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HEADER PLANT PROTEIN/HYDROLASE 10-MAR-24 8YN0
TITLE CRYSTAL STRUCTURE OF NRG1C IN COMPLEX WITH EDS1-SAG101-(ADPR-ATP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN EDS1;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SENESCENCE-ASSOCIATED CARBOXYLESTERASE 101;
COMPND 8 CHAIN: E, C;
COMPND 9 EC: 3.1.1.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PROBABLE DISEASE RESISTANCE PROTEIN AT5G66890;
COMPND 13 CHAIN: H, D;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: EDS1, EDS1-90, EDS1A, AT3G48090, T17F15.40;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 10 ORGANISM_COMMON: THALE CRESS;
SOURCE 11 ORGANISM_TAXID: 3702;
SOURCE 12 GENE: SAG101, AT5G14930, F2G14.50;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 17 ORGANISM_COMMON: THALE CRESS;
SOURCE 18 ORGANISM_TAXID: 3702;
SOURCE 19 GENE: AT5G66890, MUD21.15;
SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS EDS1, SAG101, ATP-ADPR, NRG1C, PLANT PROTEIN, PLANT PROTEIN-HYDROLASE
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HUANG,Y.XIAO,J.CHAI
REVDAT 1 11-DEC-24 8YN0 0
JRNL AUTH S.HUANG,Y.XIAO,J.CHAI
JRNL TITL CRYSTAL STRUCTURE OF NRG1C IN COMPLEX WITH
JRNL TITL 2 EDS1-SAG101-(ADPR-ATP)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 158980
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1990
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7700 - 5.9900 0.90 10787 137 0.1723 0.2097
REMARK 3 2 5.9900 - 4.7600 0.95 11257 145 0.1779 0.1996
REMARK 3 3 4.7600 - 4.1600 0.96 11264 146 0.1607 0.1822
REMARK 3 4 4.1600 - 3.7800 0.97 11396 138 0.1774 0.2497
REMARK 3 5 3.7800 - 3.5100 0.97 11364 141 0.1918 0.2414
REMARK 3 6 3.5100 - 3.3000 0.97 11412 140 0.2078 0.2383
REMARK 3 7 3.3000 - 3.1400 0.97 11351 151 0.2243 0.2513
REMARK 3 8 3.1400 - 3.0000 0.97 11359 146 0.2253 0.2744
REMARK 3 9 3.0000 - 2.8800 0.97 11356 145 0.2301 0.2563
REMARK 3 10 2.8800 - 2.7900 0.96 11255 139 0.2462 0.3212
REMARK 3 11 2.7900 - 2.7000 0.96 11268 140 0.2425 0.2693
REMARK 3 12 2.7000 - 2.6200 0.96 11200 148 0.2533 0.3005
REMARK 3 13 2.6200 - 2.5500 0.96 11267 143 0.2638 0.3028
REMARK 3 14 2.5500 - 2.4900 0.89 10454 131 0.2863 0.3321
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 25880
REMARK 3 ANGLE : 1.449 34961
REMARK 3 CHIRALITY : 0.069 3854
REMARK 3 PLANARITY : 0.008 4446
REMARK 3 DIHEDRAL : 19.508 3427
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8YN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300045892.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 159460
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% V/V (+/-)-2-METHYL-2,4-PENTANEDIOL,
REMARK 280 0.1 M HEPES PH 7.5, 10 % W/V POLYETHYLENE GLYCOL 10000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 77.45700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 9560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER E 47
REMARK 465 LYS E 48
REMARK 465 LYS E 49
REMARK 465 LYS E 50
REMARK 465 LYS E 51
REMARK 465 ASP E 52
REMARK 465 LEU E 263
REMARK 465 SER E 264
REMARK 465 LEU E 265
REMARK 465 SER C 47
REMARK 465 LYS C 48
REMARK 465 LYS C 49
REMARK 465 LYS C 50
REMARK 465 LYS C 51
REMARK 465 ASP C 52
REMARK 465 LEU C 263
REMARK 465 SER C 264
REMARK 465 LEU C 265
REMARK 465 LEU H 244
REMARK 465 ASN H 245
REMARK 465 GLU H 246
REMARK 465 MET D 1
REMARK 465 LEU D 244
REMARK 465 ASN D 245
REMARK 465 GLU D 246
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 HOH E 797 O HOH E 820 1.85
REMARK 500 O HOH B 806 O HOH B 818 1.89
REMARK 500 O TYR A 148 O HOH A 801 1.89
REMARK 500 O HOH C 721 O HOH C 784 1.89
REMARK 500 OD1 ASP A 393 O HOH A 802 1.91
REMARK 500 ND2 ASN C 339 O HOH C 701 1.95
REMARK 500 O HOH A 878 O HOH A 889 1.97
REMARK 500 NZ LYS A 76 O HOH A 803 1.99
REMARK 500 N MET A 511 O HOH A 804 2.00
REMARK 500 NZ LYS C 8 O HOH C 702 2.00
REMARK 500 O1G ATP C 601 O HOH C 703 2.01
REMARK 500 O LEU D 340 O HOH D 501 2.01
REMARK 500 NZ LYS B 76 O HOH B 801 2.01
REMARK 500 O HOH E 763 O HOH E 817 2.02
REMARK 500 O HOH A 829 O HOH A 870 2.02
REMARK 500 O HOH B 873 O HOH B 917 2.02
REMARK 500 OD1 ASN D 172 O HOH D 502 2.03
REMARK 500 O HIS A 476 O HOH A 805 2.03
REMARK 500 OD1 ASP H 327 O HOH H 501 2.03
REMARK 500 OG1 THR H 36 O HOH H 502 2.04
REMARK 500 NH1 ARG B 355 O HOH B 802 2.04
REMARK 500 O HOH C 777 O HOH C 791 2.05
REMARK 500 OH TYR B 496 O HOH B 803 2.05
REMARK 500 O HOH C 818 O HOH C 826 2.06
REMARK 500 O HOH E 729 O HOH H 609 2.06
REMARK 500 NH1 ARG E 194 O HOH E 701 2.07
REMARK 500 O VAL A 412 O HOH A 806 2.07
REMARK 500 O SER E 536 O HOH E 702 2.07
REMARK 500 OE2 GLU E 238 O HOH E 703 2.08
REMARK 500 OE1 GLU B 554 O HOH B 804 2.09
REMARK 500 OD2 ASP E 232 O HOH E 704 2.09
REMARK 500 O GLU A 427 O HOH A 807 2.09
REMARK 500 O HOH D 571 O HOH D 597 2.09
REMARK 500 OG SER B 413 O HOH B 805 2.09
REMARK 500 OE1 GLU C 449 O HOH C 704 2.11
REMARK 500 NE ARG C 528 O HOH C 705 2.11
REMARK 500 OD2 ASP A 393 O HOH A 808 2.11
REMARK 500 OE2 GLU C 495 O HOH C 706 2.11
REMARK 500 O HOH E 791 O HOH E 821 2.12
REMARK 500 O HOH C 753 O HOH C 796 2.12
REMARK 500 O GLU E 62 O HOH E 705 2.13
REMARK 500 OE2 GLU D 297 O HOH D 503 2.13
REMARK 500 NZ LYS B 366 O HOH B 806 2.14
REMARK 500 O HOH B 915 O HOH B 927 2.14
REMARK 500 OE1 GLU C 500 O HOH C 707 2.16
REMARK 500 O HOH D 538 O HOH D 599 2.16
REMARK 500 O HOH E 766 O HOH E 816 2.17
REMARK 500 O HOH A 846 O HOH A 879 2.17
REMARK 500 OD2 ASP H 263 O HOH H 503 2.17
REMARK 500 OD2 ASP A 418 O HOH A 806 2.17
REMARK 500
REMARK 500 THIS ENTRY HAS 62 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 720 O HOH H 556 1556 1.97
REMARK 500 O HOH B 920 O HOH H 520 2645 2.05
REMARK 500 O HOH E 827 O HOH D 598 1654 2.17
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 GLY E 515 N - CA - C ANGL. DEV. = 17.9 DEGREES
REMARK 500 LEU C 258 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 ALA A 35 N - CA - C ANGL. DEV. = -21.4 DEGREES
REMARK 500 LEU A 524 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 GLY A 527 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 CYS D 238 CA - CB - SG ANGL. DEV. = 7.9 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 ARG B 29 -59.64 71.49
REMARK 500 SER B 123 -131.88 57.81
REMARK 500 ASP B 163 -165.73 -100.16
REMARK 500 SER B 298 51.71 -117.99
REMARK 500 PRO B 603 153.83 -47.97
REMARK 500 PHE E 95 54.38 -119.20
REMARK 500 SER E 122 -6.68 82.69
REMARK 500 ALA E 146 -140.83 48.18
REMARK 500 PRO E 165 -8.00 -59.89
REMARK 500 ILE E 180 -43.26 -132.65
REMARK 500 VAL E 243 69.09 -103.09
REMARK 500 SER E 333 -10.60 -142.90
REMARK 500 HIS E 343 -73.70 -84.21
REMARK 500 PRO E 363 158.29 -48.10
REMARK 500 LYS C 64 -9.26 85.80
REMARK 500 CYS C 76 179.74 82.66
REMARK 500 SER C 78 -1.12 64.56
REMARK 500 SER C 100 -168.52 -102.04
REMARK 500 SER C 122 -4.80 81.17
REMARK 500 ALA C 146 -135.15 41.56
REMARK 500 PHE C 212 -50.15 -129.13
REMARK 500 HIS C 244 15.82 80.88
REMARK 500 SER C 333 -4.49 -146.79
REMARK 500 ARG C 361 -71.45 -98.68
REMARK 500 LYS C 535 76.15 -119.61
REMARK 500 SER H 147 77.13 -103.31
REMARK 500 GLU H 346 31.18 -99.36
REMARK 500 MET H 358 53.55 -146.86
REMARK 500 ARG A 29 -130.67 59.40
REMARK 500 ARG A 100 -8.43 -59.91
REMARK 500 ARG A 114 40.45 70.77
REMARK 500 SER A 123 -135.67 60.43
REMARK 500 GLU A 252 34.33 -150.26
REMARK 500 SER A 298 53.82 -118.14
REMARK 500 GLN A 529 -135.69 54.03
REMARK 500 LEU A 530 -57.88 -125.95
REMARK 500 PRO A 603 144.94 -39.95
REMARK 500 GLU D 48 11.79 -153.50
REMARK 500 ASP D 141 -167.45 -100.21
REMARK 500 MET D 358 52.82 -153.26
REMARK 500 LEU D 414 47.08 -95.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 833 DISTANCE = 5.93 ANGSTROMS
DBREF 8YN0 B 2 618 UNP Q9SU72 EDS1C_ARATH 2 618
DBREF 8YN0 E 2 537 UNP Q4F883 SG101_ARATH 2 537
DBREF 8YN0 C 2 537 UNP Q4F883 SG101_ARATH 2 537
DBREF 8YN0 H 1 415 UNP Q9FKZ2 DRL41_ARATH 1 415
DBREF 8YN0 A 2 618 UNP Q9SU72 EDS1C_ARATH 2 618
DBREF 8YN0 D 1 415 UNP Q9FKZ2 DRL41_ARATH 1 415
SEQRES 1 B 617 ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU ILE
SEQRES 2 B 617 THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU THR
SEQRES 3 B 617 GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL ILE
SEQRES 4 B 617 PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE PHE
SEQRES 5 B 617 ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS LEU
SEQRES 6 B 617 ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY LYS
SEQRES 7 B 617 GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS ASN
SEQRES 8 B 617 LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN ALA
SEQRES 9 B 617 SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE VAL
SEQRES 10 B 617 PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE LEU
SEQRES 11 B 617 ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG ASN
SEQRES 12 B 617 PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE GLY
SEQRES 13 B 617 ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA LEU
SEQRES 14 B 617 GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE VAL
SEQRES 15 B 617 SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA ARG
SEQRES 16 B 617 LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU ALA
SEQRES 17 B 617 GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER GLU
SEQRES 18 B 617 GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG ASP
SEQRES 19 B 617 THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU THR
SEQRES 20 B 617 GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER PHE
SEQRES 21 B 617 LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE VAL
SEQRES 22 B 617 PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN SER
SEQRES 23 B 617 ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN ALA
SEQRES 24 B 617 SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG SER
SEQRES 25 B 617 ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN SER
SEQRES 26 B 617 MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU ASN
SEQRES 27 B 617 SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER THR
SEQRES 28 B 617 ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU GLU
SEQRES 29 B 617 LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN VAL
SEQRES 30 B 617 ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP ILE
SEQRES 31 B 617 GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS ASN
SEQRES 32 B 617 GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU ASN
SEQRES 33 B 617 ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA GLY
SEQRES 34 B 617 VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS GLN
SEQRES 35 B 617 LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE LYS
SEQRES 36 B 617 LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU ASP
SEQRES 37 B 617 ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP THR
SEQRES 38 B 617 GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR ILE
SEQRES 39 B 617 TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS PRO
SEQRES 40 B 617 ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS VAL
SEQRES 41 B 617 ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE GLN
SEQRES 42 B 617 GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER CYS
SEQRES 43 B 617 PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO TYR
SEQRES 44 B 617 GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY MET
SEQRES 45 B 617 LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP LYS
SEQRES 46 B 617 GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP TRP
SEQRES 47 B 617 ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO LEU
SEQRES 48 B 617 ARG ASP TYR MET MET ASP
SEQRES 1 E 536 GLU SER SER SER SER LEU LYS GLY SER ALA LEU GLY LYS
SEQRES 2 E 536 LEU VAL VAL THR SER GLY LEU LEU HIS SER SER TRP SER
SEQRES 3 E 536 LYS ILE LEU GLU ILE HIS ASN PRO PRO TYR SER ASN HIS
SEQRES 4 E 536 ASP PRO GLY LEU GLN VAL SER LYS LYS LYS LYS ASP SER
SEQRES 5 E 536 GLY LEU GLU PHE GLN ILE HIS ARG GLU GLU LYS PHE THR
SEQRES 6 E 536 LEU VAL VAL PHE SER ALA PRO PRO ILE CYS ARG SER SER
SEQRES 7 E 536 SER SER ASP SER THR LEU LEU HIS VAL LYS ASP LYS GLU
SEQRES 8 E 536 ASN PRO PHE PRO PHE LEU CYS SER GLU ASN ASN PRO SER
SEQRES 9 E 536 PHE SER LEU HIS THR PRO ALA PHE ASN LEU PHE THR SER
SEQRES 10 E 536 ALA SER THR SER LEU THR TYR LEU LYS SER GLU LEU LEU
SEQRES 11 E 536 GLN THR LEU LYS SER GLU LYS PRO VAL ILE ILE THR GLY
SEQRES 12 E 536 ALA ALA LEU GLY GLY SER VAL ALA SER LEU TYR THR LEU
SEQRES 13 E 536 TRP LEU LEU GLU THR ILE GLU PRO THR LEU LYS ARG PRO
SEQRES 14 E 536 LEU CYS ILE THR PHE GLY SER PRO LEU ILE GLY ASP ALA
SEQRES 15 E 536 SER LEU GLN GLN ILE LEU GLU ASN SER VAL ARG ASN SER
SEQRES 16 E 536 CYS PHE LEU HIS VAL VAL SER ALA GLN THR ARG ILE LYS
SEQRES 17 E 536 MET ASP PHE PHE LYS PRO PHE GLY THR PHE LEU ILE CYS
SEQRES 18 E 536 PHE ASP SER GLY CYS VAL CYS ILE GLU ASP HIS VAL ALA
SEQRES 19 E 536 VAL THR GLU LEU LEU ASN GLY VAL HIS ASP SER GLY LEU
SEQRES 20 E 536 VAL ASP TYR SER GLN VAL LEU ASN ARG LEU ASP GLN SER
SEQRES 21 E 536 MET LEU SER LEU ALA ASP SER ARG LEU ILE PRO GLU ASP
SEQRES 22 E 536 VAL ILE LYS GLY ILE GLU LYS ARG ALA GLU MET LYS ASN
SEQRES 23 E 536 LEU ARG PHE ASP MET MET PHE LYS LYS LEU ASN ASP MET
SEQRES 24 E 536 LYS ILE SER MET ALA TYR ILE GLU TRP TYR LYS LYS LYS
SEQRES 25 E 536 CYS LYS GLU VAL LYS ILE GLY TYR TYR ASP ARG PHE LYS
SEQRES 26 E 536 THR GLN LEU ALA PHE PRO SER LYS GLU PHE ASP ILE ASN
SEQRES 27 E 536 ILE LYS ASN HIS HIS LYS SER GLU LEU ASN ARG PHE TRP
SEQRES 28 E 536 LYS SER VAL VAL GLU GLU VAL GLU ARG ARG PRO GLN SER
SEQRES 29 E 536 ASP ALA SER ILE LEU LYS ARG ARG PHE LEU PHE SER GLY
SEQRES 30 E 536 ASN ASN TYR ARG ARG MET ILE GLU PRO LEU ASP ILE ALA
SEQRES 31 E 536 GLU TYR TYR LEU GLU GLY ARG LYS GLU TYR ARG THR THR
SEQRES 32 E 536 GLY ARG SER HIS HIS TYR VAL MET LEU GLU LYS TRP PHE
SEQRES 33 E 536 GLY MET GLU SER ILE LEU ILE GLU LYS GLU ARG CYS LYS
SEQRES 34 E 536 LYS ARG ASP LEU SER ASP LEU LEU THR PHE ASP SER CYS
SEQRES 35 E 536 PHE TRP ALA GLU VAL GLU ASP SER LEU ILE VAL ILE ASN
SEQRES 36 E 536 GLN LEU ASN THR THR VAL GLY MET ARG ASP ASP VAL ARG
SEQRES 37 E 536 GLU VAL LEU THR ARG LYS LEU VAL GLU PHE GLU GLY TYR
SEQRES 38 E 536 VAL TRP GLU ILE ILE THR LYS ARG GLU VAL SER PRO GLU
SEQRES 39 E 536 ILE PHE LEU GLU GLU SER SER PHE MET LYS TRP TRP LYS
SEQRES 40 E 536 GLU TYR LYS LYS ILE LYS GLY PHE ASN SER SER TYR LEU
SEQRES 41 E 536 THR GLU PHE MET ASN THR ARG LYS TYR GLU SER TYR GLY
SEQRES 42 E 536 LYS SER GLN
SEQRES 1 C 536 GLU SER SER SER SER LEU LYS GLY SER ALA LEU GLY LYS
SEQRES 2 C 536 LEU VAL VAL THR SER GLY LEU LEU HIS SER SER TRP SER
SEQRES 3 C 536 LYS ILE LEU GLU ILE HIS ASN PRO PRO TYR SER ASN HIS
SEQRES 4 C 536 ASP PRO GLY LEU GLN VAL SER LYS LYS LYS LYS ASP SER
SEQRES 5 C 536 GLY LEU GLU PHE GLN ILE HIS ARG GLU GLU LYS PHE THR
SEQRES 6 C 536 LEU VAL VAL PHE SER ALA PRO PRO ILE CYS ARG SER SER
SEQRES 7 C 536 SER SER ASP SER THR LEU LEU HIS VAL LYS ASP LYS GLU
SEQRES 8 C 536 ASN PRO PHE PRO PHE LEU CYS SER GLU ASN ASN PRO SER
SEQRES 9 C 536 PHE SER LEU HIS THR PRO ALA PHE ASN LEU PHE THR SER
SEQRES 10 C 536 ALA SER THR SER LEU THR TYR LEU LYS SER GLU LEU LEU
SEQRES 11 C 536 GLN THR LEU LYS SER GLU LYS PRO VAL ILE ILE THR GLY
SEQRES 12 C 536 ALA ALA LEU GLY GLY SER VAL ALA SER LEU TYR THR LEU
SEQRES 13 C 536 TRP LEU LEU GLU THR ILE GLU PRO THR LEU LYS ARG PRO
SEQRES 14 C 536 LEU CYS ILE THR PHE GLY SER PRO LEU ILE GLY ASP ALA
SEQRES 15 C 536 SER LEU GLN GLN ILE LEU GLU ASN SER VAL ARG ASN SER
SEQRES 16 C 536 CYS PHE LEU HIS VAL VAL SER ALA GLN THR ARG ILE LYS
SEQRES 17 C 536 MET ASP PHE PHE LYS PRO PHE GLY THR PHE LEU ILE CYS
SEQRES 18 C 536 PHE ASP SER GLY CYS VAL CYS ILE GLU ASP HIS VAL ALA
SEQRES 19 C 536 VAL THR GLU LEU LEU ASN GLY VAL HIS ASP SER GLY LEU
SEQRES 20 C 536 VAL ASP TYR SER GLN VAL LEU ASN ARG LEU ASP GLN SER
SEQRES 21 C 536 MET LEU SER LEU ALA ASP SER ARG LEU ILE PRO GLU ASP
SEQRES 22 C 536 VAL ILE LYS GLY ILE GLU LYS ARG ALA GLU MET LYS ASN
SEQRES 23 C 536 LEU ARG PHE ASP MET MET PHE LYS LYS LEU ASN ASP MET
SEQRES 24 C 536 LYS ILE SER MET ALA TYR ILE GLU TRP TYR LYS LYS LYS
SEQRES 25 C 536 CYS LYS GLU VAL LYS ILE GLY TYR TYR ASP ARG PHE LYS
SEQRES 26 C 536 THR GLN LEU ALA PHE PRO SER LYS GLU PHE ASP ILE ASN
SEQRES 27 C 536 ILE LYS ASN HIS HIS LYS SER GLU LEU ASN ARG PHE TRP
SEQRES 28 C 536 LYS SER VAL VAL GLU GLU VAL GLU ARG ARG PRO GLN SER
SEQRES 29 C 536 ASP ALA SER ILE LEU LYS ARG ARG PHE LEU PHE SER GLY
SEQRES 30 C 536 ASN ASN TYR ARG ARG MET ILE GLU PRO LEU ASP ILE ALA
SEQRES 31 C 536 GLU TYR TYR LEU GLU GLY ARG LYS GLU TYR ARG THR THR
SEQRES 32 C 536 GLY ARG SER HIS HIS TYR VAL MET LEU GLU LYS TRP PHE
SEQRES 33 C 536 GLY MET GLU SER ILE LEU ILE GLU LYS GLU ARG CYS LYS
SEQRES 34 C 536 LYS ARG ASP LEU SER ASP LEU LEU THR PHE ASP SER CYS
SEQRES 35 C 536 PHE TRP ALA GLU VAL GLU ASP SER LEU ILE VAL ILE ASN
SEQRES 36 C 536 GLN LEU ASN THR THR VAL GLY MET ARG ASP ASP VAL ARG
SEQRES 37 C 536 GLU VAL LEU THR ARG LYS LEU VAL GLU PHE GLU GLY TYR
SEQRES 38 C 536 VAL TRP GLU ILE ILE THR LYS ARG GLU VAL SER PRO GLU
SEQRES 39 C 536 ILE PHE LEU GLU GLU SER SER PHE MET LYS TRP TRP LYS
SEQRES 40 C 536 GLU TYR LYS LYS ILE LYS GLY PHE ASN SER SER TYR LEU
SEQRES 41 C 536 THR GLU PHE MET ASN THR ARG LYS TYR GLU SER TYR GLY
SEQRES 42 C 536 LYS SER GLN
SEQRES 1 H 415 MET ASN SER ASN SER ILE GLN SER PHE ASP ALA LEU PRO
SEQRES 2 H 415 HIS ASN LEU ARG GLU CYS PHE LEU ASP MET ALA SER PHE
SEQRES 3 H 415 LEU GLU ASP GLN ARG ILE ILE ALA SER THR ILE ILE ASP
SEQRES 4 H 415 LEU TRP SER ALA SER TYR GLY LYS GLU GLY MET ASN ASN
SEQRES 5 H 415 LEU GLN ASP LEU ALA SER ARG ASN LEU LEU LYS LEU LEU
SEQRES 6 H 415 PRO ILE GLY ARG ASN GLU TYR GLU ASP GLY PHE TYR ASN
SEQRES 7 H 415 GLU LEU LEU VAL LYS GLN ASP ASN VAL LEU ARG GLU PHE
SEQRES 8 H 415 ALA ILE ASN GLN CYS LEU LYS GLU SER SER SER ILE PHE
SEQRES 9 H 415 GLU ARG LYS ARG LEU ASN LEU GLU ILE GLN ASP ASN LYS
SEQRES 10 H 415 PHE PRO ASN TRP CYS LEU ASN PRO LYS GLN PRO ILE VAL
SEQRES 11 H 415 ILE ASN ALA SER LEU PHE SER ILE SER THR ASP ASP SER
SEQRES 12 H 415 PHE ALA SER SER TRP PHE GLU MET ASP CYS PRO ASN VAL
SEQRES 13 H 415 GLU ALA LEU VAL LEU ASN ILE SER SER SER ASN TYR ALA
SEQRES 14 H 415 LEU PRO ASN PHE ILE ALA THR MET LYS GLU LEU LYS VAL
SEQRES 15 H 415 VAL ILE ILE ILE ASN HIS GLY LEU GLU PRO ALA LYS LEU
SEQRES 16 H 415 THR ASN LEU SER CYS LEU SER SER LEU PRO ASN LEU LYS
SEQRES 17 H 415 ARG ILE ARG PHE GLU LYS VAL SER ILE SER LEU LEU ASP
SEQRES 18 H 415 ILE PRO LYS LEU GLY LEU LYS SER LEU GLU LYS LEU SER
SEQRES 19 H 415 LEU TRP PHE CYS HIS VAL VAL ASP ALA LEU ASN GLU LEU
SEQRES 20 H 415 GLU ASP VAL SER GLU THR LEU GLN SER LEU GLN GLU ILE
SEQRES 21 H 415 GLU ILE ASP TYR CYS TYR ASN LEU ASP GLU LEU PRO TYR
SEQRES 22 H 415 TRP ILE SER GLN VAL VAL SER LEU LYS LYS LEU SER VAL
SEQRES 23 H 415 THR ASN CYS ASN LYS LEU CYS ARG VAL ILE GLU ALA ILE
SEQRES 24 H 415 GLY ASP LEU ARG ASP LEU GLU THR LEU ARG LEU SER SER
SEQRES 25 H 415 CYS ALA SER LEU LEU GLU LEU PRO GLU THR ILE ASP ARG
SEQRES 26 H 415 LEU ASP ASN LEU ARG PHE LEU ASP VAL SER GLY GLY PHE
SEQRES 27 H 415 GLN LEU LYS ASN LEU PRO LEU GLU ILE GLY LYS LEU LYS
SEQRES 28 H 415 LYS LEU GLU LYS ILE SER MET LYS ASP CYS TYR ARG CYS
SEQRES 29 H 415 GLU LEU PRO ASP SER VAL LYS ASN LEU GLU ASN LEU GLU
SEQRES 30 H 415 VAL LYS CYS ASP GLU ASP THR ALA PHE LEU TRP LYS ILE
SEQRES 31 H 415 LEU LYS PRO GLU MET LYS ASN LEU THR ILE THR GLU GLU
SEQRES 32 H 415 LYS THR GLU HIS ASN LEU ASN LEU LEU GLN LEU PHE
SEQRES 1 A 617 ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU ILE
SEQRES 2 A 617 THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU THR
SEQRES 3 A 617 GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL ILE
SEQRES 4 A 617 PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE PHE
SEQRES 5 A 617 ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS LEU
SEQRES 6 A 617 ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY LYS
SEQRES 7 A 617 GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS ASN
SEQRES 8 A 617 LEU GLU ALA ILE ILE ASP PRO ARG THR SER PHE GLN ALA
SEQRES 9 A 617 SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE VAL
SEQRES 10 A 617 PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE LEU
SEQRES 11 A 617 ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG ASN
SEQRES 12 A 617 PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE GLY
SEQRES 13 A 617 ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA LEU
SEQRES 14 A 617 GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE VAL
SEQRES 15 A 617 SER ARG PHE ASP ILE VAL PRO ARG ILE MET LEU ALA ARG
SEQRES 16 A 617 LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU ALA
SEQRES 17 A 617 GLN LEU ASP PRO ARG LYS SER SER VAL GLN GLU SER GLU
SEQRES 18 A 617 GLN ARG ILE THR GLU PHE TYR THR ARG VAL MET ARG ASP
SEQRES 19 A 617 THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU THR
SEQRES 20 A 617 GLY SER ALA GLU ALA PHE LEU GLU THR LEU SER SER PHE
SEQRES 21 A 617 LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE VAL
SEQRES 22 A 617 PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN SER
SEQRES 23 A 617 ASP ALA ILE LEU GLN MET LEU PHE TYR THR SER GLN ALA
SEQRES 24 A 617 SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG SER
SEQRES 25 A 617 ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN SER
SEQRES 26 A 617 MET GLY LYS LYS LEU PHE ASN HIS LEU ASP GLY GLU ASN
SEQRES 27 A 617 SER ILE GLU SER THR LEU ASN ASP LEU GLY VAL SER THR
SEQRES 28 A 617 ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU GLU
SEQRES 29 A 617 LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN VAL
SEQRES 30 A 617 ILE GLU GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP ILE
SEQRES 31 A 617 GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS ASN
SEQRES 32 A 617 GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU ASN
SEQRES 33 A 617 ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA GLY
SEQRES 34 A 617 VAL PHE ASP GLU VAL LEU GLY LEU MET LYS LYS CYS GLN
SEQRES 35 A 617 LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE LYS
SEQRES 36 A 617 LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU ASP
SEQRES 37 A 617 ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP THR
SEQRES 38 A 617 GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR ILE
SEQRES 39 A 617 TYR ALA GLN ARG GLY TYR GLU HIS TYR ILE LEU LYS PRO
SEQRES 40 A 617 ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS VAL
SEQRES 41 A 617 ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE GLN
SEQRES 42 A 617 GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER CYS
SEQRES 43 A 617 PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO TYR
SEQRES 44 A 617 GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY MET
SEQRES 45 A 617 LEU GLY GLU TRP ILE THR ASP GLY GLU VAL ASP ASP LYS
SEQRES 46 A 617 GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP TRP
SEQRES 47 A 617 ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO LEU
SEQRES 48 A 617 ARG ASP TYR MET MET ASP
SEQRES 1 D 415 MET ASN SER ASN SER ILE GLN SER PHE ASP ALA LEU PRO
SEQRES 2 D 415 HIS ASN LEU ARG GLU CYS PHE LEU ASP MET ALA SER PHE
SEQRES 3 D 415 LEU GLU ASP GLN ARG ILE ILE ALA SER THR ILE ILE ASP
SEQRES 4 D 415 LEU TRP SER ALA SER TYR GLY LYS GLU GLY MET ASN ASN
SEQRES 5 D 415 LEU GLN ASP LEU ALA SER ARG ASN LEU LEU LYS LEU LEU
SEQRES 6 D 415 PRO ILE GLY ARG ASN GLU TYR GLU ASP GLY PHE TYR ASN
SEQRES 7 D 415 GLU LEU LEU VAL LYS GLN ASP ASN VAL LEU ARG GLU PHE
SEQRES 8 D 415 ALA ILE ASN GLN CYS LEU LYS GLU SER SER SER ILE PHE
SEQRES 9 D 415 GLU ARG LYS ARG LEU ASN LEU GLU ILE GLN ASP ASN LYS
SEQRES 10 D 415 PHE PRO ASN TRP CYS LEU ASN PRO LYS GLN PRO ILE VAL
SEQRES 11 D 415 ILE ASN ALA SER LEU PHE SER ILE SER THR ASP ASP SER
SEQRES 12 D 415 PHE ALA SER SER TRP PHE GLU MET ASP CYS PRO ASN VAL
SEQRES 13 D 415 GLU ALA LEU VAL LEU ASN ILE SER SER SER ASN TYR ALA
SEQRES 14 D 415 LEU PRO ASN PHE ILE ALA THR MET LYS GLU LEU LYS VAL
SEQRES 15 D 415 VAL ILE ILE ILE ASN HIS GLY LEU GLU PRO ALA LYS LEU
SEQRES 16 D 415 THR ASN LEU SER CYS LEU SER SER LEU PRO ASN LEU LYS
SEQRES 17 D 415 ARG ILE ARG PHE GLU LYS VAL SER ILE SER LEU LEU ASP
SEQRES 18 D 415 ILE PRO LYS LEU GLY LEU LYS SER LEU GLU LYS LEU SER
SEQRES 19 D 415 LEU TRP PHE CYS HIS VAL VAL ASP ALA LEU ASN GLU LEU
SEQRES 20 D 415 GLU ASP VAL SER GLU THR LEU GLN SER LEU GLN GLU ILE
SEQRES 21 D 415 GLU ILE ASP TYR CYS TYR ASN LEU ASP GLU LEU PRO TYR
SEQRES 22 D 415 TRP ILE SER GLN VAL VAL SER LEU LYS LYS LEU SER VAL
SEQRES 23 D 415 THR ASN CYS ASN LYS LEU CYS ARG VAL ILE GLU ALA ILE
SEQRES 24 D 415 GLY ASP LEU ARG ASP LEU GLU THR LEU ARG LEU SER SER
SEQRES 25 D 415 CYS ALA SER LEU LEU GLU LEU PRO GLU THR ILE ASP ARG
SEQRES 26 D 415 LEU ASP ASN LEU ARG PHE LEU ASP VAL SER GLY GLY PHE
SEQRES 27 D 415 GLN LEU LYS ASN LEU PRO LEU GLU ILE GLY LYS LEU LYS
SEQRES 28 D 415 LYS LEU GLU LYS ILE SER MET LYS ASP CYS TYR ARG CYS
SEQRES 29 D 415 GLU LEU PRO ASP SER VAL LYS ASN LEU GLU ASN LEU GLU
SEQRES 30 D 415 VAL LYS CYS ASP GLU ASP THR ALA PHE LEU TRP LYS ILE
SEQRES 31 D 415 LEU LYS PRO GLU MET LYS ASN LEU THR ILE THR GLU GLU
SEQRES 32 D 415 LYS THR GLU HIS ASN LEU ASN LEU LEU GLN LEU PHE
HET APR B 701 55
HET ATP E 601 42
HET ATP C 601 42
HET APR A 701 55
HETNAM APR ADENOSINE-5-DIPHOSPHORIBOSE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 7 APR 2(C15 H23 N5 O14 P2)
FORMUL 8 ATP 2(C10 H16 N5 O13 P3)
FORMUL 11 HOH *704(H2 O)
HELIX 1 AA1 ALA B 2 GLY B 8 1 7
HELIX 2 AA2 GLY B 11 THR B 27 1 17
HELIX 3 AA3 SER B 48 PHE B 52 5 5
HELIX 4 AA4 GLU B 87 ASP B 98 1 12
HELIX 5 AA5 SER B 102 SER B 113 1 12
HELIX 6 AA6 SER B 123 TYR B 140 1 18
HELIX 7 AA7 ASN B 146 LEU B 149 5 4
HELIX 8 AA8 SER B 164 GLU B 173 1 10
HELIX 9 AA9 TRP B 175 ARG B 177 5 3
HELIX 10 AB1 ILE B 188 MET B 193 1 6
HELIX 11 AB2 ARG B 196 GLU B 201 1 6
HELIX 12 AB3 THR B 203 ASP B 212 1 10
HELIX 13 AB4 SER B 221 LEU B 247 1 27
HELIX 14 AB5 GLU B 252 SER B 260 1 9
HELIX 15 AB6 ASN B 286 THR B 297 1 12
HELIX 16 AB7 ASP B 302 ASP B 316 1 15
HELIX 17 AB8 SER B 319 SER B 326 1 8
HELIX 18 AB9 MET B 327 LYS B 330 5 4
HELIX 19 AC1 ASP B 336 GLU B 338 5 3
HELIX 20 AC2 ILE B 341 ASP B 347 1 7
HELIX 21 AC3 SER B 351 GLN B 381 1 31
HELIX 22 AC4 GLN B 381 GLU B 394 1 14
HELIX 23 AC5 GLU B 394 HIS B 402 1 9
HELIX 24 AC6 ASN B 404 VAL B 412 1 9
HELIX 25 AC7 GLU B 415 LYS B 441 1 27
HELIX 26 AC8 GLU B 447 GLY B 450 5 4
HELIX 27 AC9 ASP B 451 HIS B 476 1 26
HELIX 28 AD1 LYS B 478 GLY B 483 1 6
HELIX 29 AD2 PRO B 484 GLY B 489 1 6
HELIX 30 AD3 PRO B 491 LYS B 507 1 17
HELIX 31 AD4 PRO B 508 GLY B 510 5 3
HELIX 32 AD5 ILE B 512 LEU B 524 1 13
HELIX 33 AD6 GLN B 529 LEU B 537 1 9
HELIX 34 AD7 CYS B 544 SER B 546 5 3
HELIX 35 AD8 CYS B 547 LYS B 556 1 10
HELIX 36 AD9 PRO B 559 GLU B 562 5 4
HELIX 37 AE1 VAL B 563 ASP B 580 1 18
HELIX 38 AE2 SER B 593 THR B 601 1 9
HELIX 39 AE3 PRO B 603 SER B 610 1 8
HELIX 40 AE4 SER E 3 GLY E 20 1 18
HELIX 41 AE5 GLY E 20 ASN E 34 1 15
HELIX 42 AE6 ASP E 41 GLN E 45 5 5
HELIX 43 AE7 PHE E 95 CYS E 99 5 5
HELIX 44 AE8 THR E 110 ALA E 119 1 10
HELIX 45 AE9 LEU E 123 SER E 136 1 14
HELIX 46 AF1 ALA E 146 LEU E 160 1 15
HELIX 47 AF2 ASP E 182 GLU E 190 1 9
HELIX 48 AF3 VAL E 193 SER E 196 5 4
HELIX 49 AF4 ASP E 232 ASN E 241 1 10
HELIX 50 AF5 ASP E 250 SER E 261 1 12
HELIX 51 AF6 PRO E 272 VAL E 317 1 46
HELIX 52 AF7 GLY E 320 PHE E 331 1 12
HELIX 53 AF8 LYS E 334 HIS E 343 1 10
HELIX 54 AF9 HIS E 343 GLU E 360 1 18
HELIX 55 AG1 LYS E 371 GLU E 396 1 26
HELIX 56 AG2 GLU E 400 GLY E 405 1 6
HELIX 57 AG3 SER E 407 ILE E 422 1 16
HELIX 58 AG4 CYS E 443 THR E 461 1 19
HELIX 59 AG5 ARG E 465 LYS E 489 1 25
HELIX 60 AG6 SER E 493 LEU E 498 5 6
HELIX 61 AG7 SER E 501 LYS E 514 1 14
HELIX 62 AG8 SER E 519 THR E 527 1 9
HELIX 63 AG9 ARG E 528 TYR E 533 5 6
HELIX 64 AH1 SER C 3 GLY C 20 1 18
HELIX 65 AH2 GLY C 20 ASN C 34 1 15
HELIX 66 AH3 PHE C 95 CYS C 99 5 5
HELIX 67 AH4 THR C 110 THR C 121 1 12
HELIX 68 AH5 LEU C 123 SER C 136 1 14
HELIX 69 AH6 ALA C 146 LEU C 159 1 14
HELIX 70 AH7 ASP C 182 GLU C 190 1 9
HELIX 71 AH8 VAL C 193 SER C 196 5 4
HELIX 72 AH9 ASP C 232 ASN C 241 1 10
HELIX 73 AI1 ASP C 250 SER C 261 1 12
HELIX 74 AI2 PRO C 272 VAL C 317 1 46
HELIX 75 AI3 GLY C 320 PHE C 331 1 12
HELIX 76 AI4 LYS C 334 HIS C 343 1 10
HELIX 77 AI5 HIS C 343 GLU C 360 1 18
HELIX 78 AI6 LYS C 371 GLU C 396 1 26
HELIX 79 AI7 GLU C 400 GLY C 405 1 6
HELIX 80 AI8 SER C 407 LEU C 423 1 17
HELIX 81 AI9 CYS C 443 THR C 461 1 19
HELIX 82 AJ1 ARG C 465 LYS C 489 1 25
HELIX 83 AJ2 SER C 493 LEU C 498 5 6
HELIX 84 AJ3 SER C 501 LYS C 514 1 14
HELIX 85 AJ4 SER C 519 THR C 527 1 9
HELIX 86 AJ5 ARG C 528 TYR C 533 5 6
HELIX 87 AJ6 SER H 5 ALA H 11 1 7
HELIX 88 AJ7 PRO H 13 MET H 23 1 11
HELIX 89 AJ8 ALA H 24 PHE H 26 5 3
HELIX 90 AJ9 ALA H 34 GLY H 46 1 13
HELIX 91 AK1 GLU H 48 ARG H 59 1 12
HELIX 92 AK2 GLU H 71 GLY H 75 5 5
HELIX 93 AK3 ASP H 85 GLU H 99 1 15
HELIX 94 AK4 PRO H 119 ASN H 124 5 6
HELIX 95 AK5 PRO H 171 MET H 177 5 7
HELIX 96 AK6 ASN H 197 SER H 202 5 6
HELIX 97 AK7 ASP H 221 GLY H 226 5 6
HELIX 98 AK8 PRO H 272 GLN H 277 1 6
HELIX 99 AK9 ILE H 296 LEU H 302 5 7
HELIX 100 AL1 PRO H 320 LEU H 326 5 7
HELIX 101 AL2 GLU H 346 LEU H 350 5 5
HELIX 102 AL3 PRO H 367 LEU H 373 5 7
HELIX 103 AL4 ASP H 381 LYS H 392 1 12
HELIX 104 AL5 PRO H 393 MET H 395 5 3
HELIX 105 AL6 LEU H 409 PHE H 415 5 7
HELIX 106 AL7 PHE A 3 GLY A 8 1 6
HELIX 107 AL8 ASN A 10 THR A 27 1 18
HELIX 108 AL9 SER A 48 PHE A 52 5 5
HELIX 109 AM1 GLU A 87 ASP A 98 1 12
HELIX 110 AM2 SER A 102 ARG A 114 1 13
HELIX 111 AM3 SER A 123 TYR A 140 1 18
HELIX 112 AM4 ASN A 146 GLU A 150 5 5
HELIX 113 AM5 SER A 164 GLU A 173 1 10
HELIX 114 AM6 TRP A 175 ARG A 177 5 3
HELIX 115 AM7 ILE A 188 MET A 193 1 6
HELIX 116 AM8 ARG A 196 GLU A 201 1 6
HELIX 117 AM9 THR A 203 ASP A 212 1 10
HELIX 118 AN1 SER A 221 LEU A 247 1 27
HELIX 119 AN2 GLU A 252 SER A 260 1 9
HELIX 120 AN3 ASN A 286 THR A 297 1 12
HELIX 121 AN4 ASP A 302 ASP A 316 1 15
HELIX 122 AN5 SER A 319 GLN A 325 1 7
HELIX 123 AN6 SER A 326 LYS A 330 5 5
HELIX 124 AN7 ASP A 336 GLU A 338 5 3
HELIX 125 AN8 ILE A 341 LEU A 348 1 8
HELIX 126 AN9 SER A 351 GLN A 381 1 31
HELIX 127 AO1 GLN A 381 GLU A 394 1 14
HELIX 128 AO2 GLU A 394 HIS A 402 1 9
HELIX 129 AO3 ASN A 404 VAL A 412 1 9
HELIX 130 AO4 GLU A 415 LYS A 441 1 27
HELIX 131 AO5 GLU A 447 GLY A 450 5 4
HELIX 132 AO6 ASP A 451 HIS A 476 1 26
HELIX 133 AO7 LYS A 478 GLY A 483 1 6
HELIX 134 AO8 PRO A 484 GLY A 489 1 6
HELIX 135 AO9 PRO A 491 LYS A 507 1 17
HELIX 136 AP1 PRO A 508 GLY A 510 5 3
HELIX 137 AP2 ILE A 512 LEU A 524 1 13
HELIX 138 AP3 LEU A 530 LEU A 537 1 8
HELIX 139 AP4 CYS A 544 SER A 546 5 3
HELIX 140 AP5 CYS A 547 LYS A 556 1 10
HELIX 141 AP6 PRO A 559 GLY A 581 1 23
HELIX 142 AP7 SER A 593 ILE A 600 1 8
HELIX 143 AP8 PRO A 603 HIS A 609 1 7
HELIX 144 AP9 ASN D 4 ALA D 11 1 8
HELIX 145 AQ1 PRO D 13 MET D 23 1 11
HELIX 146 AQ2 ALA D 24 PHE D 26 5 3
HELIX 147 AQ3 ALA D 34 ALA D 43 1 10
HELIX 148 AQ4 GLU D 48 ARG D 59 1 12
HELIX 149 AQ5 GLU D 71 GLY D 75 5 5
HELIX 150 AQ6 ASP D 85 GLU D 99 1 15
HELIX 151 AQ7 SER D 102 ARG D 106 5 5
HELIX 152 AQ8 PRO D 119 LEU D 123 5 5
HELIX 153 AQ9 PRO D 171 MET D 177 5 7
HELIX 154 AR1 ASN D 197 SER D 202 5 6
HELIX 155 AR2 ASP D 221 GLY D 226 5 6
HELIX 156 AR3 PRO D 272 GLN D 277 1 6
HELIX 157 AR4 ILE D 296 LEU D 302 5 7
HELIX 158 AR5 PRO D 320 LEU D 326 5 7
HELIX 159 AR6 GLU D 346 LEU D 350 5 5
HELIX 160 AR7 PRO D 367 LEU D 373 5 7
HELIX 161 AR8 ASP D 381 LYS D 392 1 12
HELIX 162 AR9 LEU D 409 PHE D 415 5 7
SHEET 1 AA1 8 TYR B 30 ALA B 35 0
SHEET 2 AA1 8 VAL B 38 PHE B 43 -1 O VAL B 38 N ALA B 35
SHEET 3 AA1 8 GLN B 116 HIS B 122 1 O VAL B 118 N PHE B 41
SHEET 4 AA1 8 PRO B 151 PHE B 156 1 O VAL B 154 N PHE B 119
SHEET 5 AA1 8 PHE B 179 SER B 184 1 O PHE B 182 N THR B 155
SHEET 6 AA1 8 THR B 272 SER B 276 1 O VAL B 274 N ASN B 181
SHEET 7 AA1 8 ARG B 280 VAL B 284 -1 O VAL B 284 N PHE B 273
SHEET 8 AA1 8 LEU B 331 HIS B 334 1 O ASN B 333 N ALA B 283
SHEET 1 AA2 2 GLU B 63 LYS B 65 0
SHEET 2 AA2 2 THR B 84 ASN B 86 -1 O VAL B 85 N ILE B 64
SHEET 1 AA3 2 GLY B 162 ASP B 163 0
SHEET 2 AA3 2 TYR B 267 ARG B 268 -1 O ARG B 268 N GLY B 162
SHEET 1 AA4 7 GLU E 56 ARG E 61 0
SHEET 2 AA4 7 THR E 66 SER E 71 -1 O LEU E 67 N HIS E 60
SHEET 3 AA4 7 VAL E 140 ALA E 145 1 O THR E 143 N VAL E 68
SHEET 4 AA4 7 LEU E 171 PHE E 175 1 O LEU E 171 N ILE E 142
SHEET 5 AA4 7 PHE E 198 SER E 203 1 O LEU E 199 N CYS E 172
SHEET 6 AA4 7 THR E 218 CYS E 222 1 O LEU E 220 N VAL E 202
SHEET 7 AA4 7 CYS E 227 ILE E 230 -1 O ILE E 230 N PHE E 219
SHEET 1 AA5 2 SER E 83 HIS E 87 0
SHEET 2 AA5 2 SER E 105 HIS E 109 -1 O PHE E 106 N LEU E 86
SHEET 1 AA6 7 GLU C 56 GLU C 62 0
SHEET 2 AA6 7 PHE C 65 SER C 71 -1 O LEU C 67 N HIS C 60
SHEET 3 AA6 7 VAL C 140 ALA C 145 1 O THR C 143 N VAL C 68
SHEET 4 AA6 7 LEU C 171 PHE C 175 1 O LEU C 171 N ILE C 142
SHEET 5 AA6 7 PHE C 198 SER C 203 1 O LEU C 199 N CYS C 172
SHEET 6 AA6 7 THR C 218 CYS C 222 1 O THR C 218 N HIS C 200
SHEET 7 AA6 7 CYS C 227 ILE C 230 -1 O ILE C 230 N PHE C 219
SHEET 1 AA7 2 SER C 83 HIS C 87 0
SHEET 2 AA7 2 SER C 105 HIS C 109 -1 O PHE C 106 N LEU C 86
SHEET 1 AA8 3 ILE H 32 ILE H 33 0
SHEET 2 AA8 3 LEU H 80 LYS H 83 -1 O VAL H 82 N ILE H 32
SHEET 3 AA8 3 LYS H 63 PRO H 66 -1 N LYS H 63 O LYS H 83
SHEET 1 AA913 ARG H 108 ILE H 113 0
SHEET 2 AA913 LEU H 135 THR H 140 1 O SER H 137 N LEU H 111
SHEET 3 AA913 ALA H 158 ILE H 163 1 O ASN H 162 N ILE H 138
SHEET 4 AA913 VAL H 182 ASN H 187 1 O ILE H 184 N LEU H 161
SHEET 5 AA913 ARG H 209 GLU H 213 1 O ARG H 211 N ILE H 185
SHEET 6 AA913 LYS H 232 TRP H 236 1 O TRP H 236 N PHE H 212
SHEET 7 AA913 GLU H 259 ASP H 263 1 O GLU H 261 N LEU H 233
SHEET 8 AA913 LYS H 283 THR H 287 1 O SER H 285 N ILE H 262
SHEET 9 AA913 THR H 307 SER H 311 1 O ARG H 309 N LEU H 284
SHEET 10 AA913 PHE H 331 ASP H 333 1 O ASP H 333 N LEU H 310
SHEET 11 AA913 LYS H 355 SER H 357 1 O SER H 357 N LEU H 332
SHEET 12 AA913 GLU H 377 CYS H 380 1 O LYS H 379 N ILE H 356
SHEET 13 AA913 THR H 399 GLU H 402 1 O THR H 401 N VAL H 378
SHEET 1 AB1 4 ASN H 167 ALA H 169 0
SHEET 2 AB1 4 ALA H 193 THR H 196 1 O THR H 196 N TYR H 168
SHEET 3 AB1 4 VAL H 215 ILE H 217 1 O SER H 216 N ALA H 193
SHEET 4 AB1 4 HIS H 239 VAL H 240 1 O HIS H 239 N ILE H 217
SHEET 1 AB2 8 TYR A 30 GLU A 34 0
SHEET 2 AB2 8 VAL A 38 PHE A 43 -1 O ALA A 42 N HIS A 31
SHEET 3 AB2 8 GLN A 116 HIS A 122 1 O VAL A 118 N PHE A 41
SHEET 4 AB2 8 ARG A 152 PHE A 156 1 O VAL A 154 N PHE A 119
SHEET 5 AB2 8 PHE A 179 SER A 184 1 O PHE A 182 N THR A 155
SHEET 6 AB2 8 THR A 272 SER A 276 1 O VAL A 274 N ASN A 181
SHEET 7 AB2 8 ARG A 280 VAL A 284 -1 O VAL A 284 N PHE A 273
SHEET 8 AB2 8 LEU A 331 HIS A 334 1 O ASN A 333 N ALA A 283
SHEET 1 AB3 2 GLU A 63 LYS A 65 0
SHEET 2 AB3 2 THR A 84 ASN A 86 -1 O VAL A 85 N ILE A 64
SHEET 1 AB4 2 GLY A 162 ASP A 163 0
SHEET 2 AB4 2 TYR A 267 ARG A 268 -1 O ARG A 268 N GLY A 162
SHEET 1 AB5 3 ILE D 32 ILE D 33 0
SHEET 2 AB5 3 LEU D 80 LYS D 83 -1 O VAL D 82 N ILE D 32
SHEET 3 AB5 3 LYS D 63 PRO D 66 -1 N LYS D 63 O LYS D 83
SHEET 1 AB613 ARG D 108 ILE D 113 0
SHEET 2 AB613 LEU D 135 THR D 140 1 O SER D 137 N LEU D 111
SHEET 3 AB613 ALA D 158 ILE D 163 1 O VAL D 160 N PHE D 136
SHEET 4 AB613 VAL D 182 ASN D 187 1 O ILE D 184 N LEU D 161
SHEET 5 AB613 ARG D 209 GLU D 213 1 O GLU D 213 N ASN D 187
SHEET 6 AB613 LYS D 232 TRP D 236 1 O TRP D 236 N PHE D 212
SHEET 7 AB613 GLU D 259 ASP D 263 1 O GLU D 261 N LEU D 233
SHEET 8 AB613 LYS D 283 THR D 287 1 O THR D 287 N ILE D 262
SHEET 9 AB613 THR D 307 SER D 311 1 O ARG D 309 N VAL D 286
SHEET 10 AB613 PHE D 331 ASP D 333 1 O ASP D 333 N LEU D 308
SHEET 11 AB613 LYS D 355 SER D 357 1 O SER D 357 N LEU D 332
SHEET 12 AB613 GLU D 377 CYS D 380 1 O LYS D 379 N ILE D 356
SHEET 13 AB613 THR D 399 GLU D 402 1 O THR D 399 N VAL D 378
SHEET 1 AB7 4 ASN D 167 ALA D 169 0
SHEET 2 AB7 4 ALA D 193 THR D 196 1 O LYS D 194 N TYR D 168
SHEET 3 AB7 4 VAL D 215 ILE D 217 1 O SER D 216 N ALA D 193
SHEET 4 AB7 4 HIS D 239 VAL D 240 1 O HIS D 239 N ILE D 217
LINK C1D APR B 701 O2' ATP E 601 1555 1555 1.42
LINK O2' ATP C 601 C1D APR A 701 1555 1555 1.42
CISPEP 1 GLN H 127 PRO H 128 0 19.29
CRYST1 91.521 154.914 171.110 90.00 89.69 90.00 P 1 21 1 4
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 0.010926 0.000000 -0.000058 0.00000
SCALE2 0.000000 0.006455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005844 0.00000
TER 5009 ASP B 618
TER 9297 GLN E 537
TER 13585 GLN C 537
TER 16897 PHE H 415
TER 21911 ASP A 618
TER 25215 PHE D 415
MASTER 419 0 4 162 82 0 0 626040 6 194 244
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