HEADER MOTOR PROTEIN 25-APR-17 5VLJ
TITLE CRYO-EM STRUCTURE OF YEAST CYTOPLASMIC DYNEIN WITH WALKER B MUTATION
TITLE 2 AT AAA3 IN PRESENCE OF ATP-VO4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYNEIN HEAVY CHAIN, CYTOPLASMIC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1448-3028,3298-4092;
COMPND 5 SYNONYM: DYNEIN HEAVY CHAIN, CYTOSOLIC, DYHC, CYTOPLASMIC DYNEIN-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR DISTRIBUTION PROTEIN PAC1;
COMPND 9 CHAIN: B, C;
COMPND 10 SYNONYM: LISSENCEPHALY-1 HOMOLOG, LIS-1, NUDF HOMOLOG, LIS1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: DYN1, DHC1, YKR054C;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 GENE: PAC1, LIS1, SCY_5321;
SOURCE 14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS CYTOPLASMIC DYNEIN, LIS1, MOTOR PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.A.CIANFROCCO,M.E.DESANTIS,Z.M.HTET,P.T.TRAN,S.L.RECK-PETERSON,
AUTHOR 2 A.E.LESCHZINER
REVDAT 4 01-JAN-20 5VLJ 1 REMARK
REVDAT 3 27-SEP-17 5VLJ 1 REMARK
REVDAT 2 20-SEP-17 5VLJ 1 JRNL
REVDAT 1 06-SEP-17 5VLJ 0
JRNL AUTH M.E.DESANTIS,M.A.CIANFROCCO,Z.M.HTET,P.T.TRAN,
JRNL AUTH 2 S.L.RECK-PETERSON,A.E.LESCHZINER
JRNL TITL LIS1 HAS TWO OPPOSING MODES OF REGULATING CYTOPLASMIC
JRNL TITL 2 DYNEIN.
JRNL REF CELL V. 170 1197 2017
JRNL REFN ISSN 1097-4172
JRNL PMID 28886386
JRNL DOI 10.1016/J.CELL.2017.08.037
REMARK 2
REMARK 2 RESOLUTION. 10.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : LEGINON, UCSF CHIMERA, ROSETTA
REMARK 3 RECONSTRUCTION SCHEMA : NULL
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 : 800.000
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) : 10.50
REMARK 3 NUMBER OF PARTICLES : 27807
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 5VLJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227343.
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 : COMPLEX BETWEEN YEAST DYNEIN
REMARK 245 (AAA3 WALKER B) WITH LIS1 IN
REMARK 245 THE PRESENCE OF ATP.VO4
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.23
REMARK 245 SAMPLE SUPPORT DETAILS : NO GRID PRETREATMENT
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4826
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TECNAI ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
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) : 50.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 36000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ILE A 2226 H LEU A 2230 1.50
REMARK 500 O TRP A 3306 HG1 THR A 3310 1.52
REMARK 500 O PHE A 2338 HG1 THR A 2341 1.53
REMARK 500 O ARG A 2586 HG1 THR A 2589 1.53
REMARK 500 O LEU A 2852 H LEU A 2856 1.53
REMARK 500 O PRO A 2419 HG SER A 2422 1.53
REMARK 500 O LYS C 366 H MET C 370 1.54
REMARK 500 O TYR A 1451 H LEU A 1455 1.54
REMARK 500 O ASN A 1542 H LEU A 1546 1.54
REMARK 500 O ILE A 2993 H ARG A 2997 1.54
REMARK 500 O LYS A 2923 HG SER A 2926 1.55
REMARK 500 O ILE A 1712 H LYS A 1716 1.55
REMARK 500 O HIS A 2787 HG SER A 2790 1.55
REMARK 500 O ILE A 3325 HG SER A 3328 1.57
REMARK 500 O GLU A 3523 HG1 THR A 3527 1.57
REMARK 500 O PRO A 2204 HG1 THR A 2208 1.57
REMARK 500 O TYR A 3683 HG SER A 3687 1.58
REMARK 500 OG1 THR A 2941 H ASP A 2942 1.58
REMARK 500 O PRO C 400 HG1 THR C 403 1.58
REMARK 500 O THR A 2472 HG1 THR A 2525 1.59
REMARK 500 O PRO A 1797 HG1 THR A 1800 1.59
REMARK 500 O GLN A 3648 H CYS A 3652 1.59
REMARK 500 O THR A 3426 H VAL A 3449 1.60
REMARK 500 O PHE A 2404 H LEU A 2408 1.60
REMARK 500 OH TYR A 3927 O ILE A 4029 2.14
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 A1766 C - N - CD ANGL. DEV. = -16.6 DEGREES
REMARK 500 TYR A1771 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 PRO A1890 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG A1917 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A2000 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PRO A2028 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO A2160 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO A2179 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 PRO A2188 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO A2204 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO A2393 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 PRO A2562 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO A2841 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO A2894 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO A2906 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO A2946 C - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO A2986 C - N - CD ANGL. DEV. = -16.5 DEGREES
REMARK 500 PRO A2989 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 TYR A3007 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PRO A3405 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO A3501 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO A3734 C - N - CD ANGL. DEV. = -16.2 DEGREES
REMARK 500 PRO A3815 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A3891 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TYR A3927 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 PRO A4025 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO B 148 C - N - CD ANGL. DEV. = -19.0 DEGREES
REMARK 500 PRO B 190 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO B 295 C - N - CD ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO B 339 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO B 390 C - N - CD ANGL. DEV. = -13.9 DEGREES
REMARK 500 PRO B 398 C - N - CD ANGL. DEV. = -19.6 DEGREES
REMARK 500 PRO B 402 C - N - CD ANGL. DEV. = -18.8 DEGREES
REMARK 500 PRO C 190 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PHE C 293 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 PRO C 295 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO C 339 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO C 398 C - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 PRO C 402 C - N - CD ANGL. DEV. = -16.9 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 LEU A1469 101.12 -26.97
REMARK 500 MET A1485 -62.53 -102.53
REMARK 500 THR A1496 -72.22 -34.89
REMARK 500 LEU A1509 -60.24 -102.42
REMARK 500 GLU A1576 108.07 -49.29
REMARK 500 ASP A1600 -51.02 -17.17
REMARK 500 SER A1601 -68.62 -17.49
REMARK 500 GLN A1603 105.83 85.56
REMARK 500 ALA A1604 -35.76 -39.40
REMARK 500 GLU A1668 56.43 -174.07
REMARK 500 SER A1719 80.39 -55.49
REMARK 500 GLU A1722 -153.52 46.86
REMARK 500 TRP A1728 -11.00 -142.33
REMARK 500 SER A1746 -32.68 -142.29
REMARK 500 SER A1752 -117.05 53.89
REMARK 500 TYR A1762 107.73 -58.88
REMARK 500 ILE A1763 -60.45 -123.49
REMARK 500 PRO A1766 -94.51 -6.11
REMARK 500 LYS A1789 33.33 70.71
REMARK 500 SER A1877 -84.31 -62.91
REMARK 500 THR A1880 96.13 -50.61
REMARK 500 LEU A1882 -64.77 61.23
REMARK 500 GLU A1883 17.29 -163.28
REMARK 500 GLU A1884 149.40 -170.33
REMARK 500 GLU A1885 106.69 -53.26
REMARK 500 PRO A1887 77.69 -66.82
REMARK 500 PRO A1900 103.06 -29.08
REMARK 500 TYR A1902 94.79 -41.06
REMARK 500 LEU A1912 -60.16 -105.47
REMARK 500 SER A1920 78.63 -56.90
REMARK 500 HIS A1965 49.80 -90.72
REMARK 500 PHE A1968 42.73 -143.93
REMARK 500 ILE A2002 -63.83 71.97
REMARK 500 CYS A2078 59.91 -152.23
REMARK 500 ASP A2139 -0.41 -151.04
REMARK 500 ASP A2140 -28.92 -174.44
REMARK 500 PHE A2145 52.78 -117.70
REMARK 500 ASP A2155 56.22 -94.69
REMARK 500 ASP A2159 77.97 -150.88
REMARK 500 PRO A2160 -30.85 -26.79
REMARK 500 ASP A2172 -25.27 145.21
REMARK 500 ASP A2197 1.25 -150.13
REMARK 500 LEU A2237 -67.34 -134.29
REMARK 500 LEU A2249 -60.43 -103.79
REMARK 500 ALA A2327 -34.96 -152.96
REMARK 500 SER A2354 -113.51 -65.00
REMARK 500 PRO A2376 79.96 -65.43
REMARK 500 SER A2379 -74.64 -150.39
REMARK 500 HIS A2383 -73.96 80.21
REMARK 500 ARG A2412 -166.53 -115.84
REMARK 500
REMARK 500 THIS ENTRY HAS 234 RAMACHANDRAN OUTLIERS.
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 ALA A 2236 LEU A 2237 -35.12
REMARK 500 PHE A 2976 TYR A 2977 37.48
REMARK 500 ARG A 3668 THR A 3669 40.81
REMARK 500 SER A 3921 GLY A 3922 35.63
REMARK 500 SER A 4058 LEU A 4059 -38.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A2236 21.19
REMARK 500 PHE A2976 -21.39
REMARK 500 ARG A3668 -21.35
REMARK 500 SER A3921 -21.63
REMARK 500 SER A4058 21.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-8706 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF YEAST CYTOPLASMIC DYNEIN WITH WALKER B
REMARK 900 MUTATION AT AAA3 IN PRESENCE OF ATP-VO4
REMARK 900 RELATED ID: EMD-8673 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF YEAST CYTOPLASMIC DYNEIN-1 WITH LIS1 AND ATP
REMARK 900 RELATED ID: 5VH9 RELATED DB: PDB
DBREF 5VLJ A 1448 3028 UNP P36022 DYHC_YEAST 1448 3028
DBREF 5VLJ A 3298 4092 UNP P36022 DYHC_YEAST 3298 4092
DBREF 5VLJ B 140 493 UNP A6ZPA6 LIS1_YEAS7 140 493
DBREF 5VLJ C 140 493 UNP A6ZPA6 LIS1_YEAS7 140 493
SEQADV 5VLJ PHE A 1575 UNP P36022 LEU 1575 CONFLICT
SEQADV 5VLJ SER A 1578 UNP P36022 PHE 1578 CONFLICT
SEQADV 5VLJ GLU A 1668 UNP P36022 GLN 1668 CONFLICT
SEQADV 5VLJ VAL A 1777 UNP P36022 ILE 1777 CONFLICT
SEQADV 5VLJ VAL A 1984 UNP P36022 ILE 1984 CONFLICT
SEQADV 5VLJ VAL A 2936 UNP P36022 ILE 2936 CONFLICT
SEQADV 5VLJ GLY A 3343 UNP P36022 ALA 3343 CONFLICT
SEQADV 5VLJ VAL A 3444 UNP P36022 ILE 3444 CONFLICT
SEQADV 5VLJ ARG A 3556 UNP P36022 LYS 3556 CONFLICT
SEQADV 5VLJ ASP A 3742 UNP P36022 ASN 3742 CONFLICT
SEQADV 5VLJ VAL A 3895 UNP P36022 PHE 3895 CONFLICT
SEQADV 5VLJ ASP A 4072 UNP P36022 ASN 4072 CONFLICT
SEQRES 1 A 2376 VAL GLN PHE TYR TRP LEU ASP LEU TYR GLY ILE LEU GLY
SEQRES 2 A 2376 GLU ASN LEU ASP ILE GLN ASN PHE LEU PRO LEU GLU THR
SEQRES 3 A 2376 SER LYS PHE LYS SER LEU THR SER GLU TYR LYS MET ILE
SEQRES 4 A 2376 THR THR ARG ALA PHE GLN LEU ASP THR THR ILE GLU VAL
SEQRES 5 A 2376 ILE HIS ILE PRO ASN PHE ASP THR THR LEU LYS LEU THR
SEQRES 6 A 2376 ILE ASP SER LEU LYS MET ILE LYS SER SER LEU SER THR
SEQRES 7 A 2376 PHE LEU GLU ARG GLN ARG ARG GLN PHE PRO ARG PHE TYR
SEQRES 8 A 2376 PHE LEU GLY ASN ASP ASP LEU LEU LYS ILE ILE GLY SER
SEQRES 9 A 2376 GLY LYS HIS HIS ASP GLN VAL SER LYS PHE MET LYS LYS
SEQRES 10 A 2376 MET PHE GLY SER ILE GLU SER ILE ILE PHE PHE GLU ASP
SEQRES 11 A 2376 SER ILE THR GLY VAL ARG SER VAL GLU GLY GLU VAL LEU
SEQRES 12 A 2376 ASN LEU ASN GLU LYS ILE GLU LEU LYS ASP SER ILE GLN
SEQRES 13 A 2376 ALA GLN GLU TRP LEU ASN ILE LEU ASP THR GLU ILE LYS
SEQRES 14 A 2376 LEU SER VAL PHE THR GLN PHE ARG ASP CYS LEU GLY GLN
SEQRES 15 A 2376 LEU LYS ASP GLY THR ASP ILE GLU VAL VAL VAL SER LYS
SEQRES 16 A 2376 TYR ILE PHE GLN ALA ILE LEU LEU SER ALA GLN VAL MET
SEQRES 17 A 2376 TRP THR GLU LEU VAL GLU LYS CYS LEU GLN THR ASN GLU
SEQRES 18 A 2376 PHE SER LYS TYR TRP LYS GLU VAL ASP MET LYS ILE LYS
SEQRES 19 A 2376 GLY LEU LEU ASP LYS LEU ASN LYS SER SER ASP ASN VAL
SEQRES 20 A 2376 LYS LYS LYS ILE GLU ALA LEU LEU VAL GLU TYR LEU HIS
SEQRES 21 A 2376 PHE ASN ASN VAL ILE GLY GLN LEU LYS ASN CYS SER THR
SEQRES 22 A 2376 LYS GLU GLU ALA ARG LEU LEU TRP ALA LYS VAL GLN LYS
SEQRES 23 A 2376 PHE TYR GLN LYS ASN ASP THR LEU ASP ASP LEU ASN SER
SEQRES 24 A 2376 VAL PHE ILE SER GLN SER GLY TYR LEU LEU GLN TYR LYS
SEQRES 25 A 2376 PHE GLU TYR ILE GLY ILE PRO GLU ARG LEU ILE TYR THR
SEQRES 26 A 2376 PRO LEU LEU LEU VAL GLY PHE ALA THR LEU THR ASP SER
SEQRES 27 A 2376 LEU HIS GLN LYS TYR GLY GLY CYS PHE PHE GLY PRO ALA
SEQRES 28 A 2376 GLY THR GLY LYS THR GLU THR VAL LYS ALA PHE GLY GLN
SEQRES 29 A 2376 ASN LEU GLY ARG VAL VAL VAL VAL PHE ASN CYS ASP ASP
SEQRES 30 A 2376 SER PHE ASP TYR GLN VAL LEU SER ARG LEU LEU VAL GLY
SEQRES 31 A 2376 ILE THR GLN ILE GLY ALA TRP GLY CYS PHE ASP GLU PHE
SEQRES 32 A 2376 ASN ARG LEU ASP GLU LYS VAL LEU SER ALA VAL SER ALA
SEQRES 33 A 2376 ASN ILE GLN GLN ILE GLN ASN GLY LEU GLN VAL GLY LYS
SEQRES 34 A 2376 SER HIS ILE THR LEU LEU GLU GLU GLU THR PRO LEU SER
SEQRES 35 A 2376 PRO HIS THR ALA VAL PHE ILE THR LEU ASN PRO GLY TYR
SEQRES 36 A 2376 ASN GLY ARG SER GLU LEU PRO GLU ASN LEU LYS LYS SER
SEQRES 37 A 2376 PHE ARG GLU PHE SER MET LYS SER PRO GLN SER GLY THR
SEQRES 38 A 2376 ILE ALA GLU MET ILE LEU GLN ILE MET GLY PHE GLU ASP
SEQRES 39 A 2376 SER LYS SER LEU ALA SER LYS ILE VAL HIS PHE LEU GLU
SEQRES 40 A 2376 LEU LEU SER SER LYS CYS SER SER MET ASN HIS TYR HIS
SEQRES 41 A 2376 PHE GLY LEU ARG THR LEU LYS GLY VAL LEU ARG ASN CYS
SEQRES 42 A 2376 SER PRO LEU VAL SER GLU PHE GLY GLU GLY GLU LYS THR
SEQRES 43 A 2376 VAL VAL GLU SER LEU LYS ARG VAL ILE LEU PRO SER LEU
SEQRES 44 A 2376 GLY ASP THR ASP GLU LEU VAL PHE LYS ASP GLU LEU SER
SEQRES 45 A 2376 LYS ILE PHE ASP SER ALA GLY THR PRO LEU ASN SER LYS
SEQRES 46 A 2376 ALA ILE VAL GLN CYS LEU LYS ASP ALA GLY GLN ARG SER
SEQRES 47 A 2376 GLY PHE SER MET SER GLU GLU PHE LEU LYS LYS CYS MET
SEQRES 48 A 2376 GLN PHE TYR TYR MET GLN LYS THR GLN GLN ALA LEU ILE
SEQRES 49 A 2376 LEU VAL GLY LYS ALA GLY CYS GLY LYS THR ALA THR TRP
SEQRES 50 A 2376 LYS THR VAL ILE ASP ALA MET ALA ILE PHE ASP GLY HIS
SEQRES 51 A 2376 ALA ASN VAL VAL TYR VAL ILE ASP THR LYS VAL LEU THR
SEQRES 52 A 2376 LYS GLU SER LEU TYR GLY SER MET LEU LYS ALA THR LEU
SEQRES 53 A 2376 GLU TRP ARG ASP GLY LEU PHE THR SER ILE LEU ARG ARG
SEQRES 54 A 2376 VAL ASN ASP ASP ILE THR GLY THR PHE LYS ASN SER ARG
SEQRES 55 A 2376 ILE TRP VAL VAL PHE ASP SER ASP LEU ASP PRO GLU TYR
SEQRES 56 A 2376 VAL GLU ALA MET ASN SER VAL LEU ASP ASP ASN LYS ILE
SEQRES 57 A 2376 LEU THR LEU PRO ASN GLY GLU ARG LEU PRO ILE PRO PRO
SEQRES 58 A 2376 ASN PHE ARG ILE LEU PHE GLU THR ASP ASN LEU ASP HIS
SEQRES 59 A 2376 THR THR PRO ALA THR ILE THR ARG CYS GLY LEU LEU TRP
SEQRES 60 A 2376 PHE SER THR ASP VAL CYS SER ILE SER SER LYS ILE ASP
SEQRES 61 A 2376 HIS LEU LEU ASN LYS SER TYR GLU ALA LEU ASP ASN LYS
SEQRES 62 A 2376 LEU SER MET PHE GLU LEU ASP LYS LEU LYS ASP LEU ILE
SEQRES 63 A 2376 SER ASP SER PHE ASP MET ALA SER LEU THR ASN ILE PHE
SEQRES 64 A 2376 THR CYS SER ASN ASP LEU VAL HIS ILE LEU GLY VAL ARG
SEQRES 65 A 2376 THR PHE ASN LYS LEU GLU THR ALA VAL GLN LEU ALA VAL
SEQRES 66 A 2376 HIS LEU ILE SER SER TYR ARG GLN TRP PHE GLN ASN LEU
SEQRES 67 A 2376 ASP ASP LYS SER LEU LYS ASP VAL ILE THR LEU LEU ILE
SEQRES 68 A 2376 LYS ARG SER LEU LEU TYR ALA LEU ALA GLY ASP SER THR
SEQRES 69 A 2376 GLY GLU SER GLN ARG ALA PHE ILE GLN THR ILE ASN THR
SEQRES 70 A 2376 TYR PHE GLY HIS ASP SER GLN GLU LEU SER ASP TYR SER
SEQRES 71 A 2376 THR ILE VAL ILE ALA ASN ASP LYS LEU SER PHE SER SER
SEQRES 72 A 2376 PHE CYS SER GLU ILE PRO SER VAL SER LEU GLU ALA HIS
SEQRES 73 A 2376 GLU VAL MET ARG PRO ASP ILE VAL ILE PRO THR ILE ASP
SEQRES 74 A 2376 THR ILE LYS HIS GLU LYS ILE PHE TYR ASP LEU LEU ASN
SEQRES 75 A 2376 SER LYS ARG GLY ILE ILE LEU CYS GLY PRO PRO GLY SER
SEQRES 76 A 2376 GLY LYS THR MET ILE MET ASN ASN ALA LEU ARG ASN SER
SEQRES 77 A 2376 SER LEU TYR ASP VAL VAL GLY ILE ASN PHE SER LYS ASP
SEQRES 78 A 2376 THR THR THR GLU HIS ILE LEU SER ALA LEU HIS ARG HIS
SEQRES 79 A 2376 THR ASN TYR VAL THR THR SER LYS GLY LEU THR LEU LEU
SEQRES 80 A 2376 PRO LYS SER ASP ILE LYS ASN LEU VAL LEU PHE CYS ASP
SEQRES 81 A 2376 GLU ILE ASN LEU PRO LYS LEU ASP LYS TYR GLY SER GLN
SEQRES 82 A 2376 ASN VAL VAL LEU PHE LEU ARG GLN LEU MET GLU LYS GLN
SEQRES 83 A 2376 GLY PHE TRP LYS THR PRO GLU ASN LYS TRP VAL THR ILE
SEQRES 84 A 2376 GLU ARG ILE HIS ILE VAL GLY ALA CYS ASN PRO PRO THR
SEQRES 85 A 2376 ASP PRO GLY ARG ILE PRO MET SER GLU ARG PHE THR ARG
SEQRES 86 A 2376 HIS ALA ALA ILE LEU TYR LEU GLY TYR PRO SER GLY LYS
SEQRES 87 A 2376 SER LEU SER GLN ILE TYR GLU ILE TYR TYR LYS ALA ILE
SEQRES 88 A 2376 PHE LYS LEU VAL PRO GLU PHE ARG SER TYR THR GLU PRO
SEQRES 89 A 2376 PHE ALA ARG ALA SER VAL HIS LEU TYR ASN GLU CYS LYS
SEQRES 90 A 2376 ALA ARG TYR SER THR GLY LEU GLN SER HIS TYR LEU PHE
SEQRES 91 A 2376 SER PRO ARG GLU LEU THR ARG LEU VAL ARG GLY VAL TYR
SEQRES 92 A 2376 THR ALA ILE ASN THR GLY PRO ARG GLN THR LEU ARG SER
SEQRES 93 A 2376 LEU ILE ARG LEU TRP ALA TYR GLU ALA TRP ARG ILE PHE
SEQRES 94 A 2376 ALA ASP ARG LEU VAL GLY VAL LYS GLU LYS ASN SER PHE
SEQRES 95 A 2376 GLU GLN LEU LEU TYR GLU THR VAL ASP LYS TYR LEU PRO
SEQRES 96 A 2376 ASN GLN ASP LEU GLY ASN ILE SER SER THR SER LEU LEU
SEQRES 97 A 2376 PHE SER GLY LEU LEU SER LEU ASP PHE LYS GLU VAL ASN
SEQRES 98 A 2376 LYS THR ASP LEU VAL ASN PHE ILE GLU GLU ARG PHE LYS
SEQRES 99 A 2376 THR PHE CYS ASP GLU GLU LEU GLU VAL PRO MET VAL ILE
SEQRES 100 A 2376 HIS GLU SER MET VAL ASP HIS ILE LEU ARG ILE ASP ARG
SEQRES 101 A 2376 ALA LEU LYS GLN VAL GLN GLY HIS MET MET LEU ILE GLY
SEQRES 102 A 2376 ALA SER ARG THR GLY LYS THR ILE LEU THR ARG PHE VAL
SEQRES 103 A 2376 ALA TRP LEU ASN GLY LEU LYS ILE VAL GLN PRO LYS ILE
SEQRES 104 A 2376 HIS ARG HIS SER ASN LEU SER ASP PHE ASP MET ILE LEU
SEQRES 105 A 2376 LYS LYS ALA ILE SER ASP CYS SER LEU LYS GLU SER ARG
SEQRES 106 A 2376 THR CYS LEU ILE ILE ASP GLU SER ASN ILE LEU GLU THR
SEQRES 107 A 2376 ALA PHE LEU GLU ARG MET ASN THR LEU LEU ALA ASN ALA
SEQRES 108 A 2376 ASP ILE PRO ASP LEU PHE GLN GLY GLU GLU TYR ASP LYS
SEQRES 109 A 2376 LEU LEU ASN ASN LEU ARG ASN LYS THR ARG SER LEU GLY
SEQRES 110 A 2376 LEU LEU LEU ASP THR GLU GLN GLU LEU TYR ASP TRP PHE
SEQRES 111 A 2376 VAL GLY GLU ILE ALA LYS ASN LEU HIS VAL VAL PHE THR
SEQRES 112 A 2376 ILE CYS ASP PRO THR ASN ASN LYS SER SER ALA MET ILE
SEQRES 113 A 2376 SER SER PRO ALA LEU PHE ASN ARG CYS ILE ILE ASN TRP
SEQRES 114 A 2376 MET GLY ASP TRP ASP THR LYS THR MET SER GLN VAL ALA
SEQRES 115 A 2376 ASN ASN MET VAL ASP VAL VAL PRO MET GLU PHE THR ASP
SEQRES 116 A 2376 PHE ILE VAL PRO GLU VAL ASN LYS GLU LEU VAL PHE THR
SEQRES 117 A 2376 GLU PRO ILE GLN THR ILE ARG ASP ALA VAL VAL ASN ILE
SEQRES 118 A 2376 LEU ILE HIS PHE ASP ARG ASN PHE TYR GLN LYS MET LYS
SEQRES 119 A 2376 VAL GLY VAL ASN PRO ARG SER PRO GLY TYR PHE ILE ASP
SEQRES 120 A 2376 GLY LEU ARG ALA LEU VAL LYS LEU VAL THR ALA LYS TYR
SEQRES 121 A 2376 GLN ASP LEU GLN GLU ASN GLN ARG PHE VAL ASN VAL GLY
SEQRES 122 A 2376 LEU GLU LYS LEU ASN GLU SER VAL SER LEU THR PHE GLU
SEQRES 123 A 2376 LYS GLU ARG TRP LEU ASN THR THR LYS GLN PHE SER LYS
SEQRES 124 A 2376 THR SER GLN GLU LEU ILE GLY ASN CYS ILE ILE SER SER
SEQRES 125 A 2376 ILE TYR GLU THR TYR PHE GLY HIS LEU ASN GLU ARG GLU
SEQRES 126 A 2376 ARG GLY ASP MET LEU VAL ILE LEU LYS ARG LEU LEU GLY
SEQRES 127 A 2376 LYS PHE ALA VAL LYS TYR ASP VAL ASN TYR ARG PHE ILE
SEQRES 128 A 2376 ASP TYR LEU VAL THR LEU ASP GLU LYS MET LYS TRP LEU
SEQRES 129 A 2376 GLU CYS GLY LEU ASP LYS ASN ASP TYR PHE LEU GLU ASN
SEQRES 130 A 2376 MET SER ILE VAL MET ASN SER GLN ASP ALA VAL PRO PHE
SEQRES 131 A 2376 LEU LEU ASP PRO SER SER HIS MET ILE THR VAL ILE SER
SEQRES 132 A 2376 ASN TYR TYR GLY ASN LYS THR VAL LEU LEU SER PHE LEU
SEQRES 133 A 2376 GLU GLU GLY PHE VAL LYS ARG LEU GLU ASN ALA VAL ARG
SEQRES 134 A 2376 PHE GLY SER VAL VAL ILE ILE GLN ASP GLY GLU PHE PHE
SEQRES 135 A 2376 ASP PRO ILE ILE SER ARG LEU ILE SER ARG GLU PHE ASN
SEQRES 136 A 2376 HIS ALA GLY ASN ARG VAL THR VAL GLU ILE GLY ASP HIS
SEQRES 137 A 2376 GLU VAL ASP VAL SER GLY ASP PHE LYS LEU PHE ILE HIS
SEQRES 138 A 2376 SER CYS ASP PRO SER GLY ASP ILE PRO ILE PHE LEU ARG
SEQRES 139 A 2376 SER ARG VAL ARG LEU VAL HIS PHE VAL THR ASN LYS GLU
SEQRES 140 A 2376 SER ILE GLU THR ARG ILE PHE ASP ILE THR LEU THR GLU
SEQRES 141 A 2376 GLU ASN ALA GLU MET GLN ARG LYS ARG GLU ASP LEU ILE
SEQRES 142 A 2376 LYS LEU ASN THR GLU TYR ARG LEU LYS LEU LYS ASN LEU
SEQRES 143 A 2376 GLU LYS ARG LEU LEU GLU GLU LEU ASN ASN SER GLN GLY
SEQRES 144 A 2376 ASN MET LEU GLU ASN ASP GLU LEU MET VAL THR LEU ASN
SEQRES 145 A 2376 ASN LEU LYS LYS GLU ALA MET ASN ILE GLU LYS LYS LEU
SEQRES 146 A 2376 SER GLU SER GLU GLU PHE PHE PRO GLN PHE ASP ASN LEU
SEQRES 147 A 2376 VAL GLU GLU TYR SER ILE ILE GLY LYS HIS SER VAL LYS
SEQRES 148 A 2376 ILE PHE SER MET LEU GLU LYS PHE GLY GLN PHE HIS TRP
SEQRES 149 A 2376 PHE TYR GLY ILE SER ILE GLY GLN PHE LEU SER CYS PHE
SEQRES 150 A 2376 LYS ARG VAL PHE ILE LYS LYS SER ARG GLU THR ARG ALA
SEQRES 151 A 2376 ALA ARG THR ARG VAL ASP GLU ILE LEU TRP LEU LEU TYR
SEQRES 152 A 2376 GLN GLU VAL TYR CYS GLN PHE SER THR ALA LEU ASP LYS
SEQRES 153 A 2376 LYS PHE LYS MET ILE MET ALA MET THR MET PHE CYS LEU
SEQRES 154 A 2376 TYR LYS PHE ASP ILE GLU SER GLU GLN TYR LYS GLU ALA
SEQRES 155 A 2376 VAL LEU THR MET ILE GLY VAL LEU SER GLU SER SER ASP
SEQRES 156 A 2376 GLY VAL PRO LYS LEU THR VAL ASP THR ASN ASP ASP LEU
SEQRES 157 A 2376 ARG TYR LEU TRP ASP TYR VAL THR THR LYS SER TYR ILE
SEQRES 158 A 2376 SER ALA LEU ASN TRP PHE LYS ASN GLU PHE PHE VAL ASP
SEQRES 159 A 2376 GLU TRP ASN ILE ALA ASP VAL VAL ALA ASN SER GLU ASN
SEQRES 160 A 2376 ASN TYR PHE THR MET ALA SER GLU ARG ASP VAL ASP GLY
SEQRES 161 A 2376 THR PHE LYS LEU ILE GLU LEU ALA LYS ALA SER LYS GLU
SEQRES 162 A 2376 SER LEU LYS ILE ILE PRO LEU GLY SER ILE GLU ASN LEU
SEQRES 163 A 2376 ASN TYR ALA GLN GLU GLU ILE SER LYS SER LYS ILE GLU
SEQRES 164 A 2376 GLY GLY TRP ILE LEU LEU GLN ASN ILE GLN MET SER LEU
SEQRES 165 A 2376 SER TRP VAL LYS THR TYR LEU HIS LYS HIS VAL GLU GLU
SEQRES 166 A 2376 THR LYS ALA ALA GLU GLU HIS GLU LYS PHE LYS MET PHE
SEQRES 167 A 2376 MET THR CYS HIS LEU THR GLY ASP LYS LEU PRO ALA PRO
SEQRES 168 A 2376 LEU LEU GLN ARG THR ASP ARG VAL VAL TYR GLU ASP ILE
SEQRES 169 A 2376 PRO GLY ILE LEU ASP THR VAL LYS ASP LEU TRP GLY SER
SEQRES 170 A 2376 GLN PHE PHE THR GLY LYS ILE SER GLY VAL TRP SER VAL
SEQRES 171 A 2376 TYR CYS THR PHE LEU LEU SER TRP PHE HIS ALA LEU ILE
SEQRES 172 A 2376 THR ALA ARG THR ARG LEU VAL PRO HIS GLY PHE SER LYS
SEQRES 173 A 2376 LYS TYR TYR PHE ASN ASP CYS ASP PHE GLN PHE ALA SER
SEQRES 174 A 2376 VAL TYR LEU GLU ASN VAL LEU ALA THR ASN SER THR ASN
SEQRES 175 A 2376 ASN ILE PRO TRP ALA GLN VAL ARG ASP HIS ILE ALA THR
SEQRES 176 A 2376 ILE VAL TYR GLY GLY LYS ILE ASP GLU GLU LYS ASP LEU
SEQRES 177 A 2376 GLU VAL VAL ALA LYS LEU CYS ALA HIS VAL PHE CYS GLY
SEQRES 178 A 2376 SER ASP ASN LEU GLN ILE VAL PRO GLY VAL ARG ILE PRO
SEQRES 179 A 2376 GLN PRO LEU LEU GLN GLN SER GLU GLU GLU GLU ARG ALA
SEQRES 180 A 2376 ARG LEU THR ALA ILE LEU SER ASN THR ILE GLU PRO ALA
SEQRES 181 A 2376 ASP SER LEU SER SER TRP LEU GLN LEU PRO ARG GLU SER
SEQRES 182 A 2376 ILE LEU ASP TYR GLU ARG LEU GLN ALA LYS GLU VAL ALA
SEQRES 183 A 2376 SER SER THR GLU GLN LEU LEU GLN GLU MET
SEQRES 1 B 354 LEU LYS TRP ILE PRO ARG ASN LEU PRO SER CYS LEU ILE
SEQRES 2 B 354 ASN VAL GLU SER SER VAL THR SER VAL LYS LEU HIS PRO
SEQRES 3 B 354 ASN LEU PRO ILE VAL PHE VAL ALA THR ASP HIS GLY LYS
SEQRES 4 B 354 LEU TYR ALA PHE ASP LEU PHE ASN TYR THR ILE PRO LEU
SEQRES 5 B 354 ALA SER LEU GLN SER HIS THR LYS ALA ILE THR SER MET
SEQRES 6 B 354 ASP VAL LEU PHE THR ASN TYR THR ASN SER SER LYS LYS
SEQRES 7 B 354 ASN TYR LEU VAL ILE VAL THR ALA SER LYS ASP LEU GLN
SEQRES 8 B 354 ILE HIS VAL PHE LYS TRP VAL SER GLU GLU CYS LYS PHE
SEQRES 9 B 354 GLN GLN ILE ARG SER LEU LEU GLY HIS GLU HIS ILE VAL
SEQRES 10 B 354 SER ALA VAL LYS ILE TRP GLN LYS ASN ASN ASP VAL HIS
SEQRES 11 B 354 ILE ALA SER CYS SER ARG ASP GLN THR VAL LYS ILE TRP
SEQRES 12 B 354 ASP PHE HIS ASN GLY TRP SER LEU LYS THR PHE GLN PRO
SEQRES 13 B 354 HIS SER GLN TRP VAL ARG SER ILE ASP VAL LEU GLY ASP
SEQRES 14 B 354 TYR ILE ILE SER GLY SER HIS ASP THR THR LEU ARG LEU
SEQRES 15 B 354 THR HIS TRP PRO SER GLY ASN GLY LEU SER VAL GLY THR
SEQRES 16 B 354 GLY HIS GLU PHE PRO ILE GLU LYS VAL LYS PHE ILE HIS
SEQRES 17 B 354 PHE ILE GLU ASP SER PRO GLU ILE ARG PHE ARG THR PRO
SEQRES 18 B 354 SER THR ASP ARG TYR LYS ASN TRP GLY MET GLN TYR CYS
SEQRES 19 B 354 VAL SER ALA SER ARG ASP ARG THR ILE LYS ILE TRP GLU
SEQRES 20 B 354 ILE PRO LEU PRO THR LEU MET ALA HIS ARG ALA PRO ILE
SEQRES 21 B 354 PRO ASN PRO THR ASP SER ASN PHE ARG CYS VAL LEU THR
SEQRES 22 B 354 LEU LYS GLY HIS LEU SER TRP VAL ARG ASP ILE SER ILE
SEQRES 23 B 354 ARG GLY GLN TYR LEU PHE SER CYS ALA ASP ASP LYS SER
SEQRES 24 B 354 VAL ARG CYS TRP ASP LEU ASN THR GLY GLN CYS LEU HIS
SEQRES 25 B 354 VAL TRP GLU LYS LEU HIS THR GLY PHE VAL ASN CYS LEU
SEQRES 26 B 354 ASP LEU ASP VAL ASP PHE ASP SER ASN VAL THR PRO ARG
SEQRES 27 B 354 GLN MET MET VAL THR GLY GLY LEU ASP CYS LYS SER ASN
SEQRES 28 B 354 VAL PHE MET
SEQRES 1 C 354 LEU LYS TRP ILE PRO ARG ASN LEU PRO SER CYS LEU ILE
SEQRES 2 C 354 ASN VAL GLU SER SER VAL THR SER VAL LYS LEU HIS PRO
SEQRES 3 C 354 ASN LEU PRO ILE VAL PHE VAL ALA THR ASP HIS GLY LYS
SEQRES 4 C 354 LEU TYR ALA PHE ASP LEU PHE ASN TYR THR ILE PRO LEU
SEQRES 5 C 354 ALA SER LEU GLN SER HIS THR LYS ALA ILE THR SER MET
SEQRES 6 C 354 ASP VAL LEU PHE THR ASN TYR THR ASN SER SER LYS LYS
SEQRES 7 C 354 ASN TYR LEU VAL ILE VAL THR ALA SER LYS ASP LEU GLN
SEQRES 8 C 354 ILE HIS VAL PHE LYS TRP VAL SER GLU GLU CYS LYS PHE
SEQRES 9 C 354 GLN GLN ILE ARG SER LEU LEU GLY HIS GLU HIS ILE VAL
SEQRES 10 C 354 SER ALA VAL LYS ILE TRP GLN LYS ASN ASN ASP VAL HIS
SEQRES 11 C 354 ILE ALA SER CYS SER ARG ASP GLN THR VAL LYS ILE TRP
SEQRES 12 C 354 ASP PHE HIS ASN GLY TRP SER LEU LYS THR PHE GLN PRO
SEQRES 13 C 354 HIS SER GLN TRP VAL ARG SER ILE ASP VAL LEU GLY ASP
SEQRES 14 C 354 TYR ILE ILE SER GLY SER HIS ASP THR THR LEU ARG LEU
SEQRES 15 C 354 THR HIS TRP PRO SER GLY ASN GLY LEU SER VAL GLY THR
SEQRES 16 C 354 GLY HIS GLU PHE PRO ILE GLU LYS VAL LYS PHE ILE HIS
SEQRES 17 C 354 PHE ILE GLU ASP SER PRO GLU ILE ARG PHE ARG THR PRO
SEQRES 18 C 354 SER THR ASP ARG TYR LYS ASN TRP GLY MET GLN TYR CYS
SEQRES 19 C 354 VAL SER ALA SER ARG ASP ARG THR ILE LYS ILE TRP GLU
SEQRES 20 C 354 ILE PRO LEU PRO THR LEU MET ALA HIS ARG ALA PRO ILE
SEQRES 21 C 354 PRO ASN PRO THR ASP SER ASN PHE ARG CYS VAL LEU THR
SEQRES 22 C 354 LEU LYS GLY HIS LEU SER TRP VAL ARG ASP ILE SER ILE
SEQRES 23 C 354 ARG GLY GLN TYR LEU PHE SER CYS ALA ASP ASP LYS SER
SEQRES 24 C 354 VAL ARG CYS TRP ASP LEU ASN THR GLY GLN CYS LEU HIS
SEQRES 25 C 354 VAL TRP GLU LYS LEU HIS THR GLY PHE VAL ASN CYS LEU
SEQRES 26 C 354 ASP LEU ASP VAL ASP PHE ASP SER ASN VAL THR PRO ARG
SEQRES 27 C 354 GLN MET MET VAL THR GLY GLY LEU ASP CYS LYS SER ASN
SEQRES 28 C 354 VAL PHE MET
HELIX 1 AA1 VAL A 1448 LEU A 1455 1 8
HELIX 2 AA2 GLY A 1460 ILE A 1465 1 6
HELIX 3 AA3 LEU A 1469 THR A 1487 1 19
HELIX 4 AA4 THR A 1488 GLN A 1492 5 5
HELIX 5 AA5 THR A 1495 HIS A 1501 1 7
HELIX 6 AA6 ASN A 1504 LEU A 1509 1 6
HELIX 7 AA7 LEU A 1509 PHE A 1534 1 26
HELIX 8 AA8 PRO A 1535 LEU A 1540 5 6
HELIX 9 AA9 GLY A 1541 SER A 1551 1 11
HELIX 10 AB1 HIS A 1554 LYS A 1560 1 7
HELIX 11 AB2 PHE A 1561 PHE A 1566 1 6
HELIX 12 AB3 LYS A 1599 ILE A 1602 5 4
HELIX 13 AB4 GLN A 1603 GLY A 1633 1 31
HELIX 14 AB5 ASP A 1635 LYS A 1642 1 8
HELIX 15 AB6 ILE A 1644 GLN A 1665 1 22
HELIX 16 AB7 GLU A 1668 LEU A 1687 1 20
HELIX 17 AB8 SER A 1691 ASN A 1717 1 27
HELIX 18 AB9 LYS A 1721 ALA A 1724 5 4
HELIX 19 AC1 ARG A 1725 LYS A 1730 1 6
HELIX 20 AC2 THR A 1772 LYS A 1789 1 18
HELIX 21 AC3 THR A 1803 GLY A 1814 1 12
HELIX 22 AC4 ASP A 1827 GLY A 1842 1 16
HELIX 23 AC5 PHE A 1850 LEU A 1853 5 4
HELIX 24 AC6 ASP A 1854 GLY A 1875 1 22
HELIX 25 AC7 GLY A 1901 ARG A 1905 5 5
HELIX 26 AC8 PRO A 1909 LYS A 1914 1 6
HELIX 27 AC9 GLN A 1925 GLY A 1938 1 14
HELIX 28 AD1 LYS A 1943 SER A 1958 1 16
HELIX 29 AD2 GLY A 1969 GLU A 1986 1 18
HELIX 30 AD3 GLU A 1991 VAL A 2001 1 11
HELIX 31 AD4 ASP A 2010 LYS A 2020 1 11
HELIX 32 AD5 SER A 2031 SER A 2045 1 15
HELIX 33 AD6 SER A 2050 GLN A 2067 1 18
HELIX 34 AD7 THR A 2081 GLY A 2096 1 16
HELIX 35 AD8 ASP A 2105 LEU A 2109 5 5
HELIX 36 AD9 THR A 2110 GLY A 2116 1 7
HELIX 37 AE1 GLY A 2128 ASN A 2138 1 11
HELIX 38 AE2 ASP A 2159 ALA A 2165 5 7
HELIX 39 AE3 MET A 2166 ASP A 2172 1 7
HELIX 40 AE4 THR A 2203 THR A 2208 1 6
HELIX 41 AE5 SER A 2216 CYS A 2220 5 5
HELIX 42 AE6 SER A 2221 GLU A 2235 1 15
HELIX 43 AE7 MET A 2243 MET A 2259 1 17
HELIX 44 AE8 MET A 2259 ASP A 2271 1 13
HELIX 45 AE9 ARG A 2279 PHE A 2302 1 24
HELIX 46 AF1 ASP A 2306 LEU A 2326 1 21
HELIX 47 AF2 THR A 2331 GLN A 2340 1 10
HELIX 48 AF3 THR A 2341 TYR A 2345 5 5
HELIX 49 AF4 ARG A 2387 VAL A 2391 5 5
HELIX 50 AF5 THR A 2394 LYS A 2411 1 18
HELIX 51 AF6 GLY A 2423 LEU A 2432 1 10
HELIX 52 AF7 THR A 2450 HIS A 2459 1 10
HELIX 53 AF8 GLN A 2500 GLU A 2511 1 12
HELIX 54 AF9 SER A 2563 VAL A 2582 1 20
HELIX 55 AG1 PRO A 2583 SER A 2587 5 5
HELIX 56 AG2 TYR A 2588 TYR A 2607 1 20
HELIX 57 AG3 GLN A 2612 LEU A 2616 5 5
HELIX 58 AG4 PRO A 2619 ASN A 2634 1 16
HELIX 59 AG5 THR A 2640 PHE A 2656 1 17
HELIX 60 AG6 GLY A 2662 LEU A 2681 1 20
HELIX 61 AG7 ASP A 2685 ILE A 2689 5 5
HELIX 62 AG8 ASN A 2708 PHE A 2720 1 13
HELIX 63 AG9 LYS A 2721 CYS A 2724 5 4
HELIX 64 AH1 HIS A 2735 GLN A 2751 1 17
HELIX 65 AH2 LYS A 2766 GLY A 2778 1 13
HELIX 66 AH3 ASN A 2791 LEU A 2808 1 18
HELIX 67 AH4 SER A 2820 ILE A 2822 5 3
HELIX 68 AH5 GLU A 2824 ALA A 2838 1 15
HELIX 69 AH6 GLN A 2845 LEU A 2863 1 19
HELIX 70 AH7 LEU A 2865 ASP A 2868 5 4
HELIX 71 AH8 THR A 2869 ASN A 2884 1 16
HELIX 72 AH9 ASN A 2897 ALA A 2901 5 5
HELIX 73 AI1 SER A 2905 ASN A 2910 1 6
HELIX 74 AI2 ASP A 2921 VAL A 2935 1 15
HELIX 75 AI3 THR A 2960 ASN A 2975 1 16
HELIX 76 AI4 PRO A 2989 GLU A 3022 1 34
HELIX 77 AI5 LYS A 3023 VAL A 3028 5 6
HELIX 78 AI6 THR A 3300 THR A 3316 1 17
HELIX 79 AI7 GLN A 3318 TYR A 3333 1 16
HELIX 80 AI8 ASN A 3338 LEU A 3353 1 16
HELIX 81 AI9 ARG A 3365 LEU A 3370 1 6
HELIX 82 AJ1 THR A 3372 GLU A 3381 1 10
HELIX 83 AJ2 ASP A 3388 ASN A 3393 1 6
HELIX 84 AJ3 ASN A 3393 MET A 3398 1 6
HELIX 85 AJ4 SER A 3412 GLY A 3423 1 12
HELIX 86 AJ5 VAL A 3437 ARG A 3445 1 9
HELIX 87 AJ6 PHE A 3457 ILE A 3462 1 6
HELIX 88 AJ7 SER A 3463 PHE A 3470 1 8
HELIX 89 AJ8 PRO A 3506 ARG A 3512 1 7
HELIX 90 AJ9 ASN A 3521 LEU A 3534 1 14
HELIX 91 AK1 THR A 3535 ASN A 3538 5 4
HELIX 92 AK2 ALA A 3539 ASN A 3552 1 14
HELIX 93 AK3 THR A 3553 TYR A 3555 5 3
HELIX 94 AK4 ARG A 3556 ARG A 3565 1 10
HELIX 95 AK5 GLU A 3569 SER A 3573 5 5
HELIX 96 AK6 ASN A 3576 ASN A 3580 5 5
HELIX 97 AK7 LEU A 3583 ASN A 3613 1 31
HELIX 98 AK8 LEU A 3614 GLU A 3617 5 4
HELIX 99 AK9 TYR A 3618 GLY A 3636 1 19
HELIX 100 AL1 SER A 3645 ILE A 3658 1 14
HELIX 101 AL2 ARG A 3670 SER A 3687 1 18
HELIX 102 AL3 ASP A 3691 LYS A 3707 1 17
HELIX 103 AL4 LYS A 3716 ILE A 3723 1 8
HELIX 104 AL5 LEU A 3744 LYS A 3754 1 11
HELIX 105 AL6 SER A 3758 PHE A 3763 1 6
HELIX 106 AL7 ASN A 3773 ALA A 3779 1 7
HELIX 107 AL8 ASP A 3795 LYS A 3808 1 14
HELIX 108 AL9 SER A 3818 GLY A 3836 1 19
HELIX 109 AM1 SER A 3847 SER A 3849 5 3
HELIX 110 AM2 TRP A 3850 GLU A 3869 1 20
HELIX 111 AM3 PRO A 3885 GLN A 3890 1 6
HELIX 112 AM4 GLY A 3902 SER A 3913 1 12
HELIX 113 AM5 VAL A 3923 VAL A 3946 1 24
HELIX 114 AM6 ASN A 3957 VAL A 3971 1 15
HELIX 115 AM7 VAL A 3971 SER A 3976 1 6
HELIX 116 AM8 PRO A 3981 ILE A 3992 1 12
HELIX 117 AM9 GLU A 4000 PHE A 4015 1 16
HELIX 118 AN1 GLU A 4041 THR A 4046 1 6
HELIX 119 AN2 LEU A 4059 GLN A 4064 1 6
HELIX 120 AN3 ARG A 4067 GLN A 4090 1 24
HELIX 121 AN4 TYR B 211 TYR B 219 1 9
HELIX 122 AN5 GLN B 263 ASN B 266 5 4
HELIX 123 AN6 GLU B 350 ARG B 356 1 7
HELIX 124 AN7 THR B 362 LYS B 366 5 5
HELIX 125 AN8 ASN B 473 GLN B 478 1 6
HELIX 126 AN9 TYR C 211 TYR C 219 1 9
HELIX 127 AO1 GLN C 263 ASN C 266 5 4
HELIX 128 AO2 ASP C 351 ARG C 356 1 6
HELIX 129 AO3 VAL C 474 GLN C 478 5 5
SHEET 1 AA1 3 ILE A1569 PHE A1575 0
SHEET 2 AA1 3 SER A1578 SER A1584 -1 O SER A1578 N PHE A1575
SHEET 3 AA1 3 VAL A1589 GLU A1597 -1 O ILE A1596 N ILE A1579
SHEET 1 AA2 3 LYS A1733 GLN A1736 0
SHEET 2 AA2 3 VAL A1747 GLN A1751 -1 O SER A1750 N LYS A1733
SHEET 3 AA2 3 TYR A1754 GLN A1757 -1 O LEU A1756 N ILE A1749
SHEET 1 AA3 5 VAL A1818 ASN A1821 0
SHEET 2 AA3 5 TRP A1844 ASP A1848 1 O CYS A1846 N PHE A1820
SHEET 3 AA3 5 ALA A1893 LEU A1898 1 O THR A1897 N PHE A1847
SHEET 4 AA3 5 GLY A1791 PHE A1795 1 N GLY A1792 O ILE A1896
SHEET 5 AA3 5 PHE A1916 PHE A1919 1 O PHE A1919 N PHE A1795
SHEET 1 AA4 2 HIS A1878 LEU A1881 0
SHEET 2 AA4 2 GLU A1884 PRO A1887 -1 O THR A1886 N ILE A1879
SHEET 1 AA5 5 ASN A2099 VAL A2103 0
SHEET 2 AA5 5 ARG A2149 PHE A2154 1 O VAL A2153 N TYR A2102
SHEET 3 AA5 5 PHE A2190 THR A2196 1 O ARG A2191 N ILE A2150
SHEET 4 AA5 5 ALA A2069 VAL A2073 1 N LEU A2072 O PHE A2194
SHEET 5 AA5 5 GLY A2211 TRP A2214 1 O LEU A2213 N ILE A2071
SHEET 1 AA6 2 SER A2117 MET A2118 0
SHEET 2 AA6 2 TRP A2125 ARG A2126 -1 O ARG A2126 N SER A2117
SHEET 1 AA7 2 ILE A2175 THR A2177 0
SHEET 2 AA7 2 ARG A2183 PRO A2185 -1 O LEU A2184 N LEU A2176
SHEET 1 AA8 2 VAL A2360 ALA A2362 0
SHEET 2 AA8 2 PHE A2368 SER A2370 -1 O SER A2369 N ILE A2361
SHEET 1 AA9 5 ASP A2439 ILE A2443 0
SHEET 2 AA9 5 LEU A2482 CYS A2486 1 O PHE A2485 N VAL A2441
SHEET 3 AA9 5 ILE A2529 CYS A2535 1 O ALA A2534 N CYS A2486
SHEET 4 AA9 5 ILE A2414 CYS A2417 1 N LEU A2416 O CYS A2535
SHEET 5 AA9 5 ALA A2555 TYR A2558 1 O LEU A2557 N ILE A2415
SHEET 1 AB1 2 GLY A2514 TRP A2516 0
SHEET 2 AB1 2 TRP A2523 THR A2525 -1 O VAL A2524 N PHE A2515
SHEET 1 AB2 5 LYS A2780 VAL A2782 0
SHEET 2 AB2 5 THR A2813 ASP A2818 1 O CYS A2814 N LYS A2780
SHEET 3 AB2 5 VAL A2888 ILE A2891 1 O THR A2890 N ILE A2817
SHEET 4 AB2 5 MET A2756 GLY A2760 1 N LEU A2758 O ILE A2891
SHEET 5 AB2 5 ILE A2913 GLY A2918 1 O ASN A2915 N MET A2757
SHEET 1 AB3 2 PRO A3405 PHE A3406 0
SHEET 2 AB3 2 ARG A3514 LEU A3515 1 O ARG A3514 N PHE A3406
SHEET 1 AB4 5 LEU A3811 ILE A3813 0
SHEET 2 AB4 5 TRP A3838 LEU A3841 1 O TRP A3838 N LYS A3812
SHEET 3 AB4 5 LYS A3872 THR A3876 1 O PHE A3874 N LEU A3841
SHEET 4 AB4 5 PHE A3786 ALA A3789 1 N PHE A3786 O MET A3875
SHEET 5 AB4 5 ASP A3893 VAL A3896 1 O VAL A3895 N ALA A3789
SHEET 1 AB5 4 CYS B 150 ASN B 153 0
SHEET 2 AB5 4 LYS B 488 PHE B 492 -1 O SER B 489 N ILE B 152
SHEET 3 AB5 4 MET B 480 GLY B 484 -1 N MET B 480 O PHE B 492
SHEET 4 AB5 4 VAL B 461 LEU B 466 -1 N CYS B 463 O GLY B 483
SHEET 1 AB6 4 VAL B 158 LEU B 163 0
SHEET 2 AB6 4 ILE B 169 THR B 174 -1 O ALA B 173 N SER B 160
SHEET 3 AB6 4 LYS B 178 ASP B 183 -1 O PHE B 182 N VAL B 170
SHEET 4 AB6 4 ALA B 192 GLN B 195 -1 O LEU B 194 N LEU B 179
SHEET 1 AB7 4 ILE B 201 ASP B 205 0
SHEET 2 AB7 4 VAL B 221 SER B 226 -1 O ALA B 225 N THR B 202
SHEET 3 AB7 4 ILE B 231 VAL B 237 -1 O HIS B 232 N THR B 224
SHEET 4 AB7 4 CYS B 241 LEU B 249 -1 O GLN B 244 N LYS B 235
SHEET 1 AB8 4 VAL B 256 ILE B 261 0
SHEET 2 AB8 4 HIS B 269 SER B 274 -1 O ALA B 271 N LYS B 260
SHEET 3 AB8 4 VAL B 279 ASP B 283 -1 O LYS B 280 N SER B 272
SHEET 4 AB8 4 SER B 289 PHE B 293 -1 O PHE B 293 N VAL B 279
SHEET 1 AB9 4 VAL B 300 LEU B 306 0
SHEET 2 AB9 4 TYR B 309 SER B 314 -1 O ILE B 311 N ASP B 304
SHEET 3 AB9 4 LEU B 319 HIS B 323 -1 O THR B 322 N ILE B 310
SHEET 4 AB9 4 GLY B 329 GLY B 333 -1 O GLY B 333 N LEU B 319
SHEET 1 AC1 4 ILE B 340 VAL B 343 0
SHEET 2 AC1 4 TYR B 372 SER B 377 -1 O ALA B 376 N GLU B 341
SHEET 3 AC1 4 THR B 381 GLU B 386 -1 O LYS B 383 N SER B 375
SHEET 4 AC1 4 LEU B 411 LYS B 414 -1 O LEU B 411 N ILE B 384
SHEET 1 AC2 4 VAL B 420 ASP B 422 0
SHEET 2 AC2 4 TYR B 429 ALA B 434 -1 O CYS B 433 N ARG B 421
SHEET 3 AC2 4 VAL B 439 ASP B 443 -1 O ARG B 440 N SER B 432
SHEET 4 AC2 4 GLN B 448 VAL B 452 -1 O GLN B 448 N ASP B 443
SHEET 1 AC3 4 ARG C 145 ASN C 153 0
SHEET 2 AC3 4 LYS C 488 MET C 493 -1 O VAL C 491 N SER C 149
SHEET 3 AC3 4 MET C 480 GLY C 484 -1 N THR C 482 O ASN C 490
SHEET 4 AC3 4 VAL C 461 LEU C 466 -1 N ASP C 465 O VAL C 481
SHEET 1 AC4 4 VAL C 158 LEU C 163 0
SHEET 2 AC4 4 ILE C 169 THR C 174 -1 O ALA C 173 N SER C 160
SHEET 3 AC4 4 LYS C 178 ASP C 183 -1 O PHE C 182 N VAL C 170
SHEET 4 AC4 4 ALA C 192 GLN C 195 -1 O LEU C 194 N LEU C 179
SHEET 1 AC5 4 ILE C 201 ASP C 205 0
SHEET 2 AC5 4 VAL C 221 SER C 226 -1 O VAL C 223 N ASP C 205
SHEET 3 AC5 4 ILE C 231 VAL C 237 -1 O PHE C 234 N ILE C 222
SHEET 4 AC5 4 CYS C 241 LEU C 249 -1 O LEU C 249 N ILE C 231
SHEET 1 AC6 4 VAL C 256 TRP C 262 0
SHEET 2 AC6 4 HIS C 269 SER C 274 -1 O ALA C 271 N LYS C 260
SHEET 3 AC6 4 VAL C 279 ASP C 283 -1 O LYS C 280 N SER C 272
SHEET 4 AC6 4 LYS C 291 PHE C 293 -1 O PHE C 293 N VAL C 279
SHEET 1 AC7 4 VAL C 300 LEU C 306 0
SHEET 2 AC7 4 TYR C 309 SER C 314 -1 O TYR C 309 N LEU C 306
SHEET 3 AC7 4 LEU C 319 HIS C 323 -1 O ARG C 320 N SER C 312
SHEET 4 AC7 4 GLY C 329 GLY C 333 -1 O GLY C 333 N LEU C 319
SHEET 1 AC8 4 ILE C 340 PHE C 345 0
SHEET 2 AC8 4 TYR C 372 SER C 377 -1 O ALA C 376 N LYS C 342
SHEET 3 AC8 4 ILE C 382 GLU C 386 -1 O LYS C 383 N SER C 375
SHEET 4 AC8 4 CYS C 409 LEU C 413 -1 O LEU C 411 N ILE C 384
SHEET 1 AC9 4 VAL C 420 ASP C 422 0
SHEET 2 AC9 4 TYR C 429 ALA C 434 -1 O CYS C 433 N ASP C 422
SHEET 3 AC9 4 VAL C 439 ASP C 443 -1 O TRP C 442 N LEU C 430
SHEET 4 AC9 4 GLN C 448 TRP C 453 -1 O LEU C 450 N CYS C 441
SSBOND 1 CYS A 2078 CYS A 2220 1555 1555 2.02
CISPEP 1 VAL A 3946 PRO A 3947 0 3.60
CISPEP 2 HIS B 176 GLY B 177 0 -3.57
CISPEP 3 TYR B 187 THR B 188 0 -2.59
CISPEP 4 ARG B 358 THR B 359 0 7.71
CISPEP 5 HIS C 176 GLY C 177 0 -1.48
CISPEP 6 TYR C 187 THR C 188 0 -0.60
CISPEP 7 ARG C 358 THR C 359 0 -4.89
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
