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HEADER BIOSYNTHETIC PROTEIN 18-JAN-18 6FIK
TITLE ACP2 CROSSLINKED TO THE KS OF THE LOADING/CONDENSING REGION OF THE
TITLE 2 CTB1 PKS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: C553 IN CHAIN A IS CROSSLINKED TO S1816 IN CHAIN C;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: POLYKETIDE SYNTHASE;
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: S1816 IS CROSSLINKED TO C553 IN CHAIN A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CERCOSPORA NICOTIANAE;
SOURCE 3 ORGANISM_COMMON: BARN SPOT DISEASE FUNGUS;
SOURCE 4 ORGANISM_TAXID: 29003;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: CERCOSPORA NICOTIANAE;
SOURCE 9 ORGANISM_COMMON: BARN SPOT DISEASE FUNGUS;
SOURCE 10 ORGANISM_TAXID: 29003;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NR-PKS, PKS, IPKS, ITERATIVE PKS, NON-REDUCING, SAT, STARTER ACYL,
KEYWDS 2 CONDENSING, LOADING, POLYKETIDE, FUNGAL, CROSSLINK, ACP, ACYL
KEYWDS 3 CARRIER, TRANSFERASE, BIOSYNTHETIC PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR D.A.HERBST,C.R.HUITT-ROEHL,R.P.JAKOB,C.A.TOWNSEND,T.MAIER
REVDAT 1 21-MAR-18 6FIK 0
JRNL AUTH D.A.HERBST,C.R.HUITT-ROEHL,R.P.JAKOB,J.M.KRAVETZ,P.A.STORM,
JRNL AUTH 2 J.R.ALLEY,C.A.TOWNSEND,T.MAIER
JRNL TITL THE STRUCTURAL ORGANIZATION OF SUBSTRATE LOADING IN
JRNL TITL 2 ITERATIVE POLYKETIDE SYNTHASES
JRNL REF NAT.CHEM.BIOL.
JRNL REFN ESSN 1552-4469
JRNL DOI 10.1038/S41589-018-0026-3
REMARK 2
REMARK 2 RESOLUTION. 7.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : EMAN2, DIGITALMICROGRAPH, CTFFIND,
REMARK 3 GCTF, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
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) : 7.100
REMARK 3 NUMBER OF PARTICLES : 25107
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 6FIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200004641.
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 : CTB1-SAT0-KS-MAT0=ACP2
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.27
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
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) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : 800.00
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) : 41.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : 105000
REMARK 245 CALIBRATED MAGNIFICATION : 27707
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 91400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 GLY A 4
REMARK 465 ALA A 356
REMARK 465 LYS A 357
REMARK 465 ALA A 358
REMARK 465 PRO A 359
REMARK 465 THR A 360
REMARK 465 PRO A 361
REMARK 465 GLU A 362
REMARK 465 LEU A 363
REMARK 465 THR A 364
REMARK 465 VAL A 1289
REMARK 465 VAL A 1290
REMARK 465 ALA A 1291
REMARK 465 ALA A 1292
REMARK 465 SER A 1293
REMARK 465 ALA A 1294
REMARK 465 ALA A 1295
REMARK 465 ALA A 1296
REMARK 465 LEU A 1297
REMARK 465 GLU A 1298
REMARK 465 HIS A 1299
REMARK 465 HIS A 1300
REMARK 465 HIS A 1301
REMARK 465 HIS A 1302
REMARK 465 HIS A 1303
REMARK 465 HIS A 1304
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 3
REMARK 465 GLY B 4
REMARK 465 GLY B 355
REMARK 465 ALA B 356
REMARK 465 LYS B 357
REMARK 465 ALA B 358
REMARK 465 PRO B 359
REMARK 465 THR B 360
REMARK 465 PRO B 361
REMARK 465 GLU B 362
REMARK 465 LEU B 363
REMARK 465 VAL B 1289
REMARK 465 VAL B 1290
REMARK 465 ALA B 1291
REMARK 465 ALA B 1292
REMARK 465 SER B 1293
REMARK 465 ALA B 1294
REMARK 465 ALA B 1295
REMARK 465 ALA B 1296
REMARK 465 LEU B 1297
REMARK 465 GLU B 1298
REMARK 465 HIS B 1299
REMARK 465 HIS B 1300
REMARK 465 HIS B 1301
REMARK 465 HIS B 1302
REMARK 465 HIS B 1303
REMARK 465 HIS B 1304
REMARK 465 GLY C 1771
REMARK 465 SER C 1772
REMARK 465 HIS C 1773
REMARK 465 MET C 1774
REMARK 465 ASP C 1775
REMARK 465 PRO C 1776
REMARK 465 SER C 1777
REMARK 465 PRO C 1778
REMARK 465 ASN C 1779
REMARK 465 GLU C 1780
REMARK 465 ILE C 1781
REMARK 465 GLY C 1797
REMARK 465 LEU C 1798
REMARK 465 THR C 1799
REMARK 465 ASP C 1800
REMARK 465 GLU C 1801
REMARK 465 GLU C 1802
REMARK 465 LEU C 1803
REMARK 465 THR C 1804
REMARK 465 ASP C 1805
REMARK 465 ASP C 1806
REMARK 465 THR C 1807
REMARK 465 SER C 1808
REMARK 465 PHE C 1809
REMARK 465 ALA C 1810
REMARK 465 ASP C 1811
REMARK 465 VAL C 1812
REMARK 465 GLY C 1813
REMARK 465 VAL C 1814
REMARK 465 ASP C 1815
REMARK 465 GLU C 1829
REMARK 465 LEU C 1830
REMARK 465 ASP C 1831
REMARK 465 ILE C 1832
REMARK 465 ASP C 1833
REMARK 465 PHE C 1834
REMARK 465 PRO C 1835
REMARK 465 ASP C 1836
REMARK 465 ARG C 1837
REMARK 465 ALA C 1838
REMARK 465 CYS C 1843
REMARK 465 GLN C 1844
REMARK 465 THR C 1845
REMARK 465 GLY C 1855
REMARK 465 SER C 1856
REMARK 465 THR C 1857
REMARK 465 GLU C 1858
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 OE1 GLN B 85 OG1 THR B 120 2.03
REMARK 500 OD1 ASP B 952 OG SER B 962 2.07
REMARK 500 O LEU A 995 OG SER A 998 2.08
REMARK 500 OG1 THR B 924 OE2 GLU B 1194 2.08
REMARK 500 O GLN B 57 OG1 THR B 61 2.08
REMARK 500 OG1 THR A 924 OE2 GLU A 1194 2.09
REMARK 500 O ALA B 223 N LEU B 227 2.13
REMARK 500 OD1 ASP A 14 OG1 THR A 16 2.14
REMARK 500 O ALA A 223 N LEU A 227 2.14
REMARK 500 O GLY A 485 NH2 ARG A 490 2.15
REMARK 500 NH1 ARG B 30 O LEU B 643 2.15
REMARK 500 ND2 ASN A 497 OE1 GLU B 69 2.16
REMARK 500 OD1 ASN B 322 NH2 ARG B 325 2.18
REMARK 500 O TRP B 786 NH1 ARG B 794 2.18
REMARK 500 OG SER B 493 OD2 ASP B 634 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 243 C PRO A 244 N 0.150
REMARK 500 ARG A 420 CZ ARG A 420 NH2 0.101
REMARK 500 GLY A1198 C PRO A1199 N 0.174
REMARK 500 LEU B 243 C PRO B 244 N 0.167
REMARK 500 GLY B1198 C PRO B1199 N 0.184
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 ARG A 285 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LYS A 381 CB - CG - CD ANGL. DEV. = 16.7 DEGREES
REMARK 500 ARG A 471 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 529 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 529 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 903 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 903 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 285 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 471 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 471 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU B 557 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG B 950 NE - CZ - NH1 ANGL. DEV. = 3.8 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 ASP A 14 -165.59 -115.89
REMARK 500 ARG A 30 -47.45 -135.09
REMARK 500 ASP A 31 -38.94 -37.51
REMARK 500 GLN A 58 -53.77 -128.64
REMARK 500 SER A 101 -65.06 -123.13
REMARK 500 ALA A 119 -117.89 57.85
REMARK 500 VAL A 213 -61.70 -95.91
REMARK 500 ALA A 222 -177.26 168.66
REMARK 500 PRO A 244 57.45 -91.15
REMARK 500 ILE A 308 -65.82 -94.99
REMARK 500 PRO A 378 -172.97 -67.12
REMARK 500 ASN A 457 71.61 58.39
REMARK 500 ASN A 489 72.90 56.33
REMARK 500 ARG A 490 -73.20 -133.74
REMARK 500 GLN A 495 -176.79 -65.40
REMARK 500 LYS A 496 -70.20 -67.64
REMARK 500 THR A 513 -61.13 -123.07
REMARK 500 PHE A 523 -73.00 -55.93
REMARK 500 ALA A 552 -126.57 72.93
REMARK 500 ASP A 573 -57.19 -128.08
REMARK 500 ASN A 581 83.23 -154.92
REMARK 500 ALA A 708 57.81 -141.30
REMARK 500 ASN A 730 -69.38 -99.94
REMARK 500 GLU A 735 -110.51 59.38
REMARK 500 THR A 763 -71.24 -122.73
REMARK 500 ASP A 820 -70.04 -131.94
REMARK 500 ARG A 875 159.09 178.71
REMARK 500 ARG A 879 -71.64 -55.03
REMARK 500 PRO A 917 100.80 -59.92
REMARK 500 ALA A1010 -117.75 56.33
REMARK 500 VAL A1022 -71.97 -83.63
REMARK 500 ALA A1055 163.51 176.70
REMARK 500 TYR A1072 -175.45 -176.67
REMARK 500 SER A1218 -57.89 -129.82
REMARK 500 ASP A1222 -74.64 -76.22
REMARK 500 ALA A1234 -72.77 -49.16
REMARK 500 PHE A1252 76.67 50.94
REMARK 500 ASN A1277 -2.17 65.74
REMARK 500 ASP B 14 -165.60 -115.87
REMARK 500 THR B 66 -159.48 -143.19
REMARK 500 SER B 101 -65.07 -126.87
REMARK 500 ALA B 119 -111.89 57.87
REMARK 500 VAL B 213 -60.97 -95.93
REMARK 500 SER B 218 -177.24 -170.02
REMARK 500 ALA B 222 -168.62 -160.10
REMARK 500 ILE B 308 -68.30 -94.96
REMARK 500 GLN B 376 -166.65 -72.27
REMARK 500 SER B 382 143.14 -176.28
REMARK 500 PRO B 383 94.82 -64.71
REMARK 500 ARG B 420 -63.76 -94.10
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FIJ RELATED DB: PDB
REMARK 900 PENDING DEPOSITION OF AN XRD STRUCTURE OF PRINCIPALLY THE SAME
REMARK 900 MOLECULE WITHOUT THE PROTEIN IN CHAIN C.
REMARK 900 RELATED ID: EMD-4266 RELATED DB: EMDB
REMARK 900 ACP2 CROSSLINKED TO THE KS OF THE LOADING/CONDENSING REGION OF THE
REMARK 900 CTB1 PKS
DBREF 6FIK A 1 1293 UNP Q6DQW3 Q6DQW3_CERNC 1 1293
DBREF 6FIK B 1 1293 UNP Q6DQW3 Q6DQW3_CERNC 1 1293
DBREF 6FIK C 1775 1858 UNP Q6DQW3 Q6DQW3_CERNC 1775 1858
SEQADV 6FIK ALA A 119 UNP Q6DQW3 CYS 119 ENGINEERED MUTATION
SEQADV 6FIK ALA A 321 UNP Q6DQW3 THR 321 ENGINEERED MUTATION
SEQADV 6FIK ALA A 1010 UNP Q6DQW3 SER 1010 ENGINEERED MUTATION
SEQADV 6FIK ALA A 1294 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK ALA A 1295 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK ALA A 1296 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK LEU A 1297 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK GLU A 1298 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS A 1299 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS A 1300 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS A 1301 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS A 1302 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS A 1303 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS A 1304 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK ALA B 119 UNP Q6DQW3 CYS 119 ENGINEERED MUTATION
SEQADV 6FIK ALA B 321 UNP Q6DQW3 THR 321 ENGINEERED MUTATION
SEQADV 6FIK ALA B 1010 UNP Q6DQW3 SER 1010 ENGINEERED MUTATION
SEQADV 6FIK ALA B 1294 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK ALA B 1295 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK ALA B 1296 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK LEU B 1297 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK GLU B 1298 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS B 1299 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS B 1300 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS B 1301 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS B 1302 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS B 1303 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS B 1304 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK GLY C 1771 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK SER C 1772 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK HIS C 1773 UNP Q6DQW3 EXPRESSION TAG
SEQADV 6FIK MET C 1774 UNP Q6DQW3 EXPRESSION TAG
SEQRES 1 A 1304 MET GLU ASP GLY ALA GLN MET ARG VAL VAL ALA PHE GLY
SEQRES 2 A 1304 ASP GLN THR TYR ASP CYS SER GLU ALA VAL SER GLN LEU
SEQRES 3 A 1304 LEU ARG VAL ARG ASP ASP ALA ILE VAL VAL ASP PHE LEU
SEQRES 4 A 1304 GLU ARG ALA PRO ALA VAL LEU LYS ALA GLU LEU ALA ARG
SEQRES 5 A 1304 LEU SER SER GLU GLN GLN GLU GLU THR PRO ARG PHE ALA
SEQRES 6 A 1304 THR LEU ALA GLU LEU VAL PRO ARG TYR ARG ALA GLY THR
SEQRES 7 A 1304 LEU ASN PRO ALA VAL SER GLN ALA LEU THR CYS ILE ALA
SEQRES 8 A 1304 GLN LEU GLY LEU PHE ILE ARG GLN HIS SER SER GLY GLN
SEQRES 9 A 1304 GLU ALA TYR PRO THR ALA HIS ASP SER CYS ILE THR GLY
SEQRES 10 A 1304 VAL ALA THR GLY ALA LEU THR ALA VAL ALA VAL GLY SER
SEQRES 11 A 1304 ALA SER SER VAL THR ALA LEU VAL PRO LEU ALA LEU HIS
SEQRES 12 A 1304 THR VAL ALA VAL ALA VAL ARG LEU GLY ALA ARG ALA TRP
SEQRES 13 A 1304 GLU ILE GLY SER CYS LEU ALA ASP ALA ARG ARG GLY ALA
SEQRES 14 A 1304 ASN GLY ARG TYR ALA SER TRP THR SER ALA VAL GLY GLY
SEQRES 15 A 1304 ILE SER PRO GLN ASP LEU GLN ASP ARG ILE SER ALA TYR
SEQRES 16 A 1304 THR ALA GLU GLN ALA LEU ALA SER VAL SER VAL PRO TYR
SEQRES 17 A 1304 LEU SER ALA ALA VAL GLY PRO GLY GLN SER SER VAL SER
SEQRES 18 A 1304 ALA ALA PRO VAL ILE LEU ASP ALA PHE LEU SER THR LEU
SEQRES 19 A 1304 LEU ARG PRO LEU THR THR THR ARG LEU PRO ILE THR ALA
SEQRES 20 A 1304 PRO TYR HIS ALA PRO HIS LEU PHE THR ALA LYS ASP VAL
SEQRES 21 A 1304 GLN HIS VAL THR ASP CYS LEU PRO PRO SER GLU ALA TRP
SEQRES 22 A 1304 PRO THR VAL ARG ILE PRO ILE ILE SER PHE SER ARG ASP
SEQRES 23 A 1304 GLU ALA VAL SER ARG GLY ALA SER PHE PRO ALA ALA MET
SEQRES 24 A 1304 SER GLU ALA VAL ARG ASP CYS LEU ILE ARG PRO ILE ALA
SEQRES 25 A 1304 LEU ASP ARG MET ALA VAL SER ILE ALA ASN HIS ALA ARG
SEQRES 26 A 1304 ASP LEU GLY LYS ASP SER VAL LEU PRO SER PRO ILE ALA
SEQRES 27 A 1304 LEU SER PHE SER ASP LYS LEU GLY PRO GLN VAL ASN SER
SEQRES 28 A 1304 HIS LEU PRO GLY ALA LYS ALA PRO THR PRO GLU LEU THR
SEQRES 29 A 1304 SER LYS SER ILE PRO SER ALA ILE GLY ALA GLU GLN GLN
SEQRES 30 A 1304 PRO MET ALA LYS SER PRO ILE ALA ILE LEU ALA ALA SER
SEQRES 31 A 1304 GLY ARG PHE PRO GLN SER SER SER MET ASP GLN PHE TRP
SEQRES 32 A 1304 ASP VAL LEU ILE ASN GLY VAL ASP THR HIS GLU LEU VAL
SEQRES 33 A 1304 PRO PRO THR ARG TRP ASN ALA ALA THR HIS VAL SER GLU
SEQRES 34 A 1304 ASP PRO LYS ALA LYS ASN VAL SER GLY THR GLY PHE GLY
SEQRES 35 A 1304 CYS TRP LEU HIS GLU ALA GLY GLU PHE ASP ALA ALA TYR
SEQRES 36 A 1304 PHE ASN MET SER PRO ARG GLU ALA PRO GLN VAL ASP PRO
SEQRES 37 A 1304 ALA GLN ARG LEU ALA LEU LEU THR ALA THR GLU ALA LEU
SEQRES 38 A 1304 GLU GLN ALA GLY VAL VAL PRO ASN ARG THR SER SER THR
SEQRES 39 A 1304 GLN LYS ASN ARG VAL GLY VAL TRP TYR GLY ALA THR SER
SEQRES 40 A 1304 ASN ASP TRP MET GLU THR ASN SER ALA GLN ASN VAL ASP
SEQRES 41 A 1304 THR TYR PHE ILE PRO GLY GLY ASN ARG ALA PHE ILE PRO
SEQRES 42 A 1304 GLY ARG VAL ASN TYR PHE HIS LYS PHE SER GLY PRO SER
SEQRES 43 A 1304 TYR THR ILE ASP THR ALA CYS SER SER SER LEU ALA ALA
SEQRES 44 A 1304 LEU HIS MET ALA CYS ASN ALA LEU TRP ARG GLY GLU VAL
SEQRES 45 A 1304 ASP THR ALA ILE VAL GLY GLY THR ASN VAL LEU THR ASN
SEQRES 46 A 1304 PRO ASP MET THR ALA GLY LEU ASP ALA GLY HIS PHE LEU
SEQRES 47 A 1304 SER ARG SER GLY ASN CYS LYS THR PHE ASP ASP GLU ALA
SEQRES 48 A 1304 ASP GLY TYR CYS ARG GLY GLU ALA VAL VAL THR LEU ILE
SEQRES 49 A 1304 LEU LYS ARG LEU PRO ASP ALA GLN ALA ASP LYS ASP PRO
SEQRES 50 A 1304 ILE GLN ALA SER ILE LEU GLY ILE ALA THR ASN HIS SER
SEQRES 51 A 1304 ALA GLU ALA ALA SER ILE THR ARG PRO HIS ALA GLY ALA
SEQRES 52 A 1304 GLN GLN ASP LEU PHE GLN GLN VAL LEU THR GLU THR GLY
SEQRES 53 A 1304 LEU THR ALA ASN ASP ILE SER VAL CYS GLU MET HIS GLY
SEQRES 54 A 1304 THR GLY THR GLN ALA GLY ASP SER GLY GLU THR THR SER
SEQRES 55 A 1304 VAL VAL GLU THR LEU ALA PRO LEU ASN ARG SER GLY SER
SEQRES 56 A 1304 ALA VAL ARG THR THR PRO LEU TYR ILE GLY ALA VAL LYS
SEQRES 57 A 1304 SER ASN VAL GLY HIS ALA GLU SER ALA ALA GLY VAL SER
SEQRES 58 A 1304 SER LEU ALA LYS ILE LEU LEU MET LEU LYS HIS SER LYS
SEQRES 59 A 1304 ILE PRO PRO HIS VAL GLY ILE LYS THR LYS LEU ASN HIS
SEQRES 60 A 1304 ARG LEU PRO ASP LEU ALA ALA ARG ASN THR HIS ILE ALA
SEQRES 61 A 1304 ARG SER GLU VAL PRO TRP PRO ARG PRO LYS ASN GLY LYS
SEQRES 62 A 1304 ARG ARG VAL LEU LEU ASN ASN PHE SER ALA ALA GLY GLY
SEQRES 63 A 1304 ASN THR CYS LEU VAL LEU GLU ASP ALA PRO GLU PRO GLU
SEQRES 64 A 1304 ASP SER GLN GLU VAL ASP PRO ARG GLU HIS HIS ILE VAL
SEQRES 65 A 1304 ALA LEU SER ALA LYS THR PRO ASP SER MET VAL ASN ASN
SEQRES 66 A 1304 LEU THR ASN MET ILE THR TRP ILE ASP LYS HIS SER GLY
SEQRES 67 A 1304 ASP SER LEU ALA THR LEU PRO GLN LEU SER TYR THR THR
SEQRES 68 A 1304 THR ALA ARG ARG VAL HIS HIS ARG HIS ARG ALA VAL ALA
SEQRES 69 A 1304 THR GLY THR ASP LEU LEU GLN ILE ARG SER SER LEU GLN
SEQRES 70 A 1304 GLU GLN LEU ASP ARG ARG VAL SER GLY GLU ARG SER ILE
SEQRES 71 A 1304 PRO HIS PRO PRO ASN GLY PRO SER PHE VAL LEU ALA PHE
SEQRES 72 A 1304 THR GLY GLN GLY SER ALA PHE ALA GLY MET GLY VAL ASP
SEQRES 73 A 1304 LEU TYR LYS ARG PHE ALA SER PHE ARG SER ASP ILE ALA
SEQRES 74 A 1304 ARG TYR ASP GLN ILE CYS GLU GLY MET SER LEU PRO SER
SEQRES 75 A 1304 ILE LYS ALA MET PHE GLU ASP GLU LYS VAL PHE SER THR
SEQRES 76 A 1304 ALA SER PRO THR LEU GLN GLN LEU THR HIS VAL CYS PHE
SEQRES 77 A 1304 GLN MET ALA LEU TYR ARG LEU TRP LYS SER LEU GLY VAL
SEQRES 78 A 1304 GLN ALA LYS ALA VAL VAL GLY HIS ALA LEU GLY GLU TYR
SEQRES 79 A 1304 ALA ALA LEU TYR ALA ALA GLY VAL LEU SER GLN SER ASP
SEQRES 80 A 1304 THR LEU TYR LEU VAL GLY ARG ARG ALA GLN LEU MET GLU
SEQRES 81 A 1304 LYS HIS LEU SER GLN GLY THR HIS ALA MET LEU ALA VAL
SEQRES 82 A 1304 ARG ALA LYS GLU GLU ALA ILE VAL ALA ALA ILE ASP GLY
SEQRES 83 A 1304 PRO PRO GLY GLU ALA TYR GLU PHE SER CYS ARG ASN GLY
SEQRES 84 A 1304 GLU GLN ARG ASN VAL LEU GLY GLY THR VAL ALA GLN ILE
SEQRES 85 A 1304 GLN ALA ALA LYS ALA ALA LEU GLU ALA LYS LYS ILE ARG
SEQRES 86 A 1304 CYS GLN TYR LEU ASP THR PRO MET ALA PHE HIS THR GLY
SEQRES 87 A 1304 GLN VAL ASP PRO ILE LEU PRO GLU LEU LEU GLN VAL ALA
SEQRES 88 A 1304 ALA ALA CYS SER ILE GLN ASP PRO GLN ILE PRO VAL ILE
SEQRES 89 A 1304 SER PRO ALA TYR GLY LYS VAL ILE ARG SER ALA LYS ASP
SEQRES 90 A 1304 PHE GLN PRO GLU TYR PHE THR HIS HIS CYS ARG SER SER
SEQRES 91 A 1304 VAL ASN MET VAL ASP ALA LEU GLN SER ALA VAL GLU GLU
SEQRES 92 A 1304 GLY LEU LEU ASP LYS ASN VAL ILE GLY LEU GLU ILE GLY
SEQRES 93 A 1304 PRO GLY PRO VAL VAL THR GLN PHE VAL LYS GLU ALA VAL
SEQRES 94 A 1304 GLY THR THR MET GLN THR PHE ALA SER ILE ASN LYS ASP
SEQRES 95 A 1304 LYS ASP THR TRP GLN LEU MET THR GLN ALA LEU ALA LYS
SEQRES 96 A 1304 PHE TYR LEU ALA GLY ALA SER VAL GLU TRP SER ARG TYR
SEQRES 97 A 1304 HIS GLU ASP PHE PRO GLY ALA GLN LYS VAL LEU GLU LEU
SEQRES 98 A 1304 PRO ALA TYR GLY TRP ALA LEU LYS ASN TYR TRP LEU GLN
SEQRES 99 A 1304 TYR VAL ASN ASP TRP SER LEU ARG LYS GLY ASP PRO ALA
SEQRES 100 A 1304 VAL VAL VAL ALA ALA SER ALA ALA ALA LEU GLU HIS HIS
SEQRES 101 A 1304 HIS HIS HIS HIS
SEQRES 1 B 1304 MET GLU ASP GLY ALA GLN MET ARG VAL VAL ALA PHE GLY
SEQRES 2 B 1304 ASP GLN THR TYR ASP CYS SER GLU ALA VAL SER GLN LEU
SEQRES 3 B 1304 LEU ARG VAL ARG ASP ASP ALA ILE VAL VAL ASP PHE LEU
SEQRES 4 B 1304 GLU ARG ALA PRO ALA VAL LEU LYS ALA GLU LEU ALA ARG
SEQRES 5 B 1304 LEU SER SER GLU GLN GLN GLU GLU THR PRO ARG PHE ALA
SEQRES 6 B 1304 THR LEU ALA GLU LEU VAL PRO ARG TYR ARG ALA GLY THR
SEQRES 7 B 1304 LEU ASN PRO ALA VAL SER GLN ALA LEU THR CYS ILE ALA
SEQRES 8 B 1304 GLN LEU GLY LEU PHE ILE ARG GLN HIS SER SER GLY GLN
SEQRES 9 B 1304 GLU ALA TYR PRO THR ALA HIS ASP SER CYS ILE THR GLY
SEQRES 10 B 1304 VAL ALA THR GLY ALA LEU THR ALA VAL ALA VAL GLY SER
SEQRES 11 B 1304 ALA SER SER VAL THR ALA LEU VAL PRO LEU ALA LEU HIS
SEQRES 12 B 1304 THR VAL ALA VAL ALA VAL ARG LEU GLY ALA ARG ALA TRP
SEQRES 13 B 1304 GLU ILE GLY SER CYS LEU ALA ASP ALA ARG ARG GLY ALA
SEQRES 14 B 1304 ASN GLY ARG TYR ALA SER TRP THR SER ALA VAL GLY GLY
SEQRES 15 B 1304 ILE SER PRO GLN ASP LEU GLN ASP ARG ILE SER ALA TYR
SEQRES 16 B 1304 THR ALA GLU GLN ALA LEU ALA SER VAL SER VAL PRO TYR
SEQRES 17 B 1304 LEU SER ALA ALA VAL GLY PRO GLY GLN SER SER VAL SER
SEQRES 18 B 1304 ALA ALA PRO VAL ILE LEU ASP ALA PHE LEU SER THR LEU
SEQRES 19 B 1304 LEU ARG PRO LEU THR THR THR ARG LEU PRO ILE THR ALA
SEQRES 20 B 1304 PRO TYR HIS ALA PRO HIS LEU PHE THR ALA LYS ASP VAL
SEQRES 21 B 1304 GLN HIS VAL THR ASP CYS LEU PRO PRO SER GLU ALA TRP
SEQRES 22 B 1304 PRO THR VAL ARG ILE PRO ILE ILE SER PHE SER ARG ASP
SEQRES 23 B 1304 GLU ALA VAL SER ARG GLY ALA SER PHE PRO ALA ALA MET
SEQRES 24 B 1304 SER GLU ALA VAL ARG ASP CYS LEU ILE ARG PRO ILE ALA
SEQRES 25 B 1304 LEU ASP ARG MET ALA VAL SER ILE ALA ASN HIS ALA ARG
SEQRES 26 B 1304 ASP LEU GLY LYS ASP SER VAL LEU PRO SER PRO ILE ALA
SEQRES 27 B 1304 LEU SER PHE SER ASP LYS LEU GLY PRO GLN VAL ASN SER
SEQRES 28 B 1304 HIS LEU PRO GLY ALA LYS ALA PRO THR PRO GLU LEU THR
SEQRES 29 B 1304 SER LYS SER ILE PRO SER ALA ILE GLY ALA GLU GLN GLN
SEQRES 30 B 1304 PRO MET ALA LYS SER PRO ILE ALA ILE LEU ALA ALA SER
SEQRES 31 B 1304 GLY ARG PHE PRO GLN SER SER SER MET ASP GLN PHE TRP
SEQRES 32 B 1304 ASP VAL LEU ILE ASN GLY VAL ASP THR HIS GLU LEU VAL
SEQRES 33 B 1304 PRO PRO THR ARG TRP ASN ALA ALA THR HIS VAL SER GLU
SEQRES 34 B 1304 ASP PRO LYS ALA LYS ASN VAL SER GLY THR GLY PHE GLY
SEQRES 35 B 1304 CYS TRP LEU HIS GLU ALA GLY GLU PHE ASP ALA ALA TYR
SEQRES 36 B 1304 PHE ASN MET SER PRO ARG GLU ALA PRO GLN VAL ASP PRO
SEQRES 37 B 1304 ALA GLN ARG LEU ALA LEU LEU THR ALA THR GLU ALA LEU
SEQRES 38 B 1304 GLU GLN ALA GLY VAL VAL PRO ASN ARG THR SER SER THR
SEQRES 39 B 1304 GLN LYS ASN ARG VAL GLY VAL TRP TYR GLY ALA THR SER
SEQRES 40 B 1304 ASN ASP TRP MET GLU THR ASN SER ALA GLN ASN VAL ASP
SEQRES 41 B 1304 THR TYR PHE ILE PRO GLY GLY ASN ARG ALA PHE ILE PRO
SEQRES 42 B 1304 GLY ARG VAL ASN TYR PHE HIS LYS PHE SER GLY PRO SER
SEQRES 43 B 1304 TYR THR ILE ASP THR ALA CYS SER SER SER LEU ALA ALA
SEQRES 44 B 1304 LEU HIS MET ALA CYS ASN ALA LEU TRP ARG GLY GLU VAL
SEQRES 45 B 1304 ASP THR ALA ILE VAL GLY GLY THR ASN VAL LEU THR ASN
SEQRES 46 B 1304 PRO ASP MET THR ALA GLY LEU ASP ALA GLY HIS PHE LEU
SEQRES 47 B 1304 SER ARG SER GLY ASN CYS LYS THR PHE ASP ASP GLU ALA
SEQRES 48 B 1304 ASP GLY TYR CYS ARG GLY GLU ALA VAL VAL THR LEU ILE
SEQRES 49 B 1304 LEU LYS ARG LEU PRO ASP ALA GLN ALA ASP LYS ASP PRO
SEQRES 50 B 1304 ILE GLN ALA SER ILE LEU GLY ILE ALA THR ASN HIS SER
SEQRES 51 B 1304 ALA GLU ALA ALA SER ILE THR ARG PRO HIS ALA GLY ALA
SEQRES 52 B 1304 GLN GLN ASP LEU PHE GLN GLN VAL LEU THR GLU THR GLY
SEQRES 53 B 1304 LEU THR ALA ASN ASP ILE SER VAL CYS GLU MET HIS GLY
SEQRES 54 B 1304 THR GLY THR GLN ALA GLY ASP SER GLY GLU THR THR SER
SEQRES 55 B 1304 VAL VAL GLU THR LEU ALA PRO LEU ASN ARG SER GLY SER
SEQRES 56 B 1304 ALA VAL ARG THR THR PRO LEU TYR ILE GLY ALA VAL LYS
SEQRES 57 B 1304 SER ASN VAL GLY HIS ALA GLU SER ALA ALA GLY VAL SER
SEQRES 58 B 1304 SER LEU ALA LYS ILE LEU LEU MET LEU LYS HIS SER LYS
SEQRES 59 B 1304 ILE PRO PRO HIS VAL GLY ILE LYS THR LYS LEU ASN HIS
SEQRES 60 B 1304 ARG LEU PRO ASP LEU ALA ALA ARG ASN THR HIS ILE ALA
SEQRES 61 B 1304 ARG SER GLU VAL PRO TRP PRO ARG PRO LYS ASN GLY LYS
SEQRES 62 B 1304 ARG ARG VAL LEU LEU ASN ASN PHE SER ALA ALA GLY GLY
SEQRES 63 B 1304 ASN THR CYS LEU VAL LEU GLU ASP ALA PRO GLU PRO GLU
SEQRES 64 B 1304 ASP SER GLN GLU VAL ASP PRO ARG GLU HIS HIS ILE VAL
SEQRES 65 B 1304 ALA LEU SER ALA LYS THR PRO ASP SER MET VAL ASN ASN
SEQRES 66 B 1304 LEU THR ASN MET ILE THR TRP ILE ASP LYS HIS SER GLY
SEQRES 67 B 1304 ASP SER LEU ALA THR LEU PRO GLN LEU SER TYR THR THR
SEQRES 68 B 1304 THR ALA ARG ARG VAL HIS HIS ARG HIS ARG ALA VAL ALA
SEQRES 69 B 1304 THR GLY THR ASP LEU LEU GLN ILE ARG SER SER LEU GLN
SEQRES 70 B 1304 GLU GLN LEU ASP ARG ARG VAL SER GLY GLU ARG SER ILE
SEQRES 71 B 1304 PRO HIS PRO PRO ASN GLY PRO SER PHE VAL LEU ALA PHE
SEQRES 72 B 1304 THR GLY GLN GLY SER ALA PHE ALA GLY MET GLY VAL ASP
SEQRES 73 B 1304 LEU TYR LYS ARG PHE ALA SER PHE ARG SER ASP ILE ALA
SEQRES 74 B 1304 ARG TYR ASP GLN ILE CYS GLU GLY MET SER LEU PRO SER
SEQRES 75 B 1304 ILE LYS ALA MET PHE GLU ASP GLU LYS VAL PHE SER THR
SEQRES 76 B 1304 ALA SER PRO THR LEU GLN GLN LEU THR HIS VAL CYS PHE
SEQRES 77 B 1304 GLN MET ALA LEU TYR ARG LEU TRP LYS SER LEU GLY VAL
SEQRES 78 B 1304 GLN ALA LYS ALA VAL VAL GLY HIS ALA LEU GLY GLU TYR
SEQRES 79 B 1304 ALA ALA LEU TYR ALA ALA GLY VAL LEU SER GLN SER ASP
SEQRES 80 B 1304 THR LEU TYR LEU VAL GLY ARG ARG ALA GLN LEU MET GLU
SEQRES 81 B 1304 LYS HIS LEU SER GLN GLY THR HIS ALA MET LEU ALA VAL
SEQRES 82 B 1304 ARG ALA LYS GLU GLU ALA ILE VAL ALA ALA ILE ASP GLY
SEQRES 83 B 1304 PRO PRO GLY GLU ALA TYR GLU PHE SER CYS ARG ASN GLY
SEQRES 84 B 1304 GLU GLN ARG ASN VAL LEU GLY GLY THR VAL ALA GLN ILE
SEQRES 85 B 1304 GLN ALA ALA LYS ALA ALA LEU GLU ALA LYS LYS ILE ARG
SEQRES 86 B 1304 CYS GLN TYR LEU ASP THR PRO MET ALA PHE HIS THR GLY
SEQRES 87 B 1304 GLN VAL ASP PRO ILE LEU PRO GLU LEU LEU GLN VAL ALA
SEQRES 88 B 1304 ALA ALA CYS SER ILE GLN ASP PRO GLN ILE PRO VAL ILE
SEQRES 89 B 1304 SER PRO ALA TYR GLY LYS VAL ILE ARG SER ALA LYS ASP
SEQRES 90 B 1304 PHE GLN PRO GLU TYR PHE THR HIS HIS CYS ARG SER SER
SEQRES 91 B 1304 VAL ASN MET VAL ASP ALA LEU GLN SER ALA VAL GLU GLU
SEQRES 92 B 1304 GLY LEU LEU ASP LYS ASN VAL ILE GLY LEU GLU ILE GLY
SEQRES 93 B 1304 PRO GLY PRO VAL VAL THR GLN PHE VAL LYS GLU ALA VAL
SEQRES 94 B 1304 GLY THR THR MET GLN THR PHE ALA SER ILE ASN LYS ASP
SEQRES 95 B 1304 LYS ASP THR TRP GLN LEU MET THR GLN ALA LEU ALA LYS
SEQRES 96 B 1304 PHE TYR LEU ALA GLY ALA SER VAL GLU TRP SER ARG TYR
SEQRES 97 B 1304 HIS GLU ASP PHE PRO GLY ALA GLN LYS VAL LEU GLU LEU
SEQRES 98 B 1304 PRO ALA TYR GLY TRP ALA LEU LYS ASN TYR TRP LEU GLN
SEQRES 99 B 1304 TYR VAL ASN ASP TRP SER LEU ARG LYS GLY ASP PRO ALA
SEQRES 100 B 1304 VAL VAL VAL ALA ALA SER ALA ALA ALA LEU GLU HIS HIS
SEQRES 101 B 1304 HIS HIS HIS HIS
SEQRES 1 C 88 GLY SER HIS MET ASP PRO SER PRO ASN GLU ILE GLY THR
SEQRES 2 C 88 VAL TRP ARG ASP ALA LEU LYS ILE LEU SER GLU GLU SER
SEQRES 3 C 88 GLY LEU THR ASP GLU GLU LEU THR ASP ASP THR SER PHE
SEQRES 4 C 88 ALA ASP VAL GLY VAL ASP SER LEU MET SER LEU VAL ILE
SEQRES 5 C 88 THR SER ARG LEU ARG ASP GLU LEU ASP ILE ASP PHE PRO
SEQRES 6 C 88 ASP ARG ALA LEU PHE GLU GLU CYS GLN THR ILE PHE ASP
SEQRES 7 C 88 LEU ARG LYS ARG PHE SER GLY SER THR GLU
HELIX 1 AA1 CYS A 19 LEU A 27 1 9
HELIX 2 AA2 ASP A 32 ALA A 51 1 20
HELIX 3 AA3 ARG A 52 SER A 54 5 3
HELIX 4 AA4 SER A 55 GLU A 60 1 6
HELIX 5 AA5 GLU A 69 ALA A 76 1 8
HELIX 6 AA6 ASN A 80 SER A 101 1 22
HELIX 7 AA7 ALA A 119 SER A 130 1 12
HELIX 8 AA8 SER A 133 ALA A 163 1 31
HELIX 9 AA9 SER A 184 ALA A 200 1 17
HELIX 10 AB1 ALA A 223 LEU A 234 1 12
HELIX 11 AB2 THR A 256 THR A 264 1 9
HELIX 12 AB3 ASP A 265 LEU A 267 5 3
HELIX 13 AB4 SER A 294 ILE A 308 1 15
HELIX 14 AB5 ALA A 312 ASP A 314 5 3
HELIX 15 AB6 ARG A 315 LEU A 327 1 13
HELIX 16 AB7 LYS A 344 HIS A 352 1 9
HELIX 17 AB8 SER A 398 ASN A 408 1 11
HELIX 18 AB9 ASN A 422 VAL A 427 1 6
HELIX 19 AC1 ARG A 461 VAL A 466 1 6
HELIX 20 AC2 ASP A 467 ALA A 484 1 18
HELIX 21 AC3 THR A 491 GLN A 495 5 5
HELIX 22 AC4 ASN A 514 ASN A 518 5 5
HELIX 23 AC5 TYR A 522 ASN A 528 1 7
HELIX 24 AC6 ALA A 530 LYS A 541 1 12
HELIX 25 AC7 THR A 551 CYS A 553 5 3
HELIX 26 AC8 SER A 554 TRP A 568 1 15
HELIX 27 AC9 ASN A 585 GLY A 595 1 11
HELIX 28 AD1 LEU A 628 LYS A 635 1 8
HELIX 29 AD2 HIS A 660 GLY A 676 1 17
HELIX 30 AD3 THR A 678 ASN A 680 5 3
HELIX 31 AD4 THR A 692 ALA A 708 1 17
HELIX 32 AD5 VAL A 727 GLY A 732 1 6
HELIX 33 AD6 ALA A 734 SER A 736 5 3
HELIX 34 AD7 ALA A 737 SER A 753 1 17
HELIX 35 AD8 THR A 838 SER A 857 1 20
HELIX 36 AD9 ALA A 862 ARG A 874 1 13
HELIX 37 AE1 ASP A 888 SER A 905 1 18
HELIX 38 AE2 GLY A 925 ALA A 929 5 5
HELIX 39 AE3 GLY A 934 PHE A 941 1 8
HELIX 40 AE4 PHE A 941 MET A 958 1 18
HELIX 41 AE5 ILE A 963 ASP A 969 1 7
HELIX 42 AE6 GLU A 970 SER A 974 5 5
HELIX 43 AE7 SER A 977 LEU A 999 1 23
HELIX 44 AE8 LEU A 1011 GLY A 1021 1 11
HELIX 45 AE9 SER A 1024 LEU A 1043 1 20
HELIX 46 AF1 LYS A 1056 ILE A 1064 1 9
HELIX 47 AF2 VAL A 1089 LYS A 1102 1 14
HELIX 48 AF3 THR A 1117 ASP A 1121 5 5
HELIX 49 AF4 ILE A 1123 ALA A 1133 1 11
HELIX 50 AF5 SER A 1154 GLN A 1159 5 6
HELIX 51 AF6 PRO A 1160 SER A 1169 1 10
HELIX 52 AF7 MET A 1173 GLU A 1183 1 11
HELIX 53 AF8 VAL A 1200 GLY A 1210 1 11
HELIX 54 AF9 ASP A 1224 ALA A 1239 1 16
HELIX 55 AG1 GLU A 1244 GLU A 1250 1 7
HELIX 56 AG2 ASP A 1278 LYS A 1283 5 6
HELIX 57 AG3 CYS B 19 ARG B 28 1 10
HELIX 58 AG4 ASP B 32 ALA B 51 1 20
HELIX 59 AG5 SER B 54 THR B 61 1 8
HELIX 60 AG6 GLU B 69 ALA B 76 1 8
HELIX 61 AG7 ASN B 80 HIS B 100 1 21
HELIX 62 AG8 ALA B 119 ALA B 131 1 13
HELIX 63 AG9 SER B 133 ALA B 163 1 31
HELIX 64 AH1 SER B 184 GLN B 199 1 16
HELIX 65 AH2 ALA B 223 LEU B 234 1 12
HELIX 66 AH3 THR B 256 THR B 264 1 9
HELIX 67 AH4 ASP B 265 LEU B 267 5 3
HELIX 68 AH5 SER B 294 ILE B 308 1 15
HELIX 69 AH6 ARG B 315 LEU B 327 1 13
HELIX 70 AH7 LYS B 344 HIS B 352 1 9
HELIX 71 AH8 SER B 398 ASN B 408 1 11
HELIX 72 AH9 ASN B 422 VAL B 427 1 6
HELIX 73 AI1 ASP B 467 ALA B 484 1 18
HELIX 74 AI2 GLN B 495 ASN B 497 5 3
HELIX 75 AI3 ASN B 514 ASN B 518 5 5
HELIX 76 AI4 TYR B 522 ASN B 528 1 7
HELIX 77 AI5 ALA B 530 LYS B 541 1 12
HELIX 78 AI6 THR B 551 CYS B 553 5 3
HELIX 79 AI7 SER B 554 ARG B 569 1 16
HELIX 80 AI8 ASN B 585 GLY B 595 1 11
HELIX 81 AI9 ARG B 627 ASP B 634 1 8
HELIX 82 AJ1 HIS B 660 GLY B 676 1 17
HELIX 83 AJ2 THR B 678 ASN B 680 5 3
HELIX 84 AJ3 THR B 692 ALA B 708 1 17
HELIX 85 AJ4 VAL B 727 GLY B 732 1 6
HELIX 86 AJ5 ALA B 734 SER B 736 5 3
HELIX 87 AJ6 ALA B 737 SER B 753 1 17
HELIX 88 AJ7 ASP B 771 ASN B 776 1 6
HELIX 89 AJ8 THR B 838 SER B 857 1 20
HELIX 90 AJ9 ALA B 862 ARG B 874 1 13
HELIX 91 AK1 ASP B 888 SER B 905 1 18
HELIX 92 AK2 GLY B 925 ALA B 929 5 5
HELIX 93 AK3 GLY B 934 PHE B 941 1 8
HELIX 94 AK4 ALA B 942 MET B 958 1 17
HELIX 95 AK5 ILE B 963 ASP B 969 1 7
HELIX 96 AK6 GLU B 970 SER B 974 5 5
HELIX 97 AK7 SER B 977 LEU B 999 1 23
HELIX 98 AK8 LEU B 1011 ALA B 1020 1 10
HELIX 99 AK9 SER B 1024 LEU B 1043 1 20
HELIX 100 AL1 LYS B 1056 ILE B 1064 1 9
HELIX 101 AL2 VAL B 1089 LYS B 1102 1 14
HELIX 102 AL3 THR B 1117 ASP B 1121 5 5
HELIX 103 AL4 ILE B 1123 ALA B 1133 1 11
HELIX 104 AL5 SER B 1154 GLN B 1159 5 6
HELIX 105 AL6 PRO B 1160 SER B 1169 1 10
HELIX 106 AL7 MET B 1173 GLU B 1183 1 11
HELIX 107 AL8 VAL B 1200 GLY B 1210 1 11
HELIX 108 AL9 ASP B 1224 GLY B 1240 1 17
HELIX 109 AM1 PHE B 1252 GLN B 1256 5 5
HELIX 110 AM2 ASP B 1278 LYS B 1283 5 6
HELIX 111 AM3 THR C 1783 SER C 1796 1 14
HELIX 112 AM4 LEU C 1817 ASP C 1828 1 12
HELIX 113 AM5 PHE C 1847 SER C 1854 1 8
SHEET 1 AA1 5 VAL A 289 SER A 290 0
SHEET 2 AA1 5 ILE A 280 ILE A 281 -1 N ILE A 280 O SER A 290
SHEET 3 AA1 5 SER A 113 GLY A 117 1 N ILE A 115 O ILE A 281
SHEET 4 AA1 5 GLN A 6 PHE A 12 1 N VAL A 10 O THR A 116
SHEET 5 AA1 5 SER A 331 ILE A 337 1 O ILE A 337 N ALA A 11
SHEET 1 AA2 4 TYR A 208 ALA A 212 0
SHEET 2 AA2 4 GLN A 217 SER A 221 -1 O SER A 221 N TYR A 208
SHEET 3 AA2 4 THR A 177 GLY A 181 -1 N VAL A 180 O SER A 218
SHEET 4 AA2 4 THR A 239 ARG A 242 -1 O THR A 241 N ALA A 179
SHEET 1 AA311 SER A 546 ILE A 549 0
SHEET 2 AA311 VAL A 499 ALA A 505 1 N ALA A 505 O ILE A 549
SHEET 3 AA311 THR A 574 THR A 580 1 O ILE A 576 N TRP A 502
SHEET 4 AA311 VAL A 620 ARG A 627 -1 O LEU A 623 N VAL A 577
SHEET 5 AA311 ILE A 384 ARG A 392 -1 N ALA A 385 O LYS A 626
SHEET 6 AA311 ALA A 640 HIS A 649 -1 O ALA A 640 N ILE A 386
SHEET 7 AA311 GLY A 806 ASP A 814 -1 O GLU A 813 N SER A 641
SHEET 8 AA311 ARG A 795 PHE A 801 -1 N VAL A 796 O LEU A 812
SHEET 9 AA311 ILE A 682 GLU A 686 1 N GLU A 686 O LEU A 797
SHEET 10 AA311 LEU A 722 GLY A 725 1 O TYR A 723 N CYS A 685
SHEET 11 AA311 THR A 777 HIS A 778 1 O HIS A 778 N ILE A 724
SHEET 1 AA4 3 GLU A 414 LEU A 415 0
SHEET 2 AA4 3 PHE A 441 CYS A 443 -1 O GLY A 442 N GLU A 414
SHEET 3 AA4 3 ARG A 616 GLY A 617 1 O ARG A 616 N PHE A 441
SHEET 1 AA5 2 GLU A 450 PHE A 451 0
SHEET 2 AA5 2 LYS A1269 ASN A1270 -1 O LYS A1269 N PHE A 451
SHEET 1 AA6 2 LYS A 754 ILE A 755 0
SHEET 2 AA6 2 VAL A 784 PRO A 785 -1 O VAL A 784 N ILE A 755
SHEET 1 AA7 2 HIS A 830 ALA A 836 0
SHEET 2 AA7 2 HIS A 880 GLY A 886 -1 O ALA A 882 N LEU A 834
SHEET 1 AA8 6 LYS A1150 ILE A1152 0
SHEET 2 AA8 6 VAL A1143 SER A1145 -1 N VAL A1143 O ILE A1152
SHEET 3 AA8 6 ALA A1003 GLY A1008 1 N VAL A1006 O ILE A1144
SHEET 4 AA8 6 PHE A 919 PHE A 923 1 N PHE A 919 O LYS A1004
SHEET 5 AA8 6 ILE A1191 ILE A1195 1 O LEU A1193 N ALA A 922
SHEET 6 AA8 6 THR A1215 PHE A1216 1 O PHE A1216 N GLU A1194
SHEET 1 AA9 5 CYS A1106 TYR A1108 0
SHEET 2 AA9 5 HIS A1048 ARG A1054 -1 N ALA A1052 O GLN A1107
SHEET 3 AA9 5 ARG A1082 THR A1088 -1 O LEU A1085 N LEU A1051
SHEET 4 AA9 5 GLU A1073 ARG A1077 -1 N CYS A1076 O VAL A1084
SHEET 5 AA9 5 VAL A1171 ASN A1172 1 O VAL A1171 N ARG A1077
SHEET 1 AB1 5 VAL B 289 SER B 290 0
SHEET 2 AB1 5 ILE B 280 ILE B 281 -1 N ILE B 280 O SER B 290
SHEET 3 AB1 5 SER B 113 GLY B 117 1 N ILE B 115 O ILE B 281
SHEET 4 AB1 5 GLN B 6 PHE B 12 1 N VAL B 10 O THR B 116
SHEET 5 AB1 5 SER B 331 ILE B 337 1 O ILE B 337 N ALA B 11
SHEET 1 AB2 5 THR B 239 ARG B 242 0
SHEET 2 AB2 5 THR B 177 GLY B 181 -1 N ALA B 179 O THR B 241
SHEET 3 AB2 5 GLN B 217 SER B 221 -1 O VAL B 220 N SER B 178
SHEET 4 AB2 5 TYR B 208 ALA B 212 -1 N ALA B 211 O SER B 219
SHEET 5 AB2 5 ILE B 311 ALA B 312 1 O ILE B 311 N ALA B 212
SHEET 1 AB311 SER B 546 ILE B 549 0
SHEET 2 AB311 VAL B 499 ALA B 505 1 N ALA B 505 O ILE B 549
SHEET 3 AB311 THR B 574 ASN B 581 1 O ILE B 576 N TRP B 502
SHEET 4 AB311 ALA B 619 LYS B 626 -1 O LEU B 623 N VAL B 577
SHEET 5 AB311 ALA B 385 ARG B 392 -1 N LEU B 387 O ILE B 624
SHEET 6 AB311 ALA B 640 HIS B 649 -1 O ALA B 640 N ILE B 386
SHEET 7 AB311 GLY B 806 ASP B 814 -1 O GLU B 813 N SER B 641
SHEET 8 AB311 ARG B 795 PHE B 801 -1 N LEU B 798 O LEU B 810
SHEET 9 AB311 ILE B 682 GLU B 686 1 N GLU B 686 O LEU B 797
SHEET 10 AB311 LEU B 722 GLY B 725 1 O TYR B 723 N CYS B 685
SHEET 11 AB311 THR B 777 HIS B 778 1 O HIS B 778 N ILE B 724
SHEET 1 AB4 2 GLU B 414 LEU B 415 0
SHEET 2 AB4 2 PHE B 441 GLY B 442 -1 O GLY B 442 N GLU B 414
SHEET 1 AB5 2 GLU B 450 PHE B 451 0
SHEET 2 AB5 2 LYS B1269 ASN B1270 -1 O LYS B1269 N PHE B 451
SHEET 1 AB6 2 LYS B 754 ILE B 755 0
SHEET 2 AB6 2 VAL B 784 PRO B 785 -1 O VAL B 784 N ILE B 755
SHEET 1 AB7 2 HIS B 830 ALA B 836 0
SHEET 2 AB7 2 HIS B 880 GLY B 886 -1 O ALA B 882 N LEU B 834
SHEET 1 AB8 6 LYS B1150 ILE B1152 0
SHEET 2 AB8 6 VAL B1143 SER B1145 -1 N VAL B1143 O ILE B1152
SHEET 3 AB8 6 ALA B1005 GLY B1008 1 N VAL B1006 O ILE B1144
SHEET 4 AB8 6 PHE B 919 PHE B 923 1 N PHE B 923 O VAL B1007
SHEET 5 AB8 6 ILE B1191 ILE B1195 1 O LEU B1193 N ALA B 922
SHEET 6 AB8 6 GLN B1214 ALA B1217 1 O PHE B1216 N GLU B1194
SHEET 1 AB9 5 CYS B1106 TYR B1108 0
SHEET 2 AB9 5 HIS B1048 ARG B1054 -1 N ALA B1052 O GLN B1107
SHEET 3 AB9 5 ARG B1082 THR B1088 -1 O LEU B1085 N LEU B1051
SHEET 4 AB9 5 GLU B1073 ARG B1077 -1 N GLU B1073 O GLY B1086
SHEET 5 AB9 5 VAL B1171 ASN B1172 1 O VAL B1171 N ARG B1077
CISPEP 1 ARG A 236 PRO A 237 0 2.96
CISPEP 2 ARG B 236 PRO B 237 0 12.42
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 0.003591 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003591 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003591 0.00000
TER 19179 VAL A1288
TER 38366 VAL B1288
TER 39061 SER C1854
MASTER 365 0 0 113 80 0 0 619628 3 0 209
END |