5N2 GLU 111 ENGINEERED MUTATION
SEQADV 2G49 MET B 30 UNP Q5T5N2 INITIATING METHIONINE
SEQADV 2G49 HIS B 31 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS B 32 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS B 33 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS B 34 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS B 35 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 HIS B 36 UNP Q5T5N2 EXPRESSION TAG
SEQADV 2G49 ALA B 37 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 ALA B 38 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 GLY B 39 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 ILE B 40 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 PRO B 41 UNP Q5T5N2 CLONING ARTIFACT
SEQADV 2G49 GLN B 111 UNP Q5T5N2 GLU 111 ENGINEERED MUTATION
SEQRES 1 A 990 MET HIS HIS HIS HIS HIS HIS ALA ALA GLY ILE PRO MET
SEQRES 2 A 990 ASN ASN PRO ALA ILE LYS ARG ILE GLY ASN HIS ILE THR
SEQRES 3 A 990 LYS SER PRO GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU
SEQRES 4 A 990 LEU ALA ASN GLY ILE LYS VAL LEU LEU ILE SER ASP PRO
SEQRES 5 A 990 THR THR ASP LYS SER SER ALA ALA LEU ASP VAL HIS ILE
SEQRES 6 A 990 GLY SER LEU SER ASP PRO PRO ASN ILE ALA GLY LEU SER
SEQRES 7 A 990 HIS PHE CYS GLN HIS MET LEU PHE LEU GLY THR LYS LYS
SEQRES 8 A 990 TYR PRO LYS GLU ASN GLU TYR SER GLN PHE LEU SER GLU
SEQRES 9 A 990 HIS ALA GLY SER SER ASN ALA PHE THR SER GLY GLU HIS
SEQRES 10 A 990 THR ASN TYR TYR PHE ASP VAL SER HIS GLU HIS LEU GLU
SEQRES 11 A 990 GLY ALA LEU ASP ARG PHE ALA GLN PHE PHE LEU CYS PRO
SEQRES 12 A 990 LEU PHE ASP GLU SER CYS LYS ASP ARG GLU VAL ASN ALA
SEQRES 13 A 990 VAL ASP SER GLU HIS GLU LYS ASN VAL MET ASN ASP ALA
SEQRES 14 A 990 TRP ARG LEU PHE GLN LEU GLU LYS ALA THR GLY ASN PRO
SEQRES 15 A 990 LYS HIS PRO PHE SER LYS PHE GLY THR GLY ASN LYS TYR
SEQRES 16 A 990 THR LEU GLU THR ARG PRO ASN GLN GLU GLY ILE ASP VAL
SEQRES 17 A 990 ARG GLN GLU LEU LEU LYS PHE HIS SER ALA TYR TYR SER
SEQRES 18 A 990 SER ASN LEU MET ALA VAL CYS VAL LEU GLY ARG GLU SER
SEQRES 19 A 990 LEU ASP ASP LEU THR ASN LEU VAL VAL LYS LEU PHE SER
SEQRES 20 A 990 GLU VAL GLU ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO
SEQRES 21 A 990 GLU HIS PRO PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR
SEQRES 22 A 990 LYS ILE VAL PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL
SEQRES 23 A 990 THR PHE PRO ILE PRO ASP LEU GLN LYS TYR TYR LYS SER
SEQRES 24 A 990 ASN PRO GLY HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU
SEQRES 25 A 990 GLY PRO GLY SER LEU LEU SER GLU LEU LYS SER LYS GLY
SEQRES 26 A 990 TRP VAL ASN THR LEU VAL GLY GLY GLN LYS GLU GLY ALA
SEQRES 27 A 990 ARG GLY PHE MET PHE PHE ILE ILE ASN VAL ASP LEU THR
SEQRES 28 A 990 GLU GLU GLY LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS
SEQRES 29 A 990 MET PHE GLN TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO
SEQRES 30 A 990 GLN GLU TRP VAL PHE GLN GLU CYS LYS ASP LEU ASN ALA
SEQRES 31 A 990 VAL ALA PHE ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY
SEQRES 32 A 990 TYR THR SER LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO
SEQRES 33 A 990 LEU GLU GLU VAL LEU THR ALA GLU TYR LEU LEU GLU GLU
SEQRES 34 A 990 PHE ARG PRO ASP LEU ILE GLU MET VAL LEU ASP LYS LEU
SEQRES 35 A 990 ARG PRO GLU ASN VAL ARG VAL ALA ILE VAL SER LYS SER
SEQRES 36 A 990 PHE GLU GLY LYS THR ASP ARG THR GLU GLU TRP TYR GLY
SEQRES 37 A 990 THR GLN TYR LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE
SEQRES 38 A 990 LYS LYS TRP GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS
SEQRES 39 A 990 LEU PRO THR LYS ASN GLU PHE ILE PRO THR ASN PHE GLU
SEQRES 40 A 990 ILE LEU PRO LEU GLU LYS GLU ALA THR PRO TYR PRO ALA
SEQRES 41 A 990 LEU ILE LYS ASP THR ALA MET SER LYS LEU TRP PHE LYS
SEQRES 42 A 990 GLN ASP ASP LYS PHE PHE LEU PRO LYS ALA CYS LEU ASN
SEQRES 43 A 990 PHE GLU PHE PHE SER PRO PHE ALA TYR VAL ASP PRO LEU
SEQRES 44 A 990 HIS CYS ASN MET ALA TYR LEU TYR LEU GLU LEU LEU LYS
SEQRES 45 A 990 ASP SER LEU ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA
SEQRES 46 A 990 GLY LEU SER TYR ASP LEU GLN ASN THR ILE TYR GLY MET
SEQRES 47 A 990 TYR LEU SER VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE
SEQRES 48 A 990 LEU LEU LYS LYS ILE ILE GLU LYS MET ALA THR PHE GLU
SEQRES 49 A 990 ILE ASP GLU LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR
SEQRES 50 A 990 MET ARG SER LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS
SEQRES 51 A 990 GLN HIS ALA MET TYR TYR LEU ARG LEU LEU MET THR GLU
SEQRES 52 A 990 VAL ALA TRP THR LYS ASP GLU LEU LYS GLU ALA LEU ASP
SEQRES 53 A 990 ASP VAL THR LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN
SEQRES 54 A 990 LEU LEU SER ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY
SEQRES 55 A 990 ASN ILE THR LYS GLN ALA ALA LEU GLY ILE MET GLN MET
SEQRES 56 A 990 VAL GLU ASP THR LEU ILE GLU HIS ALA HIS THR LYS PRO
SEQRES 57 A 990 LEU LEU PRO SER GLN LEU VAL ARG TYR ARG GLU VAL GLN
SEQRES 58 A 990 LEU PRO ASP ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN
SEQRES 59 A 990 GLU VAL HIS ASN ASN CYS GLY ILE GLU ILE TYR TYR GLN
SEQRES 60 A 990 THR ASP MET GLN SER THR SER GLU ASN MET PHE LEU GLU
SEQRES 61 A 990 LEU PHE CYS GLN ILE ILE SER GLU PRO CYS PHE ASN THR
SEQRES 62 A 990 LEU ARG THR LYS GLU GLN LEU GLY TYR ILE VAL PHE SER
SEQRES 63 A 990 GLY PRO ARG ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE
SEQRES 64 A 990 ILE ILE GLN SER GLU LYS PRO PRO HIS TYR LEU GLU SER
SEQRES 65 A 990 ARG VAL GLU ALA PHE LEU ILE THR MET GLU LYS SER ILE
SEQRES 66 A 990 GLU ASP MET THR GLU GLU ALA PHE GLN LYS HIS ILE GLN
SEQRES 67 A 990 ALA LEU ALA ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU
SEQRES 68 A 990 SER ALA GLU CYS ALA LYS TYR TRP GLY GLU ILE ILE SER
SEQRES 69 A 990 GLN GLN TYR ASN PHE ASP ARG ASP ASN THR GLU VAL ALA
SEQRES 70 A 990 TYR LEU LYS THR LEU THR LYS GLU ASP ILE ILE LYS PHE
SEQRES 71 A 990 TYR LYS GLU MET LEU ALA VAL ASP ALA PRO ARG ARG HIS
SEQRES 72 A 990 LYS VAL SER VAL HIS VAL LEU ALA ARG GLU MET ASP SER
SEQRES 73 A 990 CYS PRO VAL VAL GLY GLU PHE PRO CYS GLN ASN ASP ILE
SEQRES 74 A 990 ASN LEU SER GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL
SEQRES 75 A 990 ILE GLN ASN MET THR GLU PHE LYS ARG GLY LEU PRO LEU
SEQRES 76 A 990 PHE PRO LEU VAL LYS PRO HIS ILE ASN PHE MET ALA ALA
SEQRES 77 A 990 LYS LEU
SEQRES 1 B 990 MET HIS HIS HIS HIS HIS HIS ALA ALA GLY ILE PRO MET
SEQRES 2 B 990 ASN ASN PRO ALA ILE LYS ARG ILE GLY ASN HIS ILE THR
SEQRES 3 B 990 LYS SER PRO GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU
SEQRES 4 B 990 LEU ALA ASN GLY ILE LYS VAL LEU LEU ILE SER ASP PRO
SEQRES 5 B 990 THR THR ASP LYS SER SER ALA ALA LEU ASP VAL HIS ILE
SEQRES 6 B 990 GLY SER LEU SER ASP PRO PRO ASN ILE ALA GLY LEU SER
SEQRES 7 B 990 HIS PHE CYS GLN HIS MET LEU PHE LEU GLY THR LYS LYS
SEQRES 8 B 990 TYR PRO LYS GLU ASN GLU TYR SER GLN PHE LEU SER GLU
SEQRES 9 B 990 HIS ALA GLY SER SER ASN ALA PHE THR SER GLY GLU HIS
SEQRES 10 B 990 THR ASN TYR TYR PHE ASP VAL SER HIS GLU HIS LEU GLU
SEQRES 11 B 990 GLY ALA LEU ASP ARG PHE ALA GLN PHE PHE LEU CYS PRO
SEQRES 12 B 990 LEU PHE ASP GLU SER CYS LYS ASP ARG GLU VAL ASN ALA
SEQRES 13 B 990 VAL ASP SER GLU HIS GLU LYS ASN VAL MET ASN ASP ALA
SEQRES 14 B 990 TRP ARG LEU PHE GLN LEU GLU LYS ALA THR GLY ASN PRO
SEQRES 15 B 990 LYS HIS PRO PHE SER LYS PHE GLY THR GLY ASN LYS TYR
SEQRES 16 B 990 THR LEU GLU THR ARG PRO ASN GLN GLU GLY ILE ASP VAL
SEQRES 17 B 990 ARG GLN GLU LEU LEU LYS PHE HIS SER ALA TYR TYR SER
SEQRES 18 B 990 SER ASN LEU MET ALA VAL CYS VAL LEU GLY ARG GLU SER
SEQRES 19 B 990 LEU ASP ASP LEU THR ASN LEU VAL VAL LYS LEU PHE SER
SEQRES 20 B 990 GLU VAL GLU ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO
SEQRES 21 B 990 GLU HIS PRO PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR
SEQRES 22 B 990 LYS ILE VAL PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL
SEQRES 23 B 990 THR PHE PRO ILE PRO ASP LEU GLN LYS TYR TYR LYS SER
SEQRES 24 B 990 ASN PRO GLY HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU
SEQRES 25 B 990 GLY PRO GLY SER LEU LEU SER GLU LEU LYS SER LYS GLY
SEQRES 26 B 990 TRP VAL ASN THR LEU VAL GLY GLY GLN LYS GLU GLY ALA
SEQRES 27 B 990 ARG GLY PHE MET PHE PHE ILE ILE ASN VAL ASP LEU THR
SEQRES 28 B 990 GLU GLU GLY LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS
SEQRES 29 B 990 MET PHE GLN TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO
SEQRES 30 B 990 GLN GLU TRP VAL PHE GLN GLU CYS LYS ASP LEU ASN ALA
SEQRES 31 B 990 VAL ALA PHE ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY
SEQRES 32 B 990 TYR THR SER LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO
SEQRES 33 B 990 LEU GLU GLU VAL LEU THR ALA GLU TYR LEU LEU GLU GLU
SEQRES 34 B 990 PHE ARG PRO ASP LEU ILE GLU MET VAL LEU ASP LYS LEU
SEQRES 35 B 990 ARG PRO GLU ASN VAL ARG VAL ALA ILE VAL SER LYS SER
SEQRES 36 B 990 PHE GLU GLY LYS THR ASP ARG THR GLU GLU TRP TYR GLY
SEQRES 37 B 990 THR GLN TYR LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE
SEQRES 38 B 990 LYS LYS TRP GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS
SEQRES 39 B 990 LEU PRO THR LYS ASN GLU PHE ILE PRO THR ASN PHE GLU
SEQRES 40 B 990 ILE LEU PRO LEU GLU LYS GLU ALA THR PRO TYR PRO ALA
SEQRES 41 B 990 LEU ILE LYS ASP THR ALA MET SER LYS LEU TRP PHE LYS
SEQRES 42 B 990 GLN ASP ASP LYS PHE PHE LEU PRO LYS ALA CYS LEU ASN
SEQRES 43 B 990 PHE GLU PHE PHE SER PRO PHE ALA TYR VAL ASP PRO LEU
SEQRES 44 B 990 HIS CYS ASN MET ALA TYR LEU TYR LEU GLU LEU LEU LYS
SEQRES 45 B 990 ASP SER LEU ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA
SEQRES 46 B 990 GLY LEU SER TYR ASP LEU GLN ASN THR ILE TYR GLY MET
SEQRES 47 B 990 TYR LEU SER VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE
SEQRES 48 B 990 LEU LEU LYS LYS ILE ILE GLU LYS MET ALA THR PHE GLU
SEQRES 49 B 990 ILE ASP GLU LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR
SEQRES 50 B 990 MET ARG SER LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS
SEQRES 51 B 990 GLN HIS ALA MET TYR TYR LEU ARG LEU LEU MET THR GLU
SEQRES 52 B 990 VAL ALA TRP THR LYS ASP GLU LEU LYS GLU ALA LEU ASP
SEQRES 53 B 990 ASP VAL THR LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN
SEQRES 54 B 990 LEU LEU SER ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY
SEQRES 55 B 990 ASN ILE THR LYS GLN ALA ALA LEU GLY ILE MET GLN MET
SEQRES 56 B 990 VAL GLU ASP THR LEU ILE GLU HIS ALA HIS THR LYS PRO
SEQRES 57 B 990 LEU LEU PRO SER GLN LEU VAL ARG TYR ARG GLU VAL GLN
SEQRES 58 B 990 LEU PRO ASP ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN
SEQRES 59 B 990 GLU VAL HIS ASN ASN CYS GLY ILE GLU ILE TYR TYR GLN
SEQRES 60 B 990 THR ASP MET GLN SER THR SER GLU ASN MET PHE LEU GLU
SEQRES 61 B 990 LEU PHE CYS GLN ILE ILE SER GLU PRO CYS PHE ASN THR
SEQRES 62 B 990 LEU ARG THR LYS GLU GLN LEU GLY TYR ILE VAL PHE SER
SEQRES 63 B 990 GLY PRO ARG ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE
SEQRES 64 B 990 ILE ILE GLN SER GLU LYS PRO PRO HIS TYR LEU GLU SER
SEQRES 65 B 990 ARG VAL GLU ALA PHE LEU ILE THR MET GLU LYS SER ILE
SEQRES 66 B 990 GLU ASP MET THR GLU GLU ALA PHE GLN LYS HIS ILE GLN
SEQRES 67 B 990 ALA LEU ALA ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU
SEQRES 68 B 990 SER ALA GLU CYS ALA LYS TYR TRP GLY GLU ILE ILE SER
SEQRES 69 B 990 GLN GLN TYR ASN PHE ASP ARG ASP ASN THR GLU VAL ALA
SEQRES 70 B 990 TYR LEU LYS THR LEU THR LYS GLU ASP ILE ILE LYS PHE
SEQRES 71 B 990 TYR LYS GLU MET LEU ALA VAL ASP ALA PRO ARG ARG HIS
SEQRES 72 B 990 LYS VAL SER VAL HIS VAL LEU ALA ARG GLU MET ASP SER
SEQRES 73 B 990 CYS PRO VAL VAL GLY GLU PHE PRO CYS GLN ASN ASP ILE
SEQRES 74 B 990 ASN LEU SER GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL
SEQRES 75 B 990 ILE GLN ASN MET THR GLU PHE LYS ARG GLY LEU PRO LEU
SEQRES 76 B 990 PHE PRO LEU VAL LYS PRO HIS ILE ASN PHE MET ALA ALA
SEQRES 77 B 990 LYS LEU
SEQRES 1 C 29 HIS SER GLN GLY THR PHE THR SER ASP TYR SER LYS TYR
SEQRES 2 C 29 LEU ASP SER ARG ARG ALA GLN ASP PHE VAL GLN TRP LEU
SEQRES 3 C 29 MET ASN THR
SEQRES 1 D 29 HIS SER GLN GLY THR PHE THR SER ASP TYR SER LYS TYR
SEQRES 2 D 29 LEU ASP SER ARG ARG ALA GLN ASP PHE VAL GLN TRP LEU
SEQRES 3 D 29 MET ASN THR
HET DIO A2000 6
HET DIO B2001 6
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
FORMUL 5 DIO 2(C4 H8 O2)
FORMUL 7 HOH *695(H2 O)
HELIX 1 1 GLY A 95 ASP A 99 5 5
HELIX 2 2 GLY A 105 LEU A 114 1 10
HELIX 3 3 ASN A 125 GLU A 133 1 9
HELIX 4 4 HIS A 157 GLN A 167 1 11
HELIX 5 5 PHE A 168 LEU A 170 5 3
HELIX 6 6 ASP A 175 MET A 195 1 21
HELIX 7 7 ASN A 196 THR A 208 1 13
HELIX 8 8 HIS A 213 LYS A 217 5 5
HELIX 9 9 ASN A 222 GLU A 227 1 6
HELIX 10 10 GLU A 227 GLN A 232 1 6
HELIX 11 11 ASP A 236 TYR A 249 1 14
HELIX 12 12 SER A 250 ASN A 252 5 3
HELIX 13 13 SER A 263 SER A 276 1 14
HELIX 14 14 GLN A 294 LEU A 298 5 5
HELIX 15 15 LEU A 322 TYR A 326 5 5
HELIX 16 16 ASN A 329 GLY A 339 1 11
HELIX 17 17 SER A 345 LYS A 353 1 9
HELIX 18 18 THR A 380 LEU A 385 1 6
HELIX 19 19 HIS A 386 GLY A 405 1 20
HELIX 20 20 GLN A 407 PHE A 424 1 18
HELIX 21 21 ARG A 429 LEU A 441 1 13
HELIX 22 22 PRO A 445 VAL A 449 5 5
HELIX 23 23 ARG A 460 ASP A 469 1 10
HELIX 24 24 LYS A 470 LEU A 471 5 2
HELIX 25 25 ARG A 472 ASN A 475 5 4
HELIX 26 26 LYS A 483 GLU A 486 5 4
HELIX 27 27 PRO A 506 ASN A 515 1 10
HELIX 28 28 PRO A 581 TYR A 584 5 4
HELIX 29 29 ASP A 586 ALA A 614 1 29
HELIX 30 30 LYS A 637 THR A 651 1 15
HELIX 31 31 ASP A 655 ASN A 672 1 18
HELIX 32 32 PHE A 673 GLU A 676 5 4
HELIX 33 33 GLN A 677 THR A 691 1 15
HELIX 34 34 THR A 696 ASP A 705 1 10
HELIX 35 35 THR A 708 SER A 721 1 14
HELIX 36 36 THR A 734 HIS A 754 1 21
HELIX 37 37 LEU A 759 LEU A 763 5 5
HELIX 38 38 SER A 801 ARG A 824 1 24
HELIX 39 39 PRO A 855 MET A 877 1 23
HELIX 40 40 THR A 878 ASP A 895 1 18
HELIX 41 41 LYS A 899 SER A 913 1 15
HELIX 42 42 ASP A 919 LYS A 929 1 11
HELIX 43 43 THR A 932 LEU A 944 1 13
HELIX 44 44 ASN A 994 GLY A 1001 1 8
HELIX 45 45 GLY B 95 ASP B 99 5 5
HELIX 46 46 GLY B 105 LEU B 114 1 10
HELIX 47 47 PHE B 115 GLY B 117 5 3
HELIX 48 48 ASN B 125 HIS B 134 1 10
HELIX 49 49 HIS B 157 GLN B 167 1 11
HELIX 50 50 PHE B 168 LEU B 170 5 3
HELIX 51 51 ASP B 175 MET B 195 1 21
HELIX 52 52 ASN B 196 ALA B 207 1 12
HELIX 53 53 HIS B 213 LYS B 217 5 5
HELIX 54 54 ASN B 222 GLU B 227 1 6
HELIX 55 55 GLU B 227 GLY B 234 1 8
HELIX 56 56 ASP B 236 TYR B 249 1 14
HELIX 57 57 SER B 250 ASN B 252 5 3
HELIX 58 58 SER B 263 SER B 276 1 14
HELIX 59 59 GLN B 294 LEU B 298 5 5
HELIX 60 60 LEU B 322 TYR B 326 5 5
HELIX 61 61 ASN B 329 GLY B 339 1 11
HELIX 62 62 SER B 345 LYS B 353 1 9
HELIX 63 63 THR B 380 HIS B 386 1 7
HELIX 64 64 HIS B 386 GLY B 405 1 20
HELIX 65 65 GLN B 407 LYS B 425 1 19
HELIX 66 66 ARG B 429 LEU B 441 1 13
HELIX 67 67 PRO B 445 VAL B 449 5 5
HELIX 68 68 ARG B 460 ASP B 469 1 10
HELIX 69 69 LYS B 470 LEU B 471 5 2
HELIX 70 70 ARG B 472 ASN B 475 5 4
HELIX 71 71 LYS B 483 GLU B 486 5 4
HELIX 72 72 PRO B 506 ASN B 515 1 10
HELIX 73 73 PRO B 581 TYR B 584 5 4
HELIX 74 74 ASP B 586 ALA B 614 1 29
HELIX 75 75 LYS B 637 THR B 651 1 15
HELIX 76 76 ASP B 655 ASN B 672 1 18
HELIX 77 77 PHE B 673 GLU B 676 5 4
HELIX 78 78 GLN B 677 THR B 691 1 15
HELIX 79 79 THR B 696 ASP B 705 1 10
HELIX 80 80 THR B 708 SER B 721 1 14
HELIX 81 81 THR B 734 HIS B 754 1 21
HELIX 82 82 LEU B 759 LEU B 763 5 5
HELIX 83 83 SER B 801 ARG B 824 1 24
HELIX 84 84 PRO B 855 MET B 877 1 23
HELIX 85 85 THR B 878 ASP B 895 1 18
HELIX 86 86 LYS B 899 SER B 913 1 15
HELIX 87 87 ASP B 919 LYS B 929 1 11
HELIX 88 88 THR B 932 MET B 943 1 12
HELIX 89 89 ASN B 994 GLY B 1001 1 8
SHEET 1 A 8 ILE A 47 ILE A 50 0
SHEET 2 A 8 GLU A 63 LEU A 69 -1 O GLU A 68 N ARG A 49
SHEET 3 A 8 LYS A 74 SER A 79 -1 O VAL A 75 N LEU A 67
SHEET 4 A 8 MET A 254 GLY A 260 1 O VAL A 256 N LYS A 74
SHEET 5 A 8 LYS A 85 VAL A 92 -1 N SER A 87 O LEU A 259
SHEET 6 A 8 THR A 147 SER A 154 -1 O VAL A 153 N SER A 86
SHEET 7 A 8 SER A 137 THR A 142 -1 N ASN A 139 O TYR A 150
SHEET 8 A 8 GLN C 24 TRP C 25 -1 O GLN C 24 N THR A 142
SHEET 1 B 7 VAL A 356 ALA A 367 0
SHEET 2 B 7 PHE A 370 LEU A 379 -1 O PHE A 372 N LYS A 364
SHEET 3 B 7 ASN A 312 ILE A 319 -1 N LEU A 313 O VAL A 377
SHEET 4 B 7 ARG A 477 VAL A 481 -1 O ALA A 479 N TYR A 314
SHEET 5 B 7 GLN A 300 ILE A 304 1 N ILE A 304 O ILE A 480
SHEET 6 B 7 GLN A 499 ALA A 504 -1 O GLU A 503 N LEU A 301
SHEET 7 B 7 ARG A 491 THR A 492 -1 N ARG A 491 O TYR A 500
SHEET 1 C 6 ALA A 549 ASP A 553 0
SHEET 2 C 6 SER A 557 GLN A 563 -1 O LEU A 559 N LYS A 552
SHEET 3 C 6 ARG A 722 GLY A 731 1 O ALA A 727 N TRP A 560
SHEET 4 C 6 LYS A 571 PHE A 579 -1 N PHE A 579 O HIS A 724
SHEET 5 C 6 GLY A 626 TYR A 634 -1 O LEU A 629 N PHE A 576
SHEET 6 C 6 LEU A 616 THR A 623 -1 N GLN A 621 O TYR A 628
SHEET 1 D 4 ALA A 549 ASP A 553 0
SHEET 2 D 4 SER A 557 GLN A 563 -1 O LEU A 559 N LYS A 552
SHEET 3 D 4 ARG A 722 GLY A 731 1 O ALA A 727 N TRP A 560
SHEET 4 D 4 LYS A 756 PRO A 757 1 O LYS A 756 N LEU A 723
SHEET 1 E 6 VAL A 833 ALA A 840 0
SHEET 2 E 6 ILE A 843 SER A 852 -1 O ILE A 843 N ALA A 840
SHEET 3 E 6 CYS A 789 MET A 799 -1 N CYS A 789 O SER A 852
SHEET 4 E 6 HIS A 952 LEU A 959 -1 O VAL A 958 N GLY A 790
SHEET 5 E 6 GLY A 775 ARG A 782 1 N GLN A 781 O LEU A 959
SHEET 6 E 6 GLU A 990 VAL A 991 1 O GLU A 990 N TRP A 776
SHEET 1 F 8 ILE B 47 GLY B 51 0
SHEET 2 F 8 GLU B 63 LEU B 69 -1 O GLY B 66 N GLY B 51
SHEET 3 F 8 LYS B 74 SER B 79 -1 O VAL B 75 N LEU B 67
SHEET 4 F 8 MET B 254 GLY B 260 1 O VAL B 256 N LYS B 74
SHEET 5 F 8 LYS B 85 VAL B 92 -1 N SER B 87 O LEU B 259
SHEET 6 F 8 THR B 147 SER B 154 -1 O VAL B 153 N SER B 86
SHEET 7 F 8 SER B 137 THR B 142 -1 N PHE B 141 O ASN B 148
SHEET 8 F 8 GLN D 24 TRP D 25 -1 O GLN D 24 N THR B 142
SHEET 1 G 7 VAL B 356 ALA B 367 0
SHEET 2 G 7 PHE B 370 LEU B 379 -1 O PHE B 372 N LYS B 364
SHEET 3 G 7 ASN B 312 PRO B 320 -1 N LEU B 313 O VAL B 377
SHEET 4 G 7 ARG B 477 VAL B 481 -1 O ALA B 479 N TYR B 314
SHEET 5 G 7 GLN B 300 ILE B 304 1 N TYR B 302 O ILE B 480
SHEET 6 G 7 GLN B 499 ALA B 504 -1 O GLU B 503 N LEU B 301
SHEET 7 G 7 ARG B 491 THR B 492 -1 N ARG B 491 O TYR B 500
SHEET 1 H 6 ALA B 549 ASP B 553 0
SHEET 2 H 6 SER B 557 GLN B 563 -1 O PHE B 561 N ALA B 549
SHEET 3 H 6 ARG B 722 GLY B 731 1 O ILE B 725 N LYS B 558
SHEET 4 H 6 LYS B 571 PHE B 579 -1 N CYS B 573 O HIS B 730
SHEET 5 H 6 GLY B 626 TYR B 634 -1 O MET B 627 N PHE B 578
SHEET 6 H 6 LEU B 616 ASN B 622 -1 N GLN B 621 O TYR B 628
SHEET 1 I 4 ALA B 549 ASP B 553 0
SHEET 2 I 4 SER B 557 GLN B 563 -1 O PHE B 561 N ALA B 549
SHEET 3 I 4 ARG B 722 GLY B 731 1 O ILE B 725 N LYS B 558
SHEET 4 I 4 LYS B 756 PRO B 757 1 O LYS B 756 N LEU B 723
SHEET 1 J 6 ILE B 832 ALA B 840 0
SHEET 2 J 6 ILE B 843 SER B 852 -1 O GLY B 845 N ARG B 838
SHEET 3 J 6 CYS B 789 MET B 799 -1 N CYS B 789 O SER B 852
SHEET 4 J 6 HIS B 952 LEU B 959 -1 O VAL B 958 N GLY B 790
SHEET 5 J 6 GLY B 775 ARG B 782 1 N GLN B 781 O LEU B 959
SHEET 6 J 6 GLU B 990 VAL B 991 1 O GLU B 990 N TRP B 776
SITE 1 AC1 3 LEU A 204 THR A 208 ARG A 477
SITE 1 AC2 5 LEU B 204 GLU B 205 TYR B 302 ARG B 477
SITE 2 AC2 5 HOH B2063
CRYST1 262.722 262.722 90.788 90.00 90.00 120.00 P 65 12
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 0.003806 0.002198 0.000000 0.00000
SCALE2 0.000000 0.004395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011015 0.00000
(ATOM LINES ARE NOT SHOWN.)
END