HEADER TRANSFERASE 26-OCT-16 5TRM
TITLE CRYSTAL STRUCTURE OF HUMAN GCN5 HISTONE ACETYLTRANSFERASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT2A;
COMPND 3 CHAIN: A, W, V, U, T, S, R, Q, P, O, N, M, L, K, J, F, C, B, D, E, G,
COMPND 4 H, I, X;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 497-662;
COMPND 6 SYNONYM: GENERAL CONTROL OF AMINO ACID SYNTHESIS PROTEIN 5-LIKE 2,
COMPND 7 HISTONE ACETYLTRANSFERASE GCN5,HSGCN5,LYSINE ACETYLTRANSFERASE 2A,
COMPND 8 STAF97;
COMPND 9 EC: 2.3.1.48;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KAT2A, GCN5, GCN5L2, HGCN5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC
KEYWDS APO, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.R.GUO,Y.J.TAO
REVDAT 4 04-OCT-23 5TRM 1 REMARK
REVDAT 3 27-DEC-17 5TRM 1 JRNL
REVDAT 2 20-DEC-17 5TRM 1 JRNL
REVDAT 1 06-DEC-17 5TRM 0
JRNL AUTH Y.WANG,Y.R.GUO,K.LIU,Z.YIN,R.LIU,Y.XIA,L.TAN,P.YANG,J.H.LEE,
JRNL AUTH 2 X.J.LI,D.HAWKE,Y.ZHENG,X.QIAN,J.LYU,J.HE,D.XING,Y.J.TAO,Z.LU
JRNL TITL KAT2A COUPLED WITH THE ALPHA-KGDH COMPLEX ACTS AS A HISTONE
JRNL TITL 2 H3 SUCCINYLTRANSFERASE.
JRNL REF NATURE V. 552 273 2017
JRNL REFN ESSN 1476-4687
JRNL PMID 29211711
JRNL DOI 10.1038/NATURE25003
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2152
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 117238
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 5790
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 48.1857 - 8.9926 0.94 3853 183 0.2047 0.2400
REMARK 3 2 8.9926 - 7.1452 0.98 3791 208 0.1737 0.1811
REMARK 3 3 7.1452 - 6.2442 0.99 3762 213 0.2150 0.2735
REMARK 3 4 6.2442 - 5.6742 0.99 3784 187 0.2349 0.3050
REMARK 3 5 5.6742 - 5.2681 1.00 3746 193 0.2027 0.2722
REMARK 3 6 5.2681 - 4.9578 1.00 3756 189 0.1950 0.2393
REMARK 3 7 4.9578 - 4.7097 1.00 3741 195 0.1824 0.2316
REMARK 3 8 4.7097 - 4.5049 1.00 3762 190 0.1782 0.2337
REMARK 3 9 4.5049 - 4.3316 1.00 3708 208 0.1762 0.2464
REMARK 3 10 4.3316 - 4.1822 1.00 3749 181 0.1920 0.2298
REMARK 3 11 4.1822 - 4.0515 1.00 3697 201 0.1951 0.2574
REMARK 3 12 4.0515 - 3.9357 1.00 3733 165 0.2083 0.2815
REMARK 3 13 3.9357 - 3.8322 1.00 3693 200 0.2091 0.2728
REMARK 3 14 3.8322 - 3.7387 1.00 3719 198 0.2122 0.2563
REMARK 3 15 3.7387 - 3.6537 1.00 3712 193 0.2265 0.3033
REMARK 3 16 3.6537 - 3.5760 1.00 3698 201 0.2361 0.2894
REMARK 3 17 3.5760 - 3.5045 1.00 3687 201 0.2368 0.2990
REMARK 3 18 3.5045 - 3.4384 1.00 3695 186 0.2296 0.3241
REMARK 3 19 3.4384 - 3.3770 1.00 3683 186 0.2205 0.2821
REMARK 3 20 3.3770 - 3.3198 1.00 3700 177 0.2245 0.2930
REMARK 3 21 3.3198 - 3.2662 1.00 3691 191 0.2318 0.3085
REMARK 3 22 3.2662 - 3.2160 1.00 3699 194 0.2453 0.3095
REMARK 3 23 3.2160 - 3.1687 1.00 3688 181 0.2497 0.3203
REMARK 3 24 3.1687 - 3.1241 1.00 3679 207 0.2569 0.3232
REMARK 3 25 3.1241 - 3.0819 1.00 3645 200 0.2616 0.3214
REMARK 3 26 3.0819 - 3.0418 1.00 3701 196 0.2556 0.2856
REMARK 3 27 3.0418 - 3.0038 1.00 3674 180 0.2652 0.3419
REMARK 3 28 3.0038 - 2.9676 1.00 3680 197 0.2652 0.3291
REMARK 3 29 2.9676 - 2.9331 1.00 3654 200 0.2746 0.3561
REMARK 3 30 2.9331 - 2.9002 1.00 3668 189 0.2756 0.3562
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) : 27.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.53
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 : 0.009 32577
REMARK 3 ANGLE : 0.867 43919
REMARK 3 CHIRALITY : 0.054 4700
REMARK 3 PLANARITY : 0.005 5492
REMARK 3 DIHEDRAL : 17.076 12071
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 5TRM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117491
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.54300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1Z4R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M SODIUM FORMATE, 0.1M SODIUM
REMARK 280 ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 173.81850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 86.73700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 86.73700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.90925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 86.73700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 86.73700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 260.72775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 86.73700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.73700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 86.90925
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 86.73700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.73700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 260.72775
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 173.81850
REMARK 290
REMARK 290 REMARK: NULL
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: 24-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, W, V, U, T, S, R, Q, P, O,
REMARK 350 AND CHAINS: N, M, L, K, J, F, C, B, D,
REMARK 350 AND CHAINS: E, G, H, I, X
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 GLY A 495
REMARK 465 SER A 496
REMARK 465 GLY A 497
REMARK 465 THR A 509
REMARK 465 PRO A 510
REMARK 465 LYS A 511
REMARK 465 GLY W 495
REMARK 465 SER W 496
REMARK 465 GLY W 497
REMARK 465 ILE W 498
REMARK 465 THR W 509
REMARK 465 PRO W 510
REMARK 465 LYS W 511
REMARK 465 ALA W 512
REMARK 465 GLY V 495
REMARK 465 SER V 496
REMARK 465 GLY V 497
REMARK 465 ILE V 498
REMARK 465 THR V 509
REMARK 465 PRO V 510
REMARK 465 LYS V 511
REMARK 465 GLY U 495
REMARK 465 SER U 496
REMARK 465 LYS U 511
REMARK 465 ALA U 512
REMARK 465 GLY T 495
REMARK 465 SER T 496
REMARK 465 GLY T 497
REMARK 465 SER T 507
REMARK 465 LEU T 508
REMARK 465 THR T 509
REMARK 465 PRO T 510
REMARK 465 LYS T 511
REMARK 465 GLY S 495
REMARK 465 SER S 496
REMARK 465 GLY S 497
REMARK 465 ILE S 498
REMARK 465 THR S 509
REMARK 465 PRO S 510
REMARK 465 LYS S 511
REMARK 465 GLY R 495
REMARK 465 SER R 496
REMARK 465 THR R 509
REMARK 465 PRO R 510
REMARK 465 LYS R 511
REMARK 465 ALA R 512
REMARK 465 GLY Q 495
REMARK 465 SER Q 496
REMARK 465 GLY Q 497
REMARK 465 ILE Q 498
REMARK 465 THR Q 509
REMARK 465 PRO Q 510
REMARK 465 LYS Q 511
REMARK 465 ALA Q 512
REMARK 465 ILE Q 659
REMARK 465 PRO Q 660
REMARK 465 TYR Q 661
REMARK 465 THR Q 662
REMARK 465 GLY P 495
REMARK 465 SER P 496
REMARK 465 GLY P 497
REMARK 465 ILE P 498
REMARK 465 THR P 509
REMARK 465 PRO P 510
REMARK 465 LYS P 511
REMARK 465 GLY O 495
REMARK 465 SER O 496
REMARK 465 GLY O 497
REMARK 465 ILE O 498
REMARK 465 THR O 509
REMARK 465 PRO O 510
REMARK 465 LYS O 511
REMARK 465 GLY N 495
REMARK 465 SER N 496
REMARK 465 THR N 509
REMARK 465 PRO N 510
REMARK 465 LYS N 511
REMARK 465 GLY M 495
REMARK 465 SER M 496
REMARK 465 GLY M 497
REMARK 465 ILE M 498
REMARK 465 LEU M 508
REMARK 465 THR M 509
REMARK 465 PRO M 510
REMARK 465 LYS M 511
REMARK 465 GLY L 495
REMARK 465 SER L 496
REMARK 465 GLY L 497
REMARK 465 ILE L 498
REMARK 465 ASN L 506
REMARK 465 SER L 507
REMARK 465 LEU L 508
REMARK 465 THR L 509
REMARK 465 PRO L 510
REMARK 465 LYS L 511
REMARK 465 ALA L 512
REMARK 465 GLY K 495
REMARK 465 SER K 496
REMARK 465 GLY K 497
REMARK 465 LEU K 508
REMARK 465 THR K 509
REMARK 465 PRO K 510
REMARK 465 LYS K 511
REMARK 465 ALA K 512
REMARK 465 GLY J 495
REMARK 465 SER J 496
REMARK 465 THR J 509
REMARK 465 PRO J 510
REMARK 465 LYS J 511
REMARK 465 GLY F 495
REMARK 465 SER F 496
REMARK 465 THR F 509
REMARK 465 PRO F 510
REMARK 465 LYS F 511
REMARK 465 ALA F 512
REMARK 465 GLY C 495
REMARK 465 SER C 496
REMARK 465 GLY C 497
REMARK 465 SER C 507
REMARK 465 LEU C 508
REMARK 465 THR C 509
REMARK 465 PRO C 510
REMARK 465 LYS C 511
REMARK 465 ALA C 512
REMARK 465 GLY B 495
REMARK 465 SER B 496
REMARK 465 GLY B 497
REMARK 465 THR B 509
REMARK 465 PRO B 510
REMARK 465 LYS B 511
REMARK 465 ALA B 512
REMARK 465 GLY D 495
REMARK 465 SER D 496
REMARK 465 GLY D 497
REMARK 465 LEU D 508
REMARK 465 THR D 509
REMARK 465 PRO D 510
REMARK 465 LYS D 511
REMARK 465 GLY E 495
REMARK 465 SER E 496
REMARK 465 LEU E 508
REMARK 465 THR E 509
REMARK 465 PRO E 510
REMARK 465 GLY G 495
REMARK 465 SER G 496
REMARK 465 LYS G 511
REMARK 465 ALA G 512
REMARK 465 GLY H 495
REMARK 465 SER H 496
REMARK 465 LEU H 508
REMARK 465 THR H 509
REMARK 465 PRO H 510
REMARK 465 LYS H 511
REMARK 465 ALA H 512
REMARK 465 ASN H 513
REMARK 465 GLY I 495
REMARK 465 SER I 496
REMARK 465 GLY I 497
REMARK 465 THR I 509
REMARK 465 PRO I 510
REMARK 465 LYS I 511
REMARK 465 GLY X 495
REMARK 465 SER X 496
REMARK 465 GLY X 497
REMARK 465 ILE X 498
REMARK 465 LEU X 508
REMARK 465 THR X 509
REMARK 465 PRO X 510
REMARK 465 LYS X 511
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS E 511 CG CD CE NZ
REMARK 470 THR G 509 OG1 CG2
REMARK 470 PRO G 510 CG CD
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 NH2 ARG J 558 CB PRO D 660 1.69
REMARK 500 NE2 GLN Q 571 O ARG Q 637 1.73
REMARK 500 NZ LYS O 555 OE2 GLU O 585 1.86
REMARK 500 OE2 GLU L 500 CE1 HIS L 502 1.88
REMARK 500 NH2 ARG J 558 CG PRO D 660 1.95
REMARK 500 OE2 GLU L 500 ND1 HIS L 502 1.96
REMARK 500 OE2 GLU L 500 NE2 HIS L 502 1.97
REMARK 500 NE2 GLN Q 571 C ARG Q 637 1.97
REMARK 500 NZ LYS S 632 OE1 GLU S 654 1.98
REMARK 500 OD1 ASN P 606 NZ LYS J 643 1.99
REMARK 500 O PHE L 544 NH1 ARG F 514 2.00
REMARK 500 NZ LYS K 632 OE1 GLU K 654 2.00
REMARK 500 NE2 GLN W 530 O VAL W 581 2.02
REMARK 500 NH1 ARG W 533 OD1 ASP W 615 2.03
REMARK 500 NH2 ARG W 533 OH TYR W 617 2.04
REMARK 500 OE2 GLU R 600 CB TYR R 661 2.05
REMARK 500 NZ LYS M 632 OE2 GLU M 654 2.05
REMARK 500 OE2 GLU N 600 OG1 THR N 662 2.06
REMARK 500 O LEU T 639 NH2 ARG X 637 2.06
REMARK 500 O ASP X 556 NH1 ARG X 558 2.07
REMARK 500 O GLN E 524 OG SER E 528 2.09
REMARK 500 NE2 GLN V 530 O VAL V 581 2.10
REMARK 500 O SER J 528 NZ LYS J 536 2.10
REMARK 500 OH TYR M 641 O THR J 570 2.12
REMARK 500 O GLN W 571 NH2 ARG W 637 2.12
REMARK 500 OE2 GLU R 600 CD2 TYR R 661 2.12
REMARK 500 OE2 GLU L 500 CD2 HIS L 502 2.14
REMARK 500 NH1 ARG O 637 O LEU X 639 2.14
REMARK 500 OE2 GLU R 600 N TYR R 661 2.14
REMARK 500 OE2 GLU L 500 CG HIS L 502 2.14
REMARK 500 NH1 ARG L 533 OD1 ASP L 615 2.15
REMARK 500 NE2 GLN T 530 O VAL T 581 2.16
REMARK 500 O VAL V 521 ND2 ASN V 525 2.16
REMARK 500 NH1 ARG V 514 CG LEU V 518 2.17
REMARK 500 OH TYR M 538 OH TYR M 645 2.17
REMARK 500 O ILE W 619 NZ LYS W 623 2.18
REMARK 500 O ASP X 615 N ALA X 618 2.18
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 NZ LYS B 629 OE2 GLU H 646 4554 1.95
REMARK 500 OE2 GLU C 646 NZ LYS G 629 4454 2.00
REMARK 500 OE1 GLU S 646 NZ LYS I 629 8655 2.07
REMARK 500 OH TYR B 617 OD1 ASP H 615 4554 2.07
REMARK 500 NZ LYS U 629 OE2 GLU F 646 5545 2.10
REMARK 500 OE1 GLU B 646 NZ LYS H 629 4554 2.11
REMARK 500 NH2 ARG O 533 OD2 ASP O 615 8665 2.16
REMARK 500 NH2 ARG S 533 OD2 ASP I 615 8655 2.17
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 GLU W 616 CD GLU W 616 OE1 -0.102
REMARK 500 GLU W 616 CD GLU W 616 OE2 -0.091
REMARK 500 ARG S 514 CZ ARG S 514 NH1 0.080
REMARK 500 ARG L 533 C MET L 534 N -0.146
REMARK 500 TYR X 621 CG TYR X 621 CD1 0.084
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 S 514 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG S 515 NH1 - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG S 515 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG S 558 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG S 558 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO G 510 N - CA - CB ANGL. DEV. = 7.6 DEGREES
REMARK 500 LYS X 624 CD - CE - NZ ANGL. DEV. = -16.4 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 A 531 58.83 -143.66
REMARK 500 PHE A 568 74.09 -119.13
REMARK 500 VAL A 587 47.93 35.39
REMARK 500 ASP W 556 -2.10 58.08
REMARK 500 PHE W 568 69.47 -115.26
REMARK 500 GLU W 585 23.69 -78.08
REMARK 500 LYS V 588 12.62 -144.90
REMARK 500 LEU U 531 72.61 -119.60
REMARK 500 PHE U 568 74.44 -116.69
REMARK 500 VAL U 587 48.86 33.36
REMARK 500 LYS U 643 99.96 -69.02
REMARK 500 LYS T 604 2.78 -69.66
REMARK 500 SER T 636 0.06 -66.23
REMARK 500 PHE S 544 56.68 -96.51
REMARK 500 PHE S 568 77.21 -119.90
REMARK 500 VAL S 577 -67.97 -96.10
REMARK 500 PHE R 568 78.03 -115.74
REMARK 500 CYS R 579 106.56 -163.55
REMARK 500 SER Q 507 -71.77 -102.63
REMARK 500 LEU Q 531 73.31 -111.86
REMARK 500 ASP Q 556 -126.17 58.15
REMARK 500 ASN Q 606 -2.07 73.02
REMARK 500 ARG Q 637 -39.69 -131.86
REMARK 500 GLU Q 646 -71.52 -65.10
REMARK 500 PHE P 568 78.04 -111.30
REMARK 500 ASN P 584 2.52 -66.53
REMARK 500 GLU P 585 19.22 -141.38
REMARK 500 VAL P 587 55.02 -90.41
REMARK 500 ASP O 556 -75.22 -130.64
REMARK 500 PHE O 568 73.77 -118.02
REMARK 500 VAL O 577 -62.15 -97.86
REMARK 500 VAL N 577 -65.46 -91.54
REMARK 500 ARG M 533 -62.06 -29.51
REMARK 500 ASP M 556 72.77 51.59
REMARK 500 PHE M 568 72.40 -112.75
REMARK 500 ASN L 584 20.31 -78.38
REMARK 500 SER L 636 9.08 -66.36
REMARK 500 ARG L 658 0.70 -60.08
REMARK 500 PHE K 568 73.68 -117.54
REMARK 500 VAL K 577 -64.08 -97.65
REMARK 500 VAL K 587 52.40 32.79
REMARK 500 ARG J 514 -71.91 -74.76
REMARK 500 LEU J 531 66.23 -110.24
REMARK 500 PRO J 532 34.10 -95.57
REMARK 500 PHE J 568 77.33 -119.55
REMARK 500 TYR J 645 48.56 -153.76
REMARK 500 PHE F 568 73.23 -117.04
REMARK 500 VAL F 577 -60.98 -97.26
REMARK 500 CYS F 579 112.91 -161.55
REMARK 500 PHE C 568 73.88 -110.13
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 HIS Q 605 ASN Q 606 146.96
REMARK 500 TYR L 645 GLU L 646 137.43
REMARK 500 GLU L 646 GLY L 647 149.58
REMARK 500 THR L 649 LEU L 650 144.92
REMARK 500 GLU J 646 GLY J 647 147.65
REMARK 500 GLN X 625 GLY X 626 148.69
REMARK 500 LYS X 632 VAL X 633 135.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TRL RELATED DB: PDB
DBREF 5TRM A 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM W 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM V 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM U 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM T 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM S 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM R 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM Q 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM P 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM O 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM N 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM M 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM L 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM K 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM J 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM F 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM C 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM B 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM D 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM E 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM G 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM H 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM I 497 662 UNP Q92830 KAT2A_HUMAN 497 662
DBREF 5TRM X 497 662 UNP Q92830 KAT2A_HUMAN 497 662
SEQADV 5TRM GLY A 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER A 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY W 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER W 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY V 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER V 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY U 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER U 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY T 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER T 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY S 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER S 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY R 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER R 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY Q 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER Q 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY P 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER P 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY O 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER O 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY N 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER N 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY M 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER M 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY L 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER L 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY K 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER K 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY J 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER J 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY F 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER F 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY C 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER C 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY B 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER B 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY D 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER D 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY E 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER E 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY G 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER G 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY H 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER H 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY I 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER I 496 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM GLY X 495 UNP Q92830 EXPRESSION TAG
SEQADV 5TRM SER X 496 UNP Q92830 EXPRESSION TAG
SEQRES 1 A 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 A 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 A 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 A 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 A 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 A 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 A 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 A 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 A 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 A 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 A 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 A 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 A 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 W 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 W 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 W 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 W 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 W 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 W 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 W 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 W 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 W 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 W 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 W 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 W 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 W 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 V 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 V 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 V 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 V 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 V 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 V 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 V 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 V 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 V 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 V 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 V 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 V 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 V 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 U 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 U 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 U 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 U 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 U 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 U 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 U 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 U 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 U 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 U 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 U 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 U 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 U 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 T 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 T 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 T 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 T 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 T 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 T 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 T 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 T 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 T 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 T 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 T 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 T 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 T 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 S 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 S 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 S 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 S 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 S 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 S 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 S 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 S 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 S 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 S 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 S 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 S 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 S 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 R 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 R 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 R 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 R 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 R 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 R 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 R 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 R 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 R 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 R 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 R 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 R 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 R 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 Q 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 Q 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 Q 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 Q 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 Q 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 Q 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 Q 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 Q 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 Q 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 Q 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 Q 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 Q 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 Q 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 P 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 P 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 P 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 P 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 P 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 P 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 P 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 P 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 P 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 P 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 P 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 P 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 P 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 O 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 O 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 O 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 O 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 O 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 O 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 O 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 O 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 O 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 O 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 O 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 O 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 O 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 N 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 N 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 N 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 N 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 N 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 N 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 N 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 N 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 N 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 N 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 N 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 N 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 N 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 M 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 M 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 M 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 M 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 M 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 M 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 M 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 M 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 M 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 M 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 M 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 M 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 M 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 L 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 L 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 L 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 L 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 L 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 L 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 L 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 L 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 L 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 L 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 L 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 L 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 L 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 K 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 K 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 K 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 K 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 K 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 K 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 K 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 K 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 K 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 K 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 K 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 K 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 K 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 J 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 J 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 J 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 J 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 J 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 J 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 J 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 J 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 J 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 J 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 J 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 J 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 J 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 F 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 F 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 F 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 F 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 F 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 F 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 F 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 F 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 F 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 F 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 F 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 F 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 F 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 C 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 C 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 C 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 C 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 C 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 C 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 C 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 C 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 C 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 C 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 C 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 C 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 C 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 B 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 B 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 B 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 B 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 B 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 B 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 B 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 B 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 B 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 B 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 B 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 B 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 B 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 D 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 D 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 D 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 D 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 D 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 D 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 D 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 D 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 D 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 D 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 D 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 D 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 D 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 E 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 E 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 E 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 E 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 E 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 E 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 E 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 E 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 E 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 E 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 E 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 E 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 E 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 G 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 G 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 G 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 G 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 G 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 G 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 G 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 G 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 G 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 G 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 G 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 G 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 G 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 H 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 H 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 H 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 H 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 H 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 H 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 H 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 H 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 H 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 H 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 H 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 H 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 H 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 I 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 I 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 I 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 I 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 I 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 I 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 I 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 I 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 I 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 I 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 I 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 I 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 I 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
SEQRES 1 X 168 GLY SER GLY ILE ILE GLU PHE HIS VAL ILE GLY ASN SER
SEQRES 2 X 168 LEU THR PRO LYS ALA ASN ARG ARG VAL LEU LEU TRP LEU
SEQRES 3 X 168 VAL GLY LEU GLN ASN VAL PHE SER HIS GLN LEU PRO ARG
SEQRES 4 X 168 MET PRO LYS GLU TYR ILE ALA ARG LEU VAL PHE ASP PRO
SEQRES 5 X 168 LYS HIS LYS THR LEU ALA LEU ILE LYS ASP GLY ARG VAL
SEQRES 6 X 168 ILE GLY GLY ILE CYS PHE ARG MET PHE PRO THR GLN GLY
SEQRES 7 X 168 PHE THR GLU ILE VAL PHE CYS ALA VAL THR SER ASN GLU
SEQRES 8 X 168 GLN VAL LYS GLY TYR GLY THR HIS LEU MET ASN HIS LEU
SEQRES 9 X 168 LYS GLU TYR HIS ILE LYS HIS ASN ILE LEU TYR PHE LEU
SEQRES 10 X 168 THR TYR ALA ASP GLU TYR ALA ILE GLY TYR PHE LYS LYS
SEQRES 11 X 168 GLN GLY PHE SER LYS ASP ILE LYS VAL PRO LYS SER ARG
SEQRES 12 X 168 TYR LEU GLY TYR ILE LYS ASP TYR GLU GLY ALA THR LEU
SEQRES 13 X 168 MET GLU CYS GLU LEU ASN PRO ARG ILE PRO TYR THR
HELIX 1 AA1 ASN A 513 LEU A 531 1 19
HELIX 2 AA2 PRO A 535 PHE A 544 1 10
HELIX 3 AA3 SER A 583 GLN A 586 5 4
HELIX 4 AA4 GLY A 589 LYS A 604 1 16
HELIX 5 AA5 ALA A 618 GLN A 625 1 8
HELIX 6 AA6 PRO A 634 LEU A 639 1 6
HELIX 7 AA7 ARG W 514 LEU W 531 1 18
HELIX 8 AA8 PRO W 535 PHE W 544 1 10
HELIX 9 AA9 GLY W 589 LYS W 604 1 16
HELIX 10 AB1 ILE W 619 GLN W 625 1 7
HELIX 11 AB2 PRO W 634 LEU W 639 1 6
HELIX 12 AB3 ASN V 513 GLN V 530 1 18
HELIX 13 AB4 PRO V 535 PHE V 544 1 10
HELIX 14 AB5 GLY V 589 HIS V 605 1 17
HELIX 15 AB6 ALA V 618 GLN V 625 1 8
HELIX 16 AB7 PRO V 634 LEU V 639 1 6
HELIX 17 AB8 ARG U 514 LEU U 531 1 18
HELIX 18 AB9 PRO U 535 PHE U 544 1 10
HELIX 19 AC1 SER U 583 GLN U 586 5 4
HELIX 20 AC2 GLY U 589 HIS U 605 1 17
HELIX 21 AC3 ASP U 615 GLN U 625 1 11
HELIX 22 AC4 PRO U 634 LEU U 639 1 6
HELIX 23 AC5 ASN T 513 LEU T 531 1 19
HELIX 24 AC6 PRO T 535 PHE T 544 1 10
HELIX 25 AC7 SER T 583 GLN T 586 5 4
HELIX 26 AC8 GLY T 589 LYS T 604 1 16
HELIX 27 AC9 ASP T 615 GLN T 625 1 11
HELIX 28 AD1 PRO T 634 LEU T 639 1 6
HELIX 29 AD2 ASN S 513 LEU S 531 1 19
HELIX 30 AD3 PRO S 535 PHE S 544 1 10
HELIX 31 AD4 SER S 583 GLN S 586 5 4
HELIX 32 AD5 GLY S 589 LYS S 604 1 16
HELIX 33 AD6 ALA S 618 GLN S 625 1 8
HELIX 34 AD7 PRO S 634 LEU S 639 1 6
HELIX 35 AD8 ARG R 514 LEU R 531 1 18
HELIX 36 AD9 PRO R 535 PHE R 544 1 10
HELIX 37 AE1 SER R 583 GLN R 586 5 4
HELIX 38 AE2 GLY R 589 LYS R 604 1 16
HELIX 39 AE3 ASP R 615 GLN R 625 1 11
HELIX 40 AE4 PRO R 634 LEU R 639 1 6
HELIX 41 AE5 ARG Q 514 LEU Q 531 1 18
HELIX 42 AE6 PRO Q 535 PHE Q 544 1 10
HELIX 43 AE7 PRO Q 569 GLY Q 572 5 4
HELIX 44 AE8 SER Q 583 GLN Q 586 5 4
HELIX 45 AE9 GLY Q 589 LYS Q 604 1 16
HELIX 46 AF1 ALA Q 618 GLN Q 625 1 8
HELIX 47 AF2 PRO Q 634 LEU Q 639 1 6
HELIX 48 AF3 ASN P 513 LEU P 531 1 19
HELIX 49 AF4 PRO P 535 PHE P 544 1 10
HELIX 50 AF5 SER P 583 LYS P 588 5 6
HELIX 51 AF6 GLY P 589 LYS P 604 1 16
HELIX 52 AF7 ALA P 618 GLN P 625 1 8
HELIX 53 AF8 PRO P 634 LEU P 639 1 6
HELIX 54 AF9 ASN O 513 LEU O 531 1 19
HELIX 55 AG1 PRO O 535 ASP O 545 1 11
HELIX 56 AG2 GLY O 589 LYS O 604 1 16
HELIX 57 AG3 ALA O 618 GLN O 625 1 8
HELIX 58 AG4 PRO O 634 LEU O 639 1 6
HELIX 59 AG5 ASN N 513 LEU N 531 1 19
HELIX 60 AG6 PRO N 535 PHE N 544 1 10
HELIX 61 AG7 SER N 583 GLN N 586 5 4
HELIX 62 AG8 GLY N 589 LYS N 604 1 16
HELIX 63 AG9 ALA N 618 GLN N 625 1 8
HELIX 64 AH1 PRO N 634 LEU N 639 1 6
HELIX 65 AH2 ASN M 513 LEU M 531 1 19
HELIX 66 AH3 PRO M 535 PHE M 544 1 10
HELIX 67 AH4 SER M 583 GLN M 586 5 4
HELIX 68 AH5 GLY M 589 LYS M 604 1 16
HELIX 69 AH6 ASP M 615 GLN M 625 1 11
HELIX 70 AH7 PRO M 634 LEU M 639 1 6
HELIX 71 AH8 ARG L 514 LEU L 531 1 18
HELIX 72 AH9 PRO L 535 ASP L 545 1 11
HELIX 73 AI1 SER L 583 LYS L 588 5 6
HELIX 74 AI2 GLY L 589 HIS L 605 1 17
HELIX 75 AI3 ASP L 615 GLN L 625 1 11
HELIX 76 AI4 PRO L 634 LEU L 639 1 6
HELIX 77 AI5 ARG K 514 LEU K 531 1 18
HELIX 78 AI6 PRO K 535 PHE K 544 1 10
HELIX 79 AI7 SER K 583 GLN K 586 5 4
HELIX 80 AI8 GLY K 589 LYS K 604 1 16
HELIX 81 AI9 ALA K 618 GLN K 625 1 8
HELIX 82 AJ1 PRO K 634 LEU K 639 1 6
HELIX 83 AJ2 ARG J 514 LEU J 531 1 18
HELIX 84 AJ3 PRO J 535 PHE J 544 1 10
HELIX 85 AJ4 GLY J 589 HIS J 605 1 17
HELIX 86 AJ5 ALA J 618 GLN J 625 1 8
HELIX 87 AJ6 PRO J 634 LEU J 639 1 6
HELIX 88 AJ7 ARG F 514 LEU F 531 1 18
HELIX 89 AJ8 PRO F 535 PHE F 544 1 10
HELIX 90 AJ9 GLY F 589 LYS F 604 1 16
HELIX 91 AK1 ALA F 618 GLN F 625 1 8
HELIX 92 AK2 PRO F 634 TYR F 638 5 5
HELIX 93 AK3 ARG C 514 GLN C 530 1 17
HELIX 94 AK4 PRO C 535 PHE C 544 1 10
HELIX 95 AK5 SER C 583 GLN C 586 5 4
HELIX 96 AK6 GLY C 589 LYS C 604 1 16
HELIX 97 AK7 ASP C 615 GLN C 625 1 11
HELIX 98 AK8 PRO C 634 LEU C 639 1 6
HELIX 99 AK9 ARG B 514 LEU B 531 1 18
HELIX 100 AL1 PRO B 535 PHE B 544 1 10
HELIX 101 AL2 SER B 583 GLN B 586 5 4
HELIX 102 AL3 GLY B 589 LYS B 604 1 16
HELIX 103 AL4 ALA B 618 GLN B 625 1 8
HELIX 104 AL5 PRO B 634 LEU B 639 1 6
HELIX 105 AL6 ARG D 514 LEU D 531 1 18
HELIX 106 AL7 PRO D 535 PHE D 544 1 10
HELIX 107 AL8 SER D 583 GLN D 586 5 4
HELIX 108 AL9 GLY D 589 LYS D 604 1 16
HELIX 109 AM1 ALA D 618 GLN D 625 1 8
HELIX 110 AM2 PRO D 634 LEU D 639 1 6
HELIX 111 AM3 ASN E 513 LEU E 531 1 19
HELIX 112 AM4 PRO E 535 PHE E 544 1 10
HELIX 113 AM5 SER E 583 GLN E 586 5 4
HELIX 114 AM6 GLY E 589 LYS E 604 1 16
HELIX 115 AM7 ASP E 615 GLN E 625 1 11
HELIX 116 AM8 PRO E 634 LEU E 639 1 6
HELIX 117 AM9 ARG G 514 GLN G 530 1 17
HELIX 118 AN1 PRO G 535 PHE G 544 1 10
HELIX 119 AN2 SER G 583 GLN G 586 5 4
HELIX 120 AN3 GLY G 589 HIS G 605 1 17
HELIX 121 AN4 ALA G 618 GLN G 625 1 8
HELIX 122 AN5 PRO G 634 LEU G 639 1 6
HELIX 123 AN6 ARG H 515 LEU H 531 1 17
HELIX 124 AN7 PRO H 535 PHE H 544 1 10
HELIX 125 AN8 SER H 583 GLN H 586 5 4
HELIX 126 AN9 GLY H 589 HIS H 605 1 17
HELIX 127 AO1 ASP H 615 TYR H 617 5 3
HELIX 128 AO2 ALA H 618 GLN H 625 1 8
HELIX 129 AO3 PRO H 634 LEU H 639 1 6
HELIX 130 AO4 ASN I 513 LEU I 531 1 19
HELIX 131 AO5 PRO I 535 PHE I 544 1 10
HELIX 132 AO6 SER I 583 GLN I 586 5 4
HELIX 133 AO7 GLY I 589 LYS I 604 1 16
HELIX 134 AO8 ALA I 618 GLN I 625 1 8
HELIX 135 AO9 PRO I 634 LEU I 639 1 6
HELIX 136 AP1 ASN X 513 LEU X 531 1 19
HELIX 137 AP2 PRO X 535 PHE X 544 1 10
HELIX 138 AP3 TYR X 590 HIS X 605 1 16
HELIX 139 AP4 ALA X 618 LYS X 623 1 6
HELIX 140 AP5 LYS X 624 GLY X 626 5 3
HELIX 141 AP6 PRO X 634 TYR X 638 5 5
SHEET 1 AA1 6 ILE A 499 ILE A 504 0
SHEET 2 AA1 6 LYS A 549 LYS A 555 -1 O ALA A 552 N HIS A 502
SHEET 3 AA1 6 ARG A 558 PHE A 568 -1 O ILE A 560 N LEU A 553
SHEET 4 AA1 6 PHE A 573 VAL A 581 -1 O VAL A 577 N CYS A 564
SHEET 5 AA1 6 TYR A 609 ALA A 614 1 O LEU A 611 N ILE A 576
SHEET 6 AA1 6 THR A 649 GLU A 654 -1 O MET A 651 N THR A 612
SHEET 1 AA2 6 GLU W 500 GLY W 505 0
SHEET 2 AA2 6 HIS W 548 LYS W 555 -1 O THR W 550 N ILE W 504
SHEET 3 AA2 6 ARG W 558 PHE W 568 -1 O ARG W 558 N LYS W 555
SHEET 4 AA2 6 PHE W 573 VAL W 581 -1 O GLU W 575 N ARG W 566
SHEET 5 AA2 6 TYR W 609 ALA W 614 1 O LEU W 611 N ILE W 576
SHEET 6 AA2 6 THR W 649 GLU W 654 -1 O MET W 651 N THR W 612
SHEET 1 AA3 6 GLU V 500 ILE V 504 0
SHEET 2 AA3 6 HIS V 548 LYS V 555 -1 O ALA V 552 N HIS V 502
SHEET 3 AA3 6 ARG V 558 PHE V 568 -1 O GLY V 561 N LEU V 553
SHEET 4 AA3 6 PHE V 573 VAL V 581 -1 O GLU V 575 N ARG V 566
SHEET 5 AA3 6 TYR V 609 ALA V 614 1 O LEU V 611 N ILE V 576
SHEET 6 AA3 6 THR V 649 GLU V 654 -1 O MET V 651 N THR V 612
SHEET 1 AA4 6 ILE U 499 ILE U 504 0
SHEET 2 AA4 6 LYS U 549 LYS U 555 -1 O ILE U 554 N GLU U 500
SHEET 3 AA4 6 ARG U 558 PHE U 568 -1 O GLY U 561 N LEU U 553
SHEET 4 AA4 6 PHE U 573 VAL U 581 -1 O VAL U 577 N CYS U 564
SHEET 5 AA4 6 TYR U 609 ALA U 614 1 O LEU U 611 N THR U 574
SHEET 6 AA4 6 THR U 649 GLU U 654 -1 O CYS U 653 N PHE U 610
SHEET 1 AA5 6 ILE T 499 GLY T 505 0
SHEET 2 AA5 6 LYS T 549 LYS T 555 -1 O ALA T 552 N HIS T 502
SHEET 3 AA5 6 ARG T 558 MET T 567 -1 O ILE T 560 N LEU T 553
SHEET 4 AA5 6 THR T 574 VAL T 581 -1 O GLU T 575 N ARG T 566
SHEET 5 AA5 6 TYR T 609 ALA T 614 1 O LEU T 611 N THR T 574
SHEET 6 AA5 6 THR T 649 GLU T 654 -1 O MET T 651 N THR T 612
SHEET 1 AA6 6 GLU S 500 ILE S 504 0
SHEET 2 AA6 6 LYS S 549 ILE S 554 -1 O ALA S 552 N HIS S 502
SHEET 3 AA6 6 GLY S 561 PHE S 568 -1 O PHE S 565 N LYS S 549
SHEET 4 AA6 6 PHE S 573 VAL S 581 -1 O PHE S 578 N CYS S 564
SHEET 5 AA6 6 TYR S 609 ALA S 614 1 O LEU S 611 N ILE S 576
SHEET 6 AA6 6 THR S 649 GLU S 654 -1 O MET S 651 N THR S 612
SHEET 1 AA7 6 ILE R 499 ILE R 504 0
SHEET 2 AA7 6 LYS R 549 LYS R 555 -1 O ALA R 552 N HIS R 502
SHEET 3 AA7 6 ARG R 558 PHE R 568 -1 O GLY R 561 N LEU R 553
SHEET 4 AA7 6 PHE R 573 VAL R 581 -1 O VAL R 577 N CYS R 564
SHEET 5 AA7 6 TYR R 609 ALA R 614 1 O LEU R 611 N THR R 574
SHEET 6 AA7 6 THR R 649 GLU R 654 -1 O MET R 651 N THR R 612
SHEET 1 AA8 6 GLU Q 500 ILE Q 504 0
SHEET 2 AA8 6 LYS Q 549 LYS Q 555 -1 O ALA Q 552 N HIS Q 502
SHEET 3 AA8 6 ARG Q 558 PHE Q 568 -1 O PHE Q 565 N LYS Q 549
SHEET 4 AA8 6 PHE Q 573 VAL Q 581 -1 O GLU Q 575 N ARG Q 566
SHEET 5 AA8 6 TYR Q 609 ALA Q 614 1 O LEU Q 611 N ILE Q 576
SHEET 6 AA8 6 THR Q 649 GLU Q 654 -1 O THR Q 649 N ALA Q 614
SHEET 1 AA9 6 GLU P 500 ILE P 504 0
SHEET 2 AA9 6 LYS P 549 LYS P 555 -1 O ALA P 552 N HIS P 502
SHEET 3 AA9 6 ARG P 558 PHE P 568 -1 O PHE P 565 N LYS P 549
SHEET 4 AA9 6 PHE P 573 VAL P 581 -1 O VAL P 577 N CYS P 564
SHEET 5 AA9 6 TYR P 609 ASP P 615 1 O LEU P 611 N ILE P 576
SHEET 6 AA9 6 ALA P 648 GLU P 654 -1 O CYS P 653 N PHE P 610
SHEET 1 AB1 6 GLU O 500 ILE O 504 0
SHEET 2 AB1 6 HIS O 548 ILE O 554 -1 O ALA O 552 N HIS O 502
SHEET 3 AB1 6 VAL O 559 PHE O 568 -1 O GLY O 561 N LEU O 553
SHEET 4 AB1 6 PHE O 573 VAL O 581 -1 O GLU O 575 N ARG O 566
SHEET 5 AB1 6 TYR O 609 ALA O 614 1 O LEU O 611 N THR O 574
SHEET 6 AB1 6 THR O 649 GLU O 654 -1 O MET O 651 N THR O 612
SHEET 1 AB2 6 ILE N 499 ILE N 504 0
SHEET 2 AB2 6 HIS N 548 LYS N 555 -1 O ALA N 552 N HIS N 502
SHEET 3 AB2 6 ARG N 558 PHE N 568 -1 O GLY N 561 N LEU N 553
SHEET 4 AB2 6 PHE N 573 VAL N 581 -1 O VAL N 577 N CYS N 564
SHEET 5 AB2 6 TYR N 609 ALA N 614 1 O LEU N 611 N THR N 574
SHEET 6 AB2 6 THR N 649 GLU N 654 -1 O MET N 651 N THR N 612
SHEET 1 AB3 6 GLU M 500 ILE M 504 0
SHEET 2 AB3 6 LYS M 549 ILE M 554 -1 O ALA M 552 N HIS M 502
SHEET 3 AB3 6 VAL M 559 MET M 567 -1 O ILE M 560 N LEU M 553
SHEET 4 AB3 6 THR M 574 VAL M 581 -1 O VAL M 577 N CYS M 564
SHEET 5 AB3 6 TYR M 609 ALA M 614 1 O LEU M 611 N ILE M 576
SHEET 6 AB3 6 THR M 649 GLU M 654 -1 O MET M 651 N THR M 612
SHEET 1 AB4 6 GLU L 500 ILE L 504 0
SHEET 2 AB4 6 LYS L 549 LYS L 555 -1 O ILE L 554 N GLU L 500
SHEET 3 AB4 6 ARG L 558 MET L 567 -1 O PHE L 565 N LYS L 549
SHEET 4 AB4 6 PHE L 573 VAL L 581 -1 O VAL L 577 N CYS L 564
SHEET 5 AB4 6 TYR L 609 ALA L 614 1 O LEU L 611 N ILE L 576
SHEET 6 AB4 6 THR L 649 GLU L 654 -1 O CYS L 653 N PHE L 610
SHEET 1 AB5 6 ILE K 499 ILE K 504 0
SHEET 2 AB5 6 LYS K 549 LYS K 555 -1 O ALA K 552 N HIS K 502
SHEET 3 AB5 6 ARG K 558 PHE K 568 -1 O GLY K 561 N LEU K 553
SHEET 4 AB5 6 PHE K 573 VAL K 581 -1 O GLU K 575 N ARG K 566
SHEET 5 AB5 6 TYR K 609 ALA K 614 1 O LEU K 611 N ILE K 576
SHEET 6 AB5 6 THR K 649 GLU K 654 -1 O MET K 651 N THR K 612
SHEET 1 AB6 6 ILE J 499 ILE J 504 0
SHEET 2 AB6 6 HIS J 548 LYS J 555 -1 O ILE J 554 N GLU J 500
SHEET 3 AB6 6 ARG J 558 PHE J 568 -1 O GLY J 561 N LEU J 553
SHEET 4 AB6 6 PHE J 573 VAL J 581 -1 O ALA J 580 N GLY J 562
SHEET 5 AB6 6 TYR J 609 ALA J 614 1 O LEU J 611 N THR J 574
SHEET 6 AB6 6 THR J 649 GLU J 654 -1 O THR J 649 N ALA J 614
SHEET 1 AB7 6 ILE F 499 GLY F 505 0
SHEET 2 AB7 6 LYS F 549 LYS F 555 -1 O ALA F 552 N HIS F 502
SHEET 3 AB7 6 ARG F 558 PHE F 568 -1 O PHE F 565 N LYS F 549
SHEET 4 AB7 6 PHE F 573 VAL F 581 -1 O VAL F 577 N CYS F 564
SHEET 5 AB7 6 TYR F 609 ALA F 614 1 O LEU F 611 N THR F 574
SHEET 6 AB7 6 THR F 649 GLU F 654 -1 O MET F 651 N THR F 612
SHEET 1 AB8 6 ILE C 499 ILE C 504 0
SHEET 2 AB8 6 HIS C 548 LYS C 555 -1 O ALA C 552 N HIS C 502
SHEET 3 AB8 6 ARG C 558 MET C 567 -1 O GLY C 561 N LEU C 553
SHEET 4 AB8 6 PHE C 573 VAL C 581 -1 O VAL C 577 N CYS C 564
SHEET 5 AB8 6 TYR C 609 ALA C 614 1 O LEU C 611 N ILE C 576
SHEET 6 AB8 6 THR C 649 GLU C 654 -1 O MET C 651 N THR C 612
SHEET 1 AB9 6 ILE B 499 GLY B 505 0
SHEET 2 AB9 6 LYS B 549 LYS B 555 -1 O ALA B 552 N HIS B 502
SHEET 3 AB9 6 ARG B 558 PHE B 568 -1 O PHE B 565 N LYS B 549
SHEET 4 AB9 6 PHE B 573 VAL B 581 -1 O VAL B 577 N CYS B 564
SHEET 5 AB9 6 TYR B 609 ALA B 614 1 O LEU B 611 N THR B 574
SHEET 6 AB9 6 THR B 649 GLU B 654 -1 O THR B 649 N ALA B 614
SHEET 1 AC1 6 GLU D 500 ILE D 504 0
SHEET 2 AC1 6 LYS D 549 LYS D 555 -1 O ILE D 554 N GLU D 500
SHEET 3 AC1 6 ARG D 558 PHE D 568 -1 O GLY D 561 N LEU D 553
SHEET 4 AC1 6 PHE D 573 VAL D 581 -1 O GLU D 575 N ARG D 566
SHEET 5 AC1 6 TYR D 609 ALA D 614 1 O LEU D 611 N THR D 574
SHEET 6 AC1 6 THR D 649 GLU D 654 -1 O CYS D 653 N PHE D 610
SHEET 1 AC2 6 ILE E 499 GLY E 505 0
SHEET 2 AC2 6 LYS E 549 LYS E 555 -1 O ALA E 552 N HIS E 502
SHEET 3 AC2 6 ARG E 558 PHE E 568 -1 O ARG E 558 N LYS E 555
SHEET 4 AC2 6 PHE E 573 VAL E 581 -1 O PHE E 578 N CYS E 564
SHEET 5 AC2 6 TYR E 609 ALA E 614 1 O LEU E 611 N THR E 574
SHEET 6 AC2 6 THR E 649 GLU E 654 -1 O MET E 651 N THR E 612
SHEET 1 AC3 6 ILE G 499 ILE G 504 0
SHEET 2 AC3 6 LYS G 549 LYS G 555 -1 O THR G 550 N ILE G 504
SHEET 3 AC3 6 ARG G 558 MET G 567 -1 O GLY G 561 N LEU G 553
SHEET 4 AC3 6 THR G 574 VAL G 581 -1 O VAL G 577 N CYS G 564
SHEET 5 AC3 6 TYR G 609 ALA G 614 1 O LEU G 611 N THR G 574
SHEET 6 AC3 6 THR G 649 GLU G 654 -1 O MET G 651 N THR G 612
SHEET 1 AC4 6 ILE H 499 ILE H 504 0
SHEET 2 AC4 6 LYS H 549 LYS H 555 -1 O ALA H 552 N HIS H 502
SHEET 3 AC4 6 ARG H 558 MET H 567 -1 O GLY H 561 N LEU H 553
SHEET 4 AC4 6 THR H 574 VAL H 581 -1 O VAL H 577 N CYS H 564
SHEET 5 AC4 6 TYR H 609 ALA H 614 1 O LEU H 611 N ILE H 576
SHEET 6 AC4 6 THR H 649 GLU H 654 -1 O MET H 651 N THR H 612
SHEET 1 AC5 6 ILE I 499 ILE I 504 0
SHEET 2 AC5 6 HIS I 548 LYS I 555 -1 O ALA I 552 N HIS I 502
SHEET 3 AC5 6 ARG I 558 MET I 567 -1 O GLY I 561 N LEU I 553
SHEET 4 AC5 6 THR I 574 VAL I 581 -1 O VAL I 577 N CYS I 564
SHEET 5 AC5 6 TYR I 609 ALA I 614 1 O LEU I 611 N ILE I 576
SHEET 6 AC5 6 THR I 649 GLU I 654 -1 O MET I 651 N THR I 612
SHEET 1 AC6 6 GLU X 500 ILE X 504 0
SHEET 2 AC6 6 HIS X 548 LYS X 555 -1 O THR X 550 N ILE X 504
SHEET 3 AC6 6 ARG X 558 PHE X 568 -1 O GLY X 561 N LEU X 553
SHEET 4 AC6 6 PHE X 573 VAL X 581 -1 O VAL X 577 N CYS X 564
SHEET 5 AC6 6 TYR X 609 ALA X 614 1 O TYR X 609 N THR X 574
SHEET 6 AC6 6 THR X 649 GLU X 654 -1 O MET X 651 N THR X 612
LINK NE ARG T 533 NH1 ARG M 533 1555 8655 1.51
CRYST1 173.474 173.474 347.637 90.00 90.00 90.00 P 41 21 2 192
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 0.005765 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005765 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002877 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
