HEADER HYDROLASE/IMMUNE SYSTEM/HORMONE 03-OCT-17 6B70
TITLE CRYO-EM STRUCTURE OF HUMAN INSULIN DEGRADING ENZYME IN COMPLEX WITH
TITLE 2 FAB H11-E HEAVY CHAIN, FAB H11-E LIGHT CHAIN AND INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-DEGRADING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 46-1011;
COMPND 5 SYNONYM: ABETA-DEGRADING PROTEASE,INSULIN PROTEASE,INSULINASE,
COMPND 6 INSULYSIN;
COMPND 7 EC: 3.4.24.56;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: FAB H11-E HEAVY CHAIN;
COMPND 11 CHAIN: C, E;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: FAB H11-E LIGHT CHAIN;
COMPND 15 CHAIN: D, F;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: INSULIN;
COMPND 19 CHAIN: a, c;
COMPND 20 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 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 11 ORGANISM_TAXID: 10090, 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 17 ORGANISM_TAXID: 10090, 9606;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 22 ORGANISM_COMMON: HUMAN;
SOURCE 23 ORGANISM_TAXID: 9606;
SOURCE 24 GENE: INS;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IDE, INSULIN DEGRADING ENZYME, AMYLOID BETA, BIOSYNTHETIC PROTEIN,
KEYWDS 2 HYDROLASE-IMMUNE SYSTEM-HORMONE COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR W.G.LIANG,Z.ZHANG,L.J.BAILEY,A.A.KOSSIAKOFF,Y.Z.TAN,H.WEI,
AUTHOR 2 B.CARRAGHER,S.C.POTTER,W.J.TANG
REVDAT 5 28-APR-21 6B70 1 REMARK
REVDAT 4 01-JAN-20 6B70 1 REMARK
REVDAT 3 11-APR-18 6B70 1 JRNL
REVDAT 2 17-JAN-18 6B70 1 REMARK
REVDAT 1 27-DEC-17 6B70 0
JRNL AUTH Z.ZHANG,W.G.LIANG,L.J.BAILEY,Y.Z.TAN,H.WEI,A.WANG,
JRNL AUTH 2 M.FARCASANU,V.A.WOODS,L.A.MCCORD,D.LEE,W.SHANG,
JRNL AUTH 3 R.DEPREZ-POULAIN,B.DEPREZ,D.R.LIU,A.KOIDE,S.KOIDE,
JRNL AUTH 4 A.A.KOSSIAKOFF,S.LI,B.CARRAGHER,C.S.POTTER,W.J.TANG
JRNL TITL ENSEMBLE CRYOEM ELUCIDATES THE MECHANISM OF INSULIN CAPTURE
JRNL TITL 2 AND DEGRADATION BY HUMAN INSULIN DEGRADING ENZYME.
JRNL REF ELIFE V. 7 2018
JRNL REFN ESSN 2050-084X
JRNL PMID 29596046
JRNL DOI 10.7554/ELIFE.33572
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : DOG PICKER, LEGINON, GCTF, COOT, UCSF
REMARK 3 CHIMERA, RELION, RELION, RELION, RELION,
REMARK 3 PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : 92.000
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.700
REMARK 3 NUMBER OF PARTICLES : 116122
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6B70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230311.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : INSULIN DEGRADING
REMARK 245 ENZYME/INSULIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.30
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : THE CRYO GRIDS WERE MADE USING
REMARK 245 SPOTITON AND HOMEMADE PLUNGER
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.80
REMARK 245 SAMPLE DETAILS : CRYO-EM STRUCTURE OF HUMAN
REMARK 245 INSULIN DEGRADING ENZYME IN COMPLEX WITH INSULIN
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 3085
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 940.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 7140.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 22500
REMARK 245 CALIBRATED MAGNIFICATION : 46598
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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 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 ASP A 964
REMARK 465 SER A 965
REMARK 465 CYS A 966
REMARK 465 PRO A 967
REMARK 465 VAL A 968
REMARK 465 VAL A 969
REMARK 465 GLY A 970
REMARK 465 GLU A 971
REMARK 465 PHE A 972
REMARK 465 PRO A 973
REMARK 465 CYS A 974
REMARK 465 GLN A 975
REMARK 465 ASN A 976
REMARK 465 ASP A 977
REMARK 465 ILE A 978
REMARK 465 ASN A 979
REMARK 465 LEU A 980
REMARK 465 MET B 963
REMARK 465 ASP B 964
REMARK 465 SER B 965
REMARK 465 CYS B 966
REMARK 465 PRO B 967
REMARK 465 VAL B 968
REMARK 465 VAL B 969
REMARK 465 GLY B 970
REMARK 465 GLU B 971
REMARK 465 PHE B 972
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 ILE B 978
REMARK 465 ASN B 979
REMARK 465 LEU B 980
REMARK 465 SER B 981
REMARK 465 GLN B 982
REMARK 465 ALA B 983
REMARK 465 PRO B 984
REMARK 465 ALA B 985
REMARK 465 LEU B 986
REMARK 465 PRO B 987
REMARK 465 GLN B 988
REMARK 465 MET a -88
REMARK 465 ALA a -87
REMARK 465 LEU a -86
REMARK 465 TRP a -85
REMARK 465 MET a -84
REMARK 465 ARG a -83
REMARK 465 LEU a -82
REMARK 465 LEU a -81
REMARK 465 PRO a -80
REMARK 465 LEU a -79
REMARK 465 LEU a -78
REMARK 465 ALA a -77
REMARK 465 LEU a -76
REMARK 465 LEU a -75
REMARK 465 ALA a -74
REMARK 465 LEU a -73
REMARK 465 TRP a -72
REMARK 465 GLY a -71
REMARK 465 PRO a -70
REMARK 465 ASP a -69
REMARK 465 PRO a -68
REMARK 465 ALA a -67
REMARK 465 ALA a -66
REMARK 465 ALA a -65
REMARK 465 PHE a -64
REMARK 465 VAL a -63
REMARK 465 ASN a -62
REMARK 465 GLN a -61
REMARK 465 HIS a -60
REMARK 465 LEU a -59
REMARK 465 CYS a -58
REMARK 465 GLY a -57
REMARK 465 SER a -56
REMARK 465 HIS a -55
REMARK 465 LEU a -54
REMARK 465 VAL a -53
REMARK 465 GLU a -52
REMARK 465 ALA a -51
REMARK 465 LEU a -50
REMARK 465 TYR a -49
REMARK 465 LEU a -48
REMARK 465 VAL a -47
REMARK 465 CYS a -46
REMARK 465 GLY a -45
REMARK 465 GLU a -44
REMARK 465 ARG a -43
REMARK 465 GLY a -42
REMARK 465 PHE a -41
REMARK 465 PHE a -40
REMARK 465 TYR a -39
REMARK 465 THR a -38
REMARK 465 PRO a -37
REMARK 465 LYS a -36
REMARK 465 THR a -35
REMARK 465 ARG a -34
REMARK 465 ARG a -33
REMARK 465 GLU a -32
REMARK 465 ALA a -31
REMARK 465 GLU a -30
REMARK 465 ASP a -29
REMARK 465 LEU a -28
REMARK 465 GLN a -27
REMARK 465 VAL a -26
REMARK 465 GLY a -25
REMARK 465 GLN a -24
REMARK 465 VAL a -23
REMARK 465 GLU a -22
REMARK 465 LEU a -21
REMARK 465 GLY a -20
REMARK 465 GLY a -19
REMARK 465 GLY a -18
REMARK 465 PRO a -17
REMARK 465 GLY a -16
REMARK 465 ALA a -15
REMARK 465 GLY a -14
REMARK 465 SER a -13
REMARK 465 LEU a -12
REMARK 465 GLN a -11
REMARK 465 PRO a -10
REMARK 465 LEU a -9
REMARK 465 ALA a -8
REMARK 465 LEU a -7
REMARK 465 GLU a -6
REMARK 465 GLY a -5
REMARK 465 SER a -4
REMARK 465 LEU a -3
REMARK 465 GLN a -2
REMARK 465 LYS a -1
REMARK 465 ARG a 0
REMARK 465 MET c -88
REMARK 465 ALA c -87
REMARK 465 LEU c -86
REMARK 465 TRP c -85
REMARK 465 MET c -84
REMARK 465 ARG c -83
REMARK 465 LEU c -82
REMARK 465 LEU c -81
REMARK 465 PRO c -80
REMARK 465 LEU c -79
REMARK 465 LEU c -78
REMARK 465 ALA c -77
REMARK 465 LEU c -76
REMARK 465 LEU c -75
REMARK 465 ALA c -74
REMARK 465 LEU c -73
REMARK 465 TRP c -72
REMARK 465 GLY c -71
REMARK 465 PRO c -70
REMARK 465 ASP c -69
REMARK 465 PRO c -68
REMARK 465 ALA c -67
REMARK 465 ALA c -66
REMARK 465 ALA c -65
REMARK 465 PHE c -64
REMARK 465 VAL c -63
REMARK 465 ASN c -62
REMARK 465 GLN c -61
REMARK 465 HIS c -60
REMARK 465 LEU c -59
REMARK 465 CYS c -58
REMARK 465 GLY c -57
REMARK 465 SER c -56
REMARK 465 HIS c -55
REMARK 465 LEU c -54
REMARK 465 VAL c -53
REMARK 465 GLU c -52
REMARK 465 ALA c -51
REMARK 465 LEU c -50
REMARK 465 TYR c -49
REMARK 465 LEU c -48
REMARK 465 VAL c -47
REMARK 465 CYS c -46
REMARK 465 GLY c -45
REMARK 465 GLU c -44
REMARK 465 ARG c -43
REMARK 465 GLY c -42
REMARK 465 PHE c -41
REMARK 465 PHE c -40
REMARK 465 TYR c -39
REMARK 465 THR c -38
REMARK 465 PRO c -37
REMARK 465 LYS c -36
REMARK 465 THR c -35
REMARK 465 ARG c -34
REMARK 465 ARG c -33
REMARK 465 GLU c -32
REMARK 465 ALA c -31
REMARK 465 GLU c -30
REMARK 465 ASP c -29
REMARK 465 LEU c -28
REMARK 465 GLN c -27
REMARK 465 VAL c -26
REMARK 465 GLY c -25
REMARK 465 GLN c -24
REMARK 465 VAL c -23
REMARK 465 GLU c -22
REMARK 465 LEU c -21
REMARK 465 GLY c -20
REMARK 465 GLY c -19
REMARK 465 GLY c -18
REMARK 465 PRO c -17
REMARK 465 GLY c -16
REMARK 465 ALA c -15
REMARK 465 GLY c -14
REMARK 465 SER c -13
REMARK 465 LEU c -12
REMARK 465 GLN c -11
REMARK 465 PRO c -10
REMARK 465 LEU c -9
REMARK 465 ALA c -8
REMARK 465 LEU c -7
REMARK 465 GLU c -6
REMARK 465 GLY c -5
REMARK 465 SER c -4
REMARK 465 LEU c -3
REMARK 465 GLN c -2
REMARK 465 LYS c -1
REMARK 465 ARG c 0
REMARK 465 LEU c 16
REMARK 465 GLU c 17
REMARK 465 ASN c 18
REMARK 465 TYR c 19
REMARK 465 CYS c 20
REMARK 465 ASN c 21
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 GLU A 365 CG CD OE1 OE2
REMARK 470 LYS A 542 CG CD CE NZ
REMARK 470 GLU A 543 CG CD OE1 OE2
REMARK 470 GLU A 934 CG CD OE1 OE2
REMARK 470 GLU A 997 CG CD OE1 OE2
REMARK 470 GLU B 365 CG CD OE1 OE2
REMARK 470 LYS B 657 CG CD CE NZ
REMARK 470 ASP B 705 CG OD1 OD2
REMARK 470 VAL B 764 CG1 CG2
REMARK 470 ARG B 765 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 934 CG CD OE1 OE2
REMARK 470 GLU B 997 CG CD OE1 OE2
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 LEU A 264 OG1 THR A 268 2.19
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 CYS c 6 CA - CB - SG ANGL. DEV. = 8.0 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 SER A 57 76.50 59.58
REMARK 500 PRO A 58 73.25 -64.62
REMARK 500 HIS A 155 -53.32 -135.45
REMARK 500 ASN A 252 -157.38 -159.00
REMARK 500 LYS A 427 158.30 175.35
REMARK 500 GLU A 453 13.04 -141.39
REMARK 500 GLU A 503 68.55 37.10
REMARK 500 MET A 690 33.56 -97.26
REMARK 500 LEU A 720 32.24 -90.15
REMARK 500 PRO A 772 43.47 -81.24
REMARK 500 ASP A 773 -13.72 71.15
REMARK 500 ARG A 774 -23.69 -141.93
REMARK 500 THR A 797 -75.31 -67.50
REMARK 500 ASP A 798 -171.21 -176.96
REMARK 500 GLU A 853 79.10 -102.80
REMARK 500 ASP A 895 104.74 -161.71
REMARK 500 THR A 930 56.17 -94.71
REMARK 500 ASP A 947 52.59 -93.29
REMARK 500 SER B 154 -176.94 -68.21
REMARK 500 ASN B 252 -177.35 -173.66
REMARK 500 GLN B 294 65.74 -101.83
REMARK 500 GLU B 295 -11.34 69.78
REMARK 500 LYS B 427 175.27 177.13
REMARK 500 LYS B 558 118.15 -164.23
REMARK 500 PRO B 570 47.38 -84.84
REMARK 500 LEU B 763 30.25 -96.37
REMARK 500 PRO B 772 39.27 -83.15
REMARK 500 ASP B 773 -13.10 77.78
REMARK 500 ARG B 774 -1.50 -148.11
REMARK 500 SER C 34 -162.26 -79.42
REMARK 500 ALA C 95 -168.40 -166.95
REMARK 500 ASP C 110 -36.70 -134.51
REMARK 500 ALA D 33 58.09 -140.55
REMARK 500 ALA D 52 -4.73 71.12
REMARK 500 ASP E 152 63.18 60.02
REMARK 500 ALA F 33 16.50 -140.24
REMARK 500 ALA F 52 -4.92 67.59
REMARK 500 ASP F 83 56.40 -94.31
REMARK 500 TYR F 93 -169.29 -121.36
REMARK 500 ASP F 171 23.12 -148.11
REMARK 500 ASN a 18 137.57 -170.47
REMARK 500 GLN c 5 146.81 -174.74
REMARK 500 CYS c 7 -126.32 41.78
REMARK 500 ILE c 10 26.61 -141.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7062 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN INSULIN DEGRADING ENZYME IN COMPLEX WITH
REMARK 900 INSULIN
REMARK 900 RELATED ID: 6B3Q RELATED DB: PDB
REMARK 900 RELATED ID: EMD-7041 RELATED DB: EMDB
REMARK 900 RELATED ID: 6B7Y RELATED DB: PDB
REMARK 900 RELATED ID: EMD-7065 RELATED DB: EMDB
REMARK 900 RELATED ID: 6B7Z RELATED DB: PDB
REMARK 900 RELATED ID: EMD-7066 RELATED DB: EMDB
DBREF 6B70 A 46 1011 UNP P14735 IDE_HUMAN 46 1011
DBREF 6B70 B 46 1011 UNP P14735 IDE_HUMAN 46 1011
DBREF 6B70 C 4 126 PDB 6B70 6B70 4 126
DBREF 6B70 C 127 221 UNP P0DOX5 IGG1_HUMAN 125 219
DBREF 6B70 D 2 105 PDB 6B70 6B70 2 105
DBREF 6B70 D 106 212 UNP Q6GMX0 Q6GMX0_HUMAN 127 233
DBREF 6B70 E 4 126 PDB 6B70 6B70 4 126
DBREF 6B70 E 127 221 UNP P0DOX5 IGG1_HUMAN 125 219
DBREF 6B70 F 2 105 PDB 6B70 6B70 2 105
DBREF 6B70 F 106 212 UNP Q6GMX0 Q6GMX0_HUMAN 127 233
DBREF 6B70 a -88 21 UNP P01308 INS_HUMAN 1 110
DBREF 6B70 c -88 21 UNP P01308 INS_HUMAN 1 110
SEQADV 6B70 LEU A 110 UNP P14735 CYS 110 CONFLICT
SEQADV 6B70 SER A 171 UNP P14735 CYS 171 CONFLICT
SEQADV 6B70 ALA A 178 UNP P14735 CYS 178 CONFLICT
SEQADV 6B70 VAL A 257 UNP P14735 CYS 257 CONFLICT
SEQADV 6B70 LEU A 414 UNP P14735 CYS 414 CONFLICT
SEQADV 6B70 ASN A 573 UNP P14735 CYS 573 CONFLICT
SEQADV 6B70 SER A 590 UNP P14735 CYS 590 CONFLICT
SEQADV 6B70 SER A 789 UNP P14735 CYS 789 CONFLICT
SEQADV 6B70 ALA A 812 UNP P14735 CYS 812 CONFLICT
SEQADV 6B70 ALA A 819 UNP P14735 CYS 819 CONFLICT
SEQADV 6B70 SER A 904 UNP P14735 CYS 904 CONFLICT
SEQADV 6B70 LEU B 110 UNP P14735 CYS 110 CONFLICT
SEQADV 6B70 SER B 171 UNP P14735 CYS 171 CONFLICT
SEQADV 6B70 ALA B 178 UNP P14735 CYS 178 CONFLICT
SEQADV 6B70 VAL B 257 UNP P14735 CYS 257 CONFLICT
SEQADV 6B70 LEU B 414 UNP P14735 CYS 414 CONFLICT
SEQADV 6B70 ASN B 573 UNP P14735 CYS 573 CONFLICT
SEQADV 6B70 SER B 590 UNP P14735 CYS 590 CONFLICT
SEQADV 6B70 SER B 789 UNP P14735 CYS 789 CONFLICT
SEQADV 6B70 ALA B 812 UNP P14735 CYS 812 CONFLICT
SEQADV 6B70 ALA B 819 UNP P14735 CYS 819 CONFLICT
SEQADV 6B70 SER B 904 UNP P14735 CYS 904 CONFLICT
SEQRES 1 A 966 ALA ILE LYS ARG ILE GLY ASN HIS ILE THR LYS SER PRO
SEQRES 2 A 966 GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU LEU ALA ASN
SEQRES 3 A 966 GLY ILE LYS VAL LEU LEU ILE SER ASP PRO THR THR ASP
SEQRES 4 A 966 LYS SER SER ALA ALA LEU ASP VAL HIS ILE GLY SER LEU
SEQRES 5 A 966 SER ASP PRO PRO ASN ILE ALA GLY LEU SER HIS PHE LEU
SEQRES 6 A 966 GLU HIS MET LEU PHE LEU GLY THR LYS LYS TYR PRO LYS
SEQRES 7 A 966 GLU ASN GLU TYR SER GLN PHE LEU SER GLU HIS ALA GLY
SEQRES 8 A 966 SER SER ASN ALA PHE THR SER GLY GLU HIS THR ASN TYR
SEQRES 9 A 966 TYR PHE ASP VAL SER HIS GLU HIS LEU GLU GLY ALA LEU
SEQRES 10 A 966 ASP ARG PHE ALA GLN PHE PHE LEU SER PRO LEU PHE ASP
SEQRES 11 A 966 GLU SER ALA LYS ASP ARG GLU VAL ASN ALA VAL ASP SER
SEQRES 12 A 966 GLU HIS GLU LYS ASN VAL MET ASN ASP ALA TRP ARG LEU
SEQRES 13 A 966 PHE GLN LEU GLU LYS ALA THR GLY ASN PRO LYS HIS PRO
SEQRES 14 A 966 PHE SER LYS PHE GLY THR GLY ASN LYS TYR THR LEU GLU
SEQRES 15 A 966 THR ARG PRO ASN GLN GLU GLY ILE ASP VAL ARG GLN GLU
SEQRES 16 A 966 LEU LEU LYS PHE HIS SER ALA TYR TYR SER SER ASN LEU
SEQRES 17 A 966 MET ALA VAL VAL VAL LEU GLY ARG GLU SER LEU ASP ASP
SEQRES 18 A 966 LEU THR ASN LEU VAL VAL LYS LEU PHE SER GLU VAL GLU
SEQRES 19 A 966 ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO GLU HIS PRO
SEQRES 20 A 966 PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR LYS ILE VAL
SEQRES 21 A 966 PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL THR PHE PRO
SEQRES 22 A 966 ILE PRO ASP LEU GLN LYS TYR TYR LYS SER ASN PRO GLY
SEQRES 23 A 966 HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU GLY PRO GLY
SEQRES 24 A 966 SER LEU LEU SER GLU LEU LYS SER LYS GLY TRP VAL ASN
SEQRES 25 A 966 THR LEU VAL GLY GLY GLN LYS GLU GLY ALA ARG GLY PHE
SEQRES 26 A 966 MET PHE PHE ILE ILE ASN VAL ASP LEU THR GLU GLU GLY
SEQRES 27 A 966 LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS MET PHE GLN
SEQRES 28 A 966 TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO GLN GLU TRP
SEQRES 29 A 966 VAL PHE GLN GLU LEU LYS ASP LEU ASN ALA VAL ALA PHE
SEQRES 30 A 966 ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY TYR THR SER
SEQRES 31 A 966 LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO LEU GLU GLU
SEQRES 32 A 966 VAL LEU THR ALA GLU TYR LEU LEU GLU GLU PHE ARG PRO
SEQRES 33 A 966 ASP LEU ILE GLU MET VAL LEU ASP LYS LEU ARG PRO GLU
SEQRES 34 A 966 ASN VAL ARG VAL ALA ILE VAL SER LYS SER PHE GLU GLY
SEQRES 35 A 966 LYS THR ASP ARG THR GLU GLU TRP TYR GLY THR GLN TYR
SEQRES 36 A 966 LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE LYS LYS TRP
SEQRES 37 A 966 GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS LEU PRO THR
SEQRES 38 A 966 LYS ASN GLU PHE ILE PRO THR ASN PHE GLU ILE LEU PRO
SEQRES 39 A 966 LEU GLU LYS GLU ALA THR PRO TYR PRO ALA LEU ILE LYS
SEQRES 40 A 966 ASP THR ALA MET SER LYS LEU TRP PHE LYS GLN ASP ASP
SEQRES 41 A 966 LYS PHE PHE LEU PRO LYS ALA ASN LEU ASN PHE GLU PHE
SEQRES 42 A 966 PHE SER PRO PHE ALA TYR VAL ASP PRO LEU HIS SER ASN
SEQRES 43 A 966 MET ALA TYR LEU TYR LEU GLU LEU LEU LYS ASP SER LEU
SEQRES 44 A 966 ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA GLY LEU SER
SEQRES 45 A 966 TYR ASP LEU GLN ASN THR ILE TYR GLY MET TYR LEU SER
SEQRES 46 A 966 VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE LEU LEU LYS
SEQRES 47 A 966 LYS ILE ILE GLU LYS MET ALA THR PHE GLU ILE ASP GLU
SEQRES 48 A 966 LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR MET ARG SER
SEQRES 49 A 966 LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS GLN HIS ALA
SEQRES 50 A 966 MET TYR TYR LEU ARG LEU LEU MET THR GLU VAL ALA TRP
SEQRES 51 A 966 THR LYS ASP GLU LEU LYS GLU ALA LEU ASP ASP VAL THR
SEQRES 52 A 966 LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN LEU LEU SER
SEQRES 53 A 966 ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY ASN ILE THR
SEQRES 54 A 966 LYS GLN ALA ALA LEU GLY ILE MET GLN MET VAL GLU ASP
SEQRES 55 A 966 THR LEU ILE GLU HIS ALA HIS THR LYS PRO LEU LEU PRO
SEQRES 56 A 966 SER GLN LEU VAL ARG TYR ARG GLU VAL GLN LEU PRO ASP
SEQRES 57 A 966 ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN GLU VAL HIS
SEQRES 58 A 966 ASN ASN SER GLY ILE GLU ILE TYR TYR GLN THR ASP MET
SEQRES 59 A 966 GLN SER THR SER GLU ASN MET PHE LEU GLU LEU PHE ALA
SEQRES 60 A 966 GLN ILE ILE SER GLU PRO ALA PHE ASN THR LEU ARG THR
SEQRES 61 A 966 LYS GLU GLN LEU GLY TYR ILE VAL PHE SER GLY PRO ARG
SEQRES 62 A 966 ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE ILE ILE GLN
SEQRES 63 A 966 SER GLU LYS PRO PRO HIS TYR LEU GLU SER ARG VAL GLU
SEQRES 64 A 966 ALA PHE LEU ILE THR MET GLU LYS SER ILE GLU ASP MET
SEQRES 65 A 966 THR GLU GLU ALA PHE GLN LYS HIS ILE GLN ALA LEU ALA
SEQRES 66 A 966 ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU SER ALA GLU
SEQRES 67 A 966 SER ALA LYS TYR TRP GLY GLU ILE ILE SER GLN GLN TYR
SEQRES 68 A 966 ASN PHE ASP ARG ASP ASN THR GLU VAL ALA TYR LEU LYS
SEQRES 69 A 966 THR LEU THR LYS GLU ASP ILE ILE LYS PHE TYR LYS GLU
SEQRES 70 A 966 MET LEU ALA VAL ASP ALA PRO ARG ARG HIS LYS VAL SER
SEQRES 71 A 966 VAL HIS VAL LEU ALA ARG GLU MET ASP SER CYS PRO VAL
SEQRES 72 A 966 VAL GLY GLU PHE PRO CYS GLN ASN ASP ILE ASN LEU SER
SEQRES 73 A 966 GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL ILE GLN ASN
SEQRES 74 A 966 MET THR GLU PHE LYS ARG GLY LEU PRO LEU PHE PRO LEU
SEQRES 75 A 966 VAL LYS PRO HIS
SEQRES 1 B 966 ALA ILE LYS ARG ILE GLY ASN HIS ILE THR LYS SER PRO
SEQRES 2 B 966 GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU LEU ALA ASN
SEQRES 3 B 966 GLY ILE LYS VAL LEU LEU ILE SER ASP PRO THR THR ASP
SEQRES 4 B 966 LYS SER SER ALA ALA LEU ASP VAL HIS ILE GLY SER LEU
SEQRES 5 B 966 SER ASP PRO PRO ASN ILE ALA GLY LEU SER HIS PHE LEU
SEQRES 6 B 966 GLU HIS MET LEU PHE LEU GLY THR LYS LYS TYR PRO LYS
SEQRES 7 B 966 GLU ASN GLU TYR SER GLN PHE LEU SER GLU HIS ALA GLY
SEQRES 8 B 966 SER SER ASN ALA PHE THR SER GLY GLU HIS THR ASN TYR
SEQRES 9 B 966 TYR PHE ASP VAL SER HIS GLU HIS LEU GLU GLY ALA LEU
SEQRES 10 B 966 ASP ARG PHE ALA GLN PHE PHE LEU SER PRO LEU PHE ASP
SEQRES 11 B 966 GLU SER ALA LYS ASP ARG GLU VAL ASN ALA VAL ASP SER
SEQRES 12 B 966 GLU HIS GLU LYS ASN VAL MET ASN ASP ALA TRP ARG LEU
SEQRES 13 B 966 PHE GLN LEU GLU LYS ALA THR GLY ASN PRO LYS HIS PRO
SEQRES 14 B 966 PHE SER LYS PHE GLY THR GLY ASN LYS TYR THR LEU GLU
SEQRES 15 B 966 THR ARG PRO ASN GLN GLU GLY ILE ASP VAL ARG GLN GLU
SEQRES 16 B 966 LEU LEU LYS PHE HIS SER ALA TYR TYR SER SER ASN LEU
SEQRES 17 B 966 MET ALA VAL VAL VAL LEU GLY ARG GLU SER LEU ASP ASP
SEQRES 18 B 966 LEU THR ASN LEU VAL VAL LYS LEU PHE SER GLU VAL GLU
SEQRES 19 B 966 ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO GLU HIS PRO
SEQRES 20 B 966 PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR LYS ILE VAL
SEQRES 21 B 966 PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL THR PHE PRO
SEQRES 22 B 966 ILE PRO ASP LEU GLN LYS TYR TYR LYS SER ASN PRO GLY
SEQRES 23 B 966 HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU GLY PRO GLY
SEQRES 24 B 966 SER LEU LEU SER GLU LEU LYS SER LYS GLY TRP VAL ASN
SEQRES 25 B 966 THR LEU VAL GLY GLY GLN LYS GLU GLY ALA ARG GLY PHE
SEQRES 26 B 966 MET PHE PHE ILE ILE ASN VAL ASP LEU THR GLU GLU GLY
SEQRES 27 B 966 LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS MET PHE GLN
SEQRES 28 B 966 TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO GLN GLU TRP
SEQRES 29 B 966 VAL PHE GLN GLU LEU LYS ASP LEU ASN ALA VAL ALA PHE
SEQRES 30 B 966 ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY TYR THR SER
SEQRES 31 B 966 LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO LEU GLU GLU
SEQRES 32 B 966 VAL LEU THR ALA GLU TYR LEU LEU GLU GLU PHE ARG PRO
SEQRES 33 B 966 ASP LEU ILE GLU MET VAL LEU ASP LYS LEU ARG PRO GLU
SEQRES 34 B 966 ASN VAL ARG VAL ALA ILE VAL SER LYS SER PHE GLU GLY
SEQRES 35 B 966 LYS THR ASP ARG THR GLU GLU TRP TYR GLY THR GLN TYR
SEQRES 36 B 966 LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE LYS LYS TRP
SEQRES 37 B 966 GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS LEU PRO THR
SEQRES 38 B 966 LYS ASN GLU PHE ILE PRO THR ASN PHE GLU ILE LEU PRO
SEQRES 39 B 966 LEU GLU LYS GLU ALA THR PRO TYR PRO ALA LEU ILE LYS
SEQRES 40 B 966 ASP THR ALA MET SER LYS LEU TRP PHE LYS GLN ASP ASP
SEQRES 41 B 966 LYS PHE PHE LEU PRO LYS ALA ASN LEU ASN PHE GLU PHE
SEQRES 42 B 966 PHE SER PRO PHE ALA TYR VAL ASP PRO LEU HIS SER ASN
SEQRES 43 B 966 MET ALA TYR LEU TYR LEU GLU LEU LEU LYS ASP SER LEU
SEQRES 44 B 966 ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA GLY LEU SER
SEQRES 45 B 966 TYR ASP LEU GLN ASN THR ILE TYR GLY MET TYR LEU SER
SEQRES 46 B 966 VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE LEU LEU LYS
SEQRES 47 B 966 LYS ILE ILE GLU LYS MET ALA THR PHE GLU ILE ASP GLU
SEQRES 48 B 966 LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR MET ARG SER
SEQRES 49 B 966 LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS GLN HIS ALA
SEQRES 50 B 966 MET TYR TYR LEU ARG LEU LEU MET THR GLU VAL ALA TRP
SEQRES 51 B 966 THR LYS ASP GLU LEU LYS GLU ALA LEU ASP ASP VAL THR
SEQRES 52 B 966 LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN LEU LEU SER
SEQRES 53 B 966 ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY ASN ILE THR
SEQRES 54 B 966 LYS GLN ALA ALA LEU GLY ILE MET GLN MET VAL GLU ASP
SEQRES 55 B 966 THR LEU ILE GLU HIS ALA HIS THR LYS PRO LEU LEU PRO
SEQRES 56 B 966 SER GLN LEU VAL ARG TYR ARG GLU VAL GLN LEU PRO ASP
SEQRES 57 B 966 ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN GLU VAL HIS
SEQRES 58 B 966 ASN ASN SER GLY ILE GLU ILE TYR TYR GLN THR ASP MET
SEQRES 59 B 966 GLN SER THR SER GLU ASN MET PHE LEU GLU LEU PHE ALA
SEQRES 60 B 966 GLN ILE ILE SER GLU PRO ALA PHE ASN THR LEU ARG THR
SEQRES 61 B 966 LYS GLU GLN LEU GLY TYR ILE VAL PHE SER GLY PRO ARG
SEQRES 62 B 966 ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE ILE ILE GLN
SEQRES 63 B 966 SER GLU LYS PRO PRO HIS TYR LEU GLU SER ARG VAL GLU
SEQRES 64 B 966 ALA PHE LEU ILE THR MET GLU LYS SER ILE GLU ASP MET
SEQRES 65 B 966 THR GLU GLU ALA PHE GLN LYS HIS ILE GLN ALA LEU ALA
SEQRES 66 B 966 ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU SER ALA GLU
SEQRES 67 B 966 SER ALA LYS TYR TRP GLY GLU ILE ILE SER GLN GLN TYR
SEQRES 68 B 966 ASN PHE ASP ARG ASP ASN THR GLU VAL ALA TYR LEU LYS
SEQRES 69 B 966 THR LEU THR LYS GLU ASP ILE ILE LYS PHE TYR LYS GLU
SEQRES 70 B 966 MET LEU ALA VAL ASP ALA PRO ARG ARG HIS LYS VAL SER
SEQRES 71 B 966 VAL HIS VAL LEU ALA ARG GLU MET ASP SER CYS PRO VAL
SEQRES 72 B 966 VAL GLY GLU PHE PRO CYS GLN ASN ASP ILE ASN LEU SER
SEQRES 73 B 966 GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL ILE GLN ASN
SEQRES 74 B 966 MET THR GLU PHE LYS ARG GLY LEU PRO LEU PHE PRO LEU
SEQRES 75 B 966 VAL LYS PRO HIS
SEQRES 1 C 218 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 C 218 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 C 218 PHE ASN ILE SER SER SER SER ILE HIS TRP VAL ARG GLN
SEQRES 4 C 218 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE TYR
SEQRES 5 C 218 SER TYR SER GLY SER THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 C 218 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR
SEQRES 7 C 218 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 C 218 ALA VAL TYR TYR CYS ALA ARG HIS TYR SER ALA VAL ALA
SEQRES 9 C 218 GLY LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 C 218 PHE ASN GLN ILE LYS PRO PRO SER VAL PHE PRO LEU ALA
SEQRES 11 C 218 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 12 C 218 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 13 C 218 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 14 C 218 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 15 C 218 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 16 C 218 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 17 C 218 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO
SEQRES 1 D 211 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 D 211 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 D 211 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 D 211 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 D 211 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 D 211 ARG SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU
SEQRES 7 D 211 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER
SEQRES 8 D 211 TYR PHE ASN PRO ILE THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 D 211 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 D 211 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 D 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 D 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 D 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 D 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 D 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 D 211 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 D 211 PHE ASN ARG
SEQRES 1 E 218 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 E 218 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 E 218 PHE ASN ILE SER SER SER SER ILE HIS TRP VAL ARG GLN
SEQRES 4 E 218 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE TYR
SEQRES 5 E 218 SER TYR SER GLY SER THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 E 218 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR
SEQRES 7 E 218 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 E 218 ALA VAL TYR TYR CYS ALA ARG HIS TYR SER ALA VAL ALA
SEQRES 9 E 218 GLY LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 E 218 PHE ASN GLN ILE LYS PRO PRO SER VAL PHE PRO LEU ALA
SEQRES 11 E 218 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 12 E 218 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 13 E 218 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 14 E 218 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 15 E 218 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 16 E 218 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 17 E 218 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO
SEQRES 1 F 211 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 F 211 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 F 211 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 F 211 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 F 211 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 F 211 ARG SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU
SEQRES 7 F 211 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER
SEQRES 8 F 211 TYR PHE ASN PRO ILE THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 F 211 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 F 211 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 F 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 F 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 F 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 F 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 F 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 F 211 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 F 211 PHE ASN ARG
SEQRES 1 a 110 MET ALA LEU TRP MET ARG LEU LEU PRO LEU LEU ALA LEU
SEQRES 2 a 110 LEU ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA PHE VAL
SEQRES 3 a 110 ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU ALA LEU
SEQRES 4 a 110 TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR THR PRO
SEQRES 5 a 110 LYS THR ARG ARG GLU ALA GLU ASP LEU GLN VAL GLY GLN
SEQRES 6 a 110 VAL GLU LEU GLY GLY GLY PRO GLY ALA GLY SER LEU GLN
SEQRES 7 a 110 PRO LEU ALA LEU GLU GLY SER LEU GLN LYS ARG GLY ILE
SEQRES 8 a 110 VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU TYR GLN
SEQRES 9 a 110 LEU GLU ASN TYR CYS ASN
SEQRES 1 c 110 MET ALA LEU TRP MET ARG LEU LEU PRO LEU LEU ALA LEU
SEQRES 2 c 110 LEU ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA PHE VAL
SEQRES 3 c 110 ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU ALA LEU
SEQRES 4 c 110 TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR THR PRO
SEQRES 5 c 110 LYS THR ARG ARG GLU ALA GLU ASP LEU GLN VAL GLY GLN
SEQRES 6 c 110 VAL GLU LEU GLY GLY GLY PRO GLY ALA GLY SER LEU GLN
SEQRES 7 c 110 PRO LEU ALA LEU GLU GLY SER LEU GLN LYS ARG GLY ILE
SEQRES 8 c 110 VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU TYR GLN
SEQRES 9 c 110 LEU GLU ASN TYR CYS ASN
HELIX 1 AA1 GLY A 105 LEU A 114 1 10
HELIX 2 AA2 ASN A 125 HIS A 134 1 10
HELIX 3 AA3 HIS A 157 GLN A 167 1 11
HELIX 4 AA4 ASP A 175 LYS A 192 1 18
HELIX 5 AA5 ASN A 196 THR A 208 1 13
HELIX 6 AA6 HIS A 213 LYS A 217 5 5
HELIX 7 AA7 ASN A 222 GLU A 227 1 6
HELIX 8 AA8 GLU A 227 GLU A 233 1 7
HELIX 9 AA9 ASP A 236 TYR A 248 1 13
HELIX 10 AB1 ASP A 265 PHE A 275 1 11
HELIX 11 AB2 ASN A 329 GLY A 339 1 11
HELIX 12 AB3 SER A 345 LYS A 353 1 9
HELIX 13 AB4 GLY A 383 LEU A 385 5 3
HELIX 14 AB5 HIS A 386 GLY A 405 1 20
HELIX 15 AB6 GLU A 408 PHE A 424 1 17
HELIX 16 AB7 GLY A 432 LEU A 441 1 10
HELIX 17 AB8 ARG A 460 LEU A 471 1 12
HELIX 18 AB9 ARG A 472 VAL A 476 5 5
HELIX 19 AC1 PRO A 506 ALA A 516 1 11
HELIX 20 AC2 ASP A 586 GLY A 615 1 30
HELIX 21 AC3 LYS A 637 THR A 651 1 15
HELIX 22 AC4 ASP A 655 ASN A 671 1 17
HELIX 23 AC5 ASN A 672 GLU A 676 5 5
HELIX 24 AC6 GLN A 677 MET A 690 1 14
HELIX 25 AC7 THR A 696 ALA A 703 1 8
HELIX 26 AC8 LEU A 704 ASP A 706 5 3
HELIX 27 AC9 THR A 708 LEU A 720 1 13
HELIX 28 AD1 THR A 734 HIS A 754 1 21
HELIX 29 AD2 SER A 801 ILE A 815 1 15
HELIX 30 AD3 ILE A 815 LEU A 823 1 9
HELIX 31 AD4 PRO A 855 ASP A 876 1 22
HELIX 32 AD5 THR A 878 LEU A 894 1 17
HELIX 33 AD6 LYS A 899 SER A 913 1 15
HELIX 34 AD7 ASP A 919 LYS A 929 1 11
HELIX 35 AD8 THR A 932 LEU A 944 1 13
HELIX 36 AD9 ASN A 994 GLY A 1001 1 8
HELIX 37 AE1 GLY B 105 LEU B 116 1 12
HELIX 38 AE2 ASN B 125 GLU B 133 1 9
HELIX 39 AE3 HIS B 157 ARG B 164 1 8
HELIX 40 AE4 ALA B 166 SER B 171 1 6
HELIX 41 AE5 ASP B 175 ASN B 193 1 19
HELIX 42 AE6 ASN B 196 THR B 208 1 13
HELIX 43 AE7 HIS B 213 LYS B 217 5 5
HELIX 44 AE8 ASN B 222 GLU B 227 1 6
HELIX 45 AE9 THR B 228 GLU B 233 1 6
HELIX 46 AF1 ASP B 236 TYR B 249 1 14
HELIX 47 AF2 SER B 250 ASN B 252 5 3
HELIX 48 AF3 ASP B 265 PHE B 275 1 11
HELIX 49 AF4 ASN B 329 GLY B 339 1 11
HELIX 50 AF5 SER B 345 LYS B 353 1 9
HELIX 51 AF6 GLU B 381 LEU B 385 5 5
HELIX 52 AF7 HIS B 386 GLY B 405 1 20
HELIX 53 AF8 GLN B 407 PHE B 424 1 18
HELIX 54 AF9 TYR B 433 LEU B 441 1 9
HELIX 55 AG1 ARG B 460 ASP B 469 1 10
HELIX 56 AG2 LYS B 470 LEU B 471 5 2
HELIX 57 AG3 ARG B 472 VAL B 476 5 5
HELIX 58 AG4 PRO B 506 ASN B 515 1 10
HELIX 59 AG5 PRO B 581 VAL B 585 5 5
HELIX 60 AG6 ASP B 586 ALA B 614 1 29
HELIX 61 AG7 LYS B 637 THR B 651 1 15
HELIX 62 AG8 ASP B 655 PHE B 673 1 19
HELIX 63 AG9 ARG B 674 GLU B 676 5 3
HELIX 64 AH1 GLN B 677 MET B 690 1 14
HELIX 65 AH2 ASP B 698 ALA B 703 1 6
HELIX 66 AH3 LEU B 704 VAL B 707 5 4
HELIX 67 AH4 THR B 708 SER B 721 1 14
HELIX 68 AH5 THR B 734 HIS B 754 1 21
HELIX 69 AH6 LEU B 759 LEU B 763 5 5
HELIX 70 AH7 SER B 801 LEU B 823 1 23
HELIX 71 AH8 PRO B 855 ILE B 874 1 20
HELIX 72 AH9 THR B 878 LEU B 894 1 17
HELIX 73 AI1 LYS B 899 ILE B 912 1 14
HELIX 74 AI2 ASP B 919 LYS B 929 1 11
HELIX 75 AI3 THR B 932 GLU B 942 1 11
HELIX 76 AI4 ASN B 994 LEU B 1002 1 9
HELIX 77 AI5 ARG C 90 THR C 94 5 5
HELIX 78 AI6 SER C 135 THR C 139 5 5
HELIX 79 AI7 SER C 195 LEU C 197 5 3
HELIX 80 AI8 SER D 122 LYS D 127 1 6
HELIX 81 AI9 SER D 183 HIS D 190 1 8
HELIX 82 AJ1 ARG E 90 THR E 94 5 5
HELIX 83 AJ2 SER E 135 THR E 139 5 5
HELIX 84 AJ3 SER F 122 LYS F 127 1 6
HELIX 85 AJ4 SER F 183 GLU F 188 1 6
SHEET 1 AA1 6 GLU A 63 LEU A 69 0
SHEET 2 AA1 6 ILE A 73 SER A 79 -1 O LEU A 77 N ARG A 65
SHEET 3 AA1 6 MET A 254 GLY A 260 1 O VAL A 256 N LYS A 74
SHEET 4 AA1 6 SER A 86 VAL A 92 -1 N SER A 87 O LEU A 259
SHEET 5 AA1 6 THR A 147 VAL A 153 -1 O TYR A 149 N LEU A 90
SHEET 6 AA1 6 ASN A 139 THR A 142 -1 N ASN A 139 O TYR A 150
SHEET 1 AA2 5 LYS A 303 ILE A 304 0
SHEET 2 AA2 5 ARG A 477 SER A 482 1 O ILE A 480 N ILE A 304
SHEET 3 AA2 5 ARG A 311 PRO A 320 -1 N TYR A 314 O ALA A 479
SHEET 4 AA2 5 PHE A 370 ASP A 378 -1 O MET A 371 N ILE A 319
SHEET 5 AA2 5 LEU A 359 LYS A 364 -1 N VAL A 360 O ASN A 376
SHEET 1 AA3 2 ARG A 491 THR A 492 0
SHEET 2 AA3 2 GLN A 499 TYR A 500 -1 O TYR A 500 N ARG A 491
SHEET 1 AA4 6 ALA A 549 ASP A 553 0
SHEET 2 AA4 6 SER A 557 GLN A 563 -1 O PHE A 561 N ALA A 549
SHEET 3 AA4 6 ILE A 725 GLY A 731 1 O ALA A 727 N TRP A 560
SHEET 4 AA4 6 LYS A 571 PHE A 579 -1 N ASN A 573 O HIS A 730
SHEET 5 AA4 6 GLY A 626 TYR A 634 -1 O LEU A 629 N PHE A 576
SHEET 6 AA4 6 LEU A 616 ASN A 622 -1 N ASP A 619 O SER A 630
SHEET 1 AA5 5 TRP A 776 GLN A 780 0
SHEET 2 AA5 5 LYS A 953 VAL A 958 1 O HIS A 957 N TYR A 779
SHEET 3 AA5 5 SER A 789 TYR A 795 -1 N GLY A 790 O VAL A 958
SHEET 4 AA5 5 ILE A 843 SER A 852 -1 O SER A 852 N SER A 789
SHEET 5 AA5 5 VAL A 833 ALA A 840 -1 N PHE A 834 O ILE A 849
SHEET 1 AA6 6 GLU B 63 LEU B 69 0
SHEET 2 AA6 6 ILE B 73 SER B 79 -1 O LEU B 77 N ARG B 65
SHEET 3 AA6 6 MET B 254 GLY B 260 1 O VAL B 258 N ILE B 78
SHEET 4 AA6 6 SER B 87 VAL B 92 -1 N SER B 87 O LEU B 259
SHEET 5 AA6 6 THR B 147 ASP B 152 -1 O TYR B 149 N LEU B 90
SHEET 6 AA6 6 SER B 137 THR B 142 -1 N ASN B 139 O TYR B 150
SHEET 1 AA7 5 LYS B 303 ILE B 304 0
SHEET 2 AA7 5 ARG B 477 SER B 482 1 O SER B 482 N ILE B 304
SHEET 3 AA7 5 ARG B 311 THR B 316 -1 N TYR B 314 O ALA B 479
SHEET 4 AA7 5 ILE B 374 ASP B 378 -1 O ILE B 375 N VAL B 315
SHEET 5 AA7 5 LEU B 359 GLY B 362 -1 N VAL B 360 O ASN B 376
SHEET 1 AA8 2 ARG B 491 THR B 492 0
SHEET 2 AA8 2 GLN B 499 TYR B 500 -1 O TYR B 500 N ARG B 491
SHEET 1 AA9 6 ALA B 549 ASP B 553 0
SHEET 2 AA9 6 LYS B 558 GLN B 563 -1 O LEU B 559 N ILE B 551
SHEET 3 AA9 6 HIS B 724 GLY B 731 1 O LEU B 729 N TRP B 560
SHEET 4 AA9 6 LYS B 571 PHE B 579 -1 N ASN B 573 O HIS B 730
SHEET 5 AA9 6 GLY B 626 TYR B 634 -1 O LEU B 629 N PHE B 576
SHEET 6 AA9 6 LEU B 616 ASN B 622 -1 N SER B 617 O LYS B 632
SHEET 1 AB1 6 ILE B 832 ALA B 840 0
SHEET 2 AB1 6 ILE B 843 SER B 852 -1 O ILE B 849 N PHE B 834
SHEET 3 AB1 6 SER B 789 MET B 799 -1 N SER B 789 O SER B 852
SHEET 4 AB1 6 LYS B 953 LEU B 959 -1 O VAL B 954 N TYR B 794
SHEET 5 AB1 6 TRP B 776 ARG B 782 1 N GLN B 781 O LEU B 959
SHEET 6 AB1 6 GLU B 990 VAL B 991 1 O GLU B 990 N VAL B 778
SHEET 1 AB2 4 GLN C 6 SER C 10 0
SHEET 2 AB2 4 GLY C 19 SER C 28 -1 O ALA C 26 N VAL C 8
SHEET 3 AB2 4 THR C 81 LEU C 89 -1 O LEU C 84 N LEU C 23
SHEET 4 AB2 4 PHE C 71 ASP C 76 -1 N THR C 72 O GLN C 85
SHEET 1 AB3 6 LEU C 14 VAL C 15 0
SHEET 2 AB3 6 THR C 116 VAL C 120 1 O THR C 119 N VAL C 15
SHEET 3 AB3 6 ALA C 95 HIS C 102 -1 N ALA C 95 O VAL C 118
SHEET 4 AB3 6 ILE C 37 GLN C 42 -1 N GLN C 42 O VAL C 96
SHEET 5 AB3 6 LEU C 48 TYR C 55 -1 O GLU C 49 N ARG C 41
SHEET 6 AB3 6 SER C 60 TYR C 63 -1 O TYR C 62 N SER C 53
SHEET 1 AB4 4 LEU C 14 VAL C 15 0
SHEET 2 AB4 4 THR C 116 VAL C 120 1 O THR C 119 N VAL C 15
SHEET 3 AB4 4 ALA C 95 HIS C 102 -1 N ALA C 95 O VAL C 118
SHEET 4 AB4 4 LEU C 109 TRP C 112 -1 O TYR C 111 N ARG C 101
SHEET 1 AB5 4 SER C 128 PRO C 131 0
SHEET 2 AB5 4 THR C 143 TYR C 153 -1 O LYS C 151 N SER C 128
SHEET 3 AB5 4 TYR C 184 PRO C 193 -1 O VAL C 190 N LEU C 146
SHEET 4 AB5 4 VAL C 171 THR C 173 -1 N HIS C 172 O VAL C 189
SHEET 1 AB6 4 SER C 128 PRO C 131 0
SHEET 2 AB6 4 THR C 143 TYR C 153 -1 O LYS C 151 N SER C 128
SHEET 3 AB6 4 TYR C 184 PRO C 193 -1 O VAL C 190 N LEU C 146
SHEET 4 AB6 4 VAL C 177 LEU C 178 -1 N VAL C 177 O SER C 185
SHEET 1 AB7 3 SER C 161 TRP C 162 0
SHEET 2 AB7 3 ILE C 203 ASN C 205 -1 O ASN C 205 N SER C 161
SHEET 3 AB7 3 ASP C 216 LYS C 218 -1 O LYS C 217 N CYS C 204
SHEET 1 AB8 4 MET D 5 SER D 8 0
SHEET 2 AB8 4 VAL D 20 ALA D 26 -1 O ARG D 25 N THR D 6
SHEET 3 AB8 4 ASP D 71 ILE D 76 -1 O ILE D 76 N VAL D 20
SHEET 4 AB8 4 PHE D 63 SER D 64 -1 N SER D 64 O THR D 75
SHEET 1 AB9 4 MET D 5 SER D 8 0
SHEET 2 AB9 4 VAL D 20 ALA D 26 -1 O ARG D 25 N THR D 6
SHEET 3 AB9 4 ASP D 71 ILE D 76 -1 O ILE D 76 N VAL D 20
SHEET 4 AB9 4 ARG D 67 SER D 68 -1 N SER D 68 O ASP D 71
SHEET 1 AC1 2 SER D 11 SER D 13 0
SHEET 2 AC1 2 LYS D 104 GLU D 106 1 O LYS D 104 N LEU D 12
SHEET 1 AC2 3 LYS D 46 ILE D 49 0
SHEET 2 AC2 3 TRP D 36 GLN D 39 -1 N TRP D 36 O LEU D 48
SHEET 3 AC2 3 THR D 86 CYS D 89 -1 O THR D 86 N GLN D 39
SHEET 1 AC3 4 PHE D 117 PHE D 119 0
SHEET 2 AC3 4 ALA D 131 PHE D 140 -1 O LEU D 136 N PHE D 117
SHEET 3 AC3 4 TYR D 174 SER D 177 -1 O LEU D 176 N LEU D 137
SHEET 4 AC3 4 SER D 163 VAL D 164 -1 N SER D 163 O SER D 177
SHEET 1 AC4 3 PHE D 117 PHE D 119 0
SHEET 2 AC4 3 ALA D 131 PHE D 140 -1 O LEU D 136 N PHE D 117
SHEET 3 AC4 3 LEU D 180 LEU D 182 -1 O LEU D 180 N VAL D 133
SHEET 1 AC5 4 ALA D 154 LEU D 155 0
SHEET 2 AC5 4 ALA D 145 VAL D 151 -1 N VAL D 151 O ALA D 154
SHEET 3 AC5 4 VAL D 192 HIS D 199 -1 O ALA D 194 N LYS D 150
SHEET 4 AC5 4 THR D 207 ASN D 211 -1 O PHE D 210 N TYR D 193
SHEET 1 AC6 4 GLN E 6 SER E 10 0
SHEET 2 AC6 4 SER E 20 SER E 28 -1 O SER E 28 N GLN E 6
SHEET 3 AC6 4 THR E 81 ASN E 87 -1 O MET E 86 N LEU E 21
SHEET 4 AC6 4 PHE E 71 ASP E 76 -1 N THR E 72 O GLN E 85
SHEET 1 AC7 5 TYR E 62 TYR E 63 0
SHEET 2 AC7 5 GLU E 49 ILE E 54 -1 N SER E 53 O TYR E 62
SHEET 3 AC7 5 ILE E 37 GLN E 42 -1 N ARG E 41 O GLU E 49
SHEET 4 AC7 5 ALA E 95 CYS E 99 -1 O VAL E 96 N GLN E 42
SHEET 5 AC7 5 THR E 116 VAL E 118 -1 O VAL E 118 N ALA E 95
SHEET 1 AC8 2 ARG E 101 HIS E 102 0
SHEET 2 AC8 2 LEU E 109 TYR E 111 -1 O TYR E 111 N ARG E 101
SHEET 1 AC9 4 SER E 128 LEU E 132 0
SHEET 2 AC9 4 THR E 143 TYR E 153 -1 O LEU E 149 N PHE E 130
SHEET 3 AC9 4 LEU E 183 PRO E 193 -1 O VAL E 192 N ALA E 144
SHEET 4 AC9 4 VAL E 171 THR E 173 -1 N HIS E 172 O VAL E 189
SHEET 1 AD1 4 SER E 128 LEU E 132 0
SHEET 2 AD1 4 THR E 143 TYR E 153 -1 O LEU E 149 N PHE E 130
SHEET 3 AD1 4 LEU E 183 PRO E 193 -1 O VAL E 192 N ALA E 144
SHEET 4 AD1 4 VAL E 177 GLN E 179 -1 N GLN E 179 O LEU E 183
SHEET 1 AD2 3 SER E 161 TRP E 162 0
SHEET 2 AD2 3 TYR E 202 ASN E 205 -1 O ASN E 205 N SER E 161
SHEET 3 AD2 3 ASP E 216 VAL E 219 -1 O VAL E 219 N TYR E 202
SHEET 1 AD3 4 MET F 5 SER F 8 0
SHEET 2 AD3 4 VAL F 20 ALA F 26 -1 O ARG F 25 N THR F 6
SHEET 3 AD3 4 ASP F 71 ILE F 76 -1 O ILE F 76 N VAL F 20
SHEET 4 AD3 4 PHE F 63 SER F 64 -1 N SER F 64 O THR F 75
SHEET 1 AD4 4 MET F 5 SER F 8 0
SHEET 2 AD4 4 VAL F 20 ALA F 26 -1 O ARG F 25 N THR F 6
SHEET 3 AD4 4 ASP F 71 ILE F 76 -1 O ILE F 76 N VAL F 20
SHEET 4 AD4 4 ARG F 67 SER F 68 -1 N SER F 68 O ASP F 71
SHEET 1 AD5 2 SER F 11 SER F 13 0
SHEET 2 AD5 2 LYS F 104 GLU F 106 1 O GLU F 106 N LEU F 12
SHEET 1 AD6 5 SER F 54 LEU F 55 0
SHEET 2 AD6 5 PRO F 45 TYR F 50 -1 N TYR F 50 O SER F 54
SHEET 3 AD6 5 VAL F 34 GLN F 39 -1 N TRP F 36 O LEU F 48
SHEET 4 AD6 5 THR F 86 GLN F 91 -1 O TYR F 88 N TYR F 37
SHEET 5 AD6 5 THR F 98 PHE F 99 -1 O THR F 98 N GLN F 91
SHEET 1 AD7 4 SER F 115 PHE F 119 0
SHEET 2 AD7 4 ALA F 131 PHE F 140 -1 O LEU F 136 N PHE F 117
SHEET 3 AD7 4 TYR F 174 LEU F 182 -1 O LEU F 176 N LEU F 137
SHEET 4 AD7 4 SER F 163 VAL F 164 -1 N SER F 163 O SER F 177
SHEET 1 AD8 3 VAL F 147 VAL F 151 0
SHEET 2 AD8 3 TYR F 193 VAL F 197 -1 O GLU F 196 N GLN F 148
SHEET 3 AD8 3 VAL F 206 THR F 207 -1 O VAL F 206 N VAL F 197
SSBOND 1 CYS C 25 CYS C 99 1555 1555 2.03
SSBOND 2 CYS C 148 CYS C 204 1555 1555 2.03
SSBOND 3 CYS D 24 CYS D 89 1555 1555 2.03
SSBOND 4 CYS D 135 CYS D 195 1555 1555 2.04
SSBOND 5 CYS E 25 CYS E 99 1555 1555 2.03
SSBOND 6 CYS E 148 CYS E 204 1555 1555 2.03
SSBOND 7 CYS F 24 CYS F 89 1555 1555 2.03
SSBOND 8 CYS F 135 CYS F 195 1555 1555 2.03
SSBOND 9 CYS a 6 CYS a 11 1555 1555 2.05
SSBOND 10 CYS c 6 CYS c 11 1555 1555 2.04
CISPEP 1 PHE C 154 PRO C 155 0 -23.45
CISPEP 2 SER D 8 PRO D 9 0 -1.46
CISPEP 3 TYR D 141 PRO D 142 0 0.25
CISPEP 4 PHE E 154 PRO E 155 0 10.38
CISPEP 5 SER F 8 PRO F 9 0 -1.18
CISPEP 6 TYR F 141 PRO F 142 0 -7.82
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
