HEADER LIGASE/RNA 28-OCT-09 3KFU
TITLE CRYSTAL STRUCTURE OF THE TRANSAMIDOSOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-DISCRIMINATING AND ARCHAEAL-TYPE ASPARTYL-TRNA
COMPND 3 SYNTHETASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A;
COMPND 8 CHAIN: E, H;
COMPND 9 SYNONYM: GLU-ADT SUBUNIT A;
COMPND 10 EC: 6.3.5.-;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: ASPARTYL/GLUTAMYL-TRNA(ASN/GLN) AMIDOTRANSFERASE SUBUNIT B;
COMPND 14 CHAIN: F, I;
COMPND 15 SYNONYM: ASP/GLU-ADT SUBUNIT B;
COMPND 16 EC: 6.3.5.-;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C;
COMPND 20 CHAIN: G, J;
COMPND 21 SYNONYM: GLU-ADT SUBUNIT C;
COMPND 22 EC: 6.3.5.-;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: TRNA-ASN;
COMPND 26 CHAIN: K, L, M, N;
COMPND 27 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: TTHA1452;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 10 ORGANISM_TAXID: 300852;
SOURCE 11 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 12 GENE: GATA, TTHA0573;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 17 ORGANISM_TAXID: 300852;
SOURCE 18 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 19 GENE: GATB, TTHA0366;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 24 ORGANISM_TAXID: 300852;
SOURCE 25 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 26 GENE: GATC, TTHA0876;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 29 MOL_ID: 5;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 31 ORGANISM_TAXID: 300852;
SOURCE 32 STRAIN: HB8;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ASPRS, GATCAB, ATP-BINDING, AMINOACYL-TRNA SYNTHETASE, LIGASE,
KEYWDS 2 NUCLEOTIDE-BINDING, PROTEIN BIOSYNTHESIS, LIGASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BLAISE,M.BAILLY,M.FRECHIN,S.THIRUP,H.D.BECKER,D.KERN
REVDAT 3 06-SEP-23 3KFU 1 REMARK SEQADV LINK
REVDAT 2 29-SEP-10 3KFU 1 JRNL
REVDAT 1 25-AUG-10 3KFU 0
JRNL AUTH M.BLAISE,M.BAILLY,M.FRECHIN,M.A.BEHRENS,F.FISCHER,
JRNL AUTH 2 C.L.OLIVEIRA,H.D.BECKER,J.S.PEDERSEN,S.THIRUP,D.KERN
JRNL TITL CRYSTAL STRUCTURE OF A TRANSFER-RIBONUCLEOPROTEIN PARTICLE
JRNL TITL 2 THAT PROMOTES ASPARAGINE FORMATION.
JRNL REF EMBO J. V. 29 3118 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 20717102
JRNL DOI 10.1038/EMBOJ.2010.192
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 123923
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2487
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 39.1928 - 7.8424 0.99 6804 146 0.1985 0.2282
REMARK 3 2 7.8424 - 6.2328 1.00 6780 154 0.1865 0.2337
REMARK 3 3 6.2328 - 5.4473 1.00 6746 155 0.1932 0.2389
REMARK 3 4 5.4473 - 4.9503 1.00 6756 138 0.1786 0.2659
REMARK 3 5 4.9503 - 4.5961 1.00 6765 123 0.1611 0.1794
REMARK 3 6 4.5961 - 4.3255 1.00 6787 120 0.1565 0.1933
REMARK 3 7 4.3255 - 4.1091 1.00 6712 128 0.1628 0.2117
REMARK 3 8 4.1091 - 3.9304 1.00 6774 135 0.1758 0.2286
REMARK 3 9 3.9304 - 3.7792 1.00 6738 134 0.1796 0.2753
REMARK 3 10 3.7792 - 3.6489 1.00 6738 122 0.1987 0.2885
REMARK 3 11 3.6489 - 3.5349 1.00 6749 149 0.2020 0.2604
REMARK 3 12 3.5349 - 3.4339 1.00 6677 155 0.2128 0.2876
REMARK 3 13 3.4339 - 3.3435 1.00 6750 141 0.2279 0.2983
REMARK 3 14 3.3435 - 3.2620 1.00 6745 141 0.2348 0.3292
REMARK 3 15 3.2620 - 3.1879 1.00 6713 131 0.2463 0.2628
REMARK 3 16 3.1879 - 3.1201 1.00 6688 140 0.2872 0.3204
REMARK 3 17 3.1201 - 3.0577 1.00 6750 132 0.3180 0.3900
REMARK 3 18 3.0577 - 3.0000 1.00 6764 143 0.3467 0.3642
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 : 0.31
REMARK 3 B_SOL : 52.37
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.600
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) : 2.47040
REMARK 3 B22 (A**2) : 1.47410
REMARK 3 B33 (A**2) : -3.94450
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.51130
REMARK 3 B23 (A**2) : 0.00000
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 : 0.007 34742
REMARK 3 ANGLE : 0.734 48537
REMARK 3 CHIRALITY : 0.062 5625
REMARK 3 PLANARITY : 0.004 5250
REMARK 3 DIHEDRAL : 15.793 14024
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 : 7
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN H AND (RESSEQ 2:393 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 2:393 )
REMARK 3 ATOM PAIRS NUMBER : 2945
REMARK 3 RMSD : 0.057
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:150 OR RESSEQ
REMARK 3 180:200 OR RESSEQ 211:415 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 1:150 OR RESSEQ
REMARK 3 180:200 OR RESSEQ 211:415 )
REMARK 3 ATOM PAIRS NUMBER : 3003
REMARK 3 RMSD : 0.017
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:150 OR RESSEQ
REMARK 3 180:200 OR RESSEQ 211:415 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 1:150 OR RESSEQ
REMARK 3 180:200 OR RESSEQ 211:415 )
REMARK 3 ATOM PAIRS NUMBER : 3019
REMARK 3 RMSD : 0.026
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN J AND (RESSEQ 3:47 OR RESSEQ 51:88
REMARK 3 )
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 3:47 OR RESSEQ 51:88
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 662
REMARK 3 RMSD : 0.036
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN I AND (RESSEQ 2:194 OR RESSEQ
REMARK 3 200:253 OR RESSEQ 260:391 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 2:194 OR RESSEQ
REMARK 3 200:253 OR RESSEQ 260:391 )
REMARK 3 ATOM PAIRS NUMBER : 3000
REMARK 3 RMSD : 0.030
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN K
REMARK 3 SELECTION : CHAIN L
REMARK 3 ATOM PAIRS NUMBER : 1579
REMARK 3 RMSD : 0.012
REMARK 3 NCS GROUP : 7
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN N
REMARK 3 SELECTION : CHAIN M
REMARK 3 ATOM PAIRS NUMBER : 1525
REMARK 3 RMSD : 0.082
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000055939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9807
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123945
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <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: NULL
REMARK 200 STARTING MODEL: 1N9W AND 2F2A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 10% PEG4000 0.2 M
REMARK 280 MGCL2, VAPOR DIFFUSION, SITTING 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 107.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 59360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 172900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -357.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N
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 LYS A 151
REMARK 465 VAL A 152
REMARK 465 VAL A 153
REMARK 465 ARG A 154
REMARK 465 ALA A 155
REMARK 465 GLY A 156
REMARK 465 ALA A 157
REMARK 465 GLU A 158
REMARK 465 GLY A 159
REMARK 465 GLY A 160
REMARK 465 SER A 161
REMARK 465 GLY A 162
REMARK 465 LEU A 163
REMARK 465 PHE A 164
REMARK 465 GLY A 165
REMARK 465 VAL A 166
REMARK 465 ASP A 167
REMARK 465 TYR A 168
REMARK 465 PHE A 169
REMARK 465 GLU A 170
REMARK 465 LYS A 171
REMARK 465 ARG A 172
REMARK 465 ALA A 173
REMARK 465 TYR A 174
REMARK 465 LEU A 175
REMARK 465 ALA A 176
REMARK 465 GLN A 177
REMARK 465 SER A 178
REMARK 465 ARG A 201
REMARK 465 MET A 202
REMARK 465 GLU A 203
REMARK 465 GLU A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 THR A 207
REMARK 465 SER A 208
REMARK 465 ARG A 209
REMARK 465 HIS A 210
REMARK 465 LEU A 211
REMARK 465 ASN A 212
REMARK 465 ARG A 415
REMARK 465 ASP A 416
REMARK 465 ARG A 417
REMARK 465 HIS A 418
REMARK 465 ARG A 419
REMARK 465 LEU A 420
REMARK 465 THR A 421
REMARK 465 PRO A 422
REMARK 465 LYS B 151
REMARK 465 VAL B 152
REMARK 465 VAL B 153
REMARK 465 ARG B 154
REMARK 465 ALA B 155
REMARK 465 GLY B 156
REMARK 465 ALA B 157
REMARK 465 GLU B 158
REMARK 465 GLY B 159
REMARK 465 GLY B 160
REMARK 465 SER B 161
REMARK 465 GLY B 162
REMARK 465 LEU B 163
REMARK 465 PHE B 164
REMARK 465 GLY B 165
REMARK 465 VAL B 166
REMARK 465 ASP B 167
REMARK 465 TYR B 168
REMARK 465 PHE B 169
REMARK 465 GLU B 170
REMARK 465 LYS B 171
REMARK 465 ARG B 172
REMARK 465 ALA B 173
REMARK 465 TYR B 174
REMARK 465 LEU B 175
REMARK 465 ALA B 176
REMARK 465 GLN B 177
REMARK 465 SER B 178
REMARK 465 PRO B 179
REMARK 465 ARG B 201
REMARK 465 MET B 202
REMARK 465 GLU B 203
REMARK 465 GLU B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 THR B 207
REMARK 465 SER B 208
REMARK 465 ARG B 209
REMARK 465 HIS B 210
REMARK 465 ASP B 416
REMARK 465 ARG B 417
REMARK 465 HIS B 418
REMARK 465 ARG B 419
REMARK 465 LEU B 420
REMARK 465 THR B 421
REMARK 465 PRO B 422
REMARK 465 LYS C 151
REMARK 465 VAL C 152
REMARK 465 VAL C 153
REMARK 465 ARG C 154
REMARK 465 ALA C 155
REMARK 465 GLY C 156
REMARK 465 ALA C 157
REMARK 465 GLU C 158
REMARK 465 GLY C 159
REMARK 465 GLY C 160
REMARK 465 SER C 161
REMARK 465 GLY C 162
REMARK 465 LEU C 163
REMARK 465 PHE C 164
REMARK 465 GLY C 165
REMARK 465 VAL C 166
REMARK 465 ASP C 167
REMARK 465 TYR C 168
REMARK 465 PHE C 169
REMARK 465 GLU C 170
REMARK 465 LYS C 171
REMARK 465 ARG C 172
REMARK 465 ALA C 173
REMARK 465 TYR C 174
REMARK 465 LEU C 175
REMARK 465 ALA C 176
REMARK 465 GLN C 177
REMARK 465 SER C 178
REMARK 465 ARG C 201
REMARK 465 MET C 202
REMARK 465 GLU C 203
REMARK 465 GLU C 204
REMARK 465 HIS C 205
REMARK 465 HIS C 206
REMARK 465 THR C 207
REMARK 465 SER C 208
REMARK 465 ARG C 209
REMARK 465 HIS C 210
REMARK 465 ASP C 416
REMARK 465 ARG C 417
REMARK 465 HIS C 418
REMARK 465 ARG C 419
REMARK 465 LEU C 420
REMARK 465 THR C 421
REMARK 465 PRO C 422
REMARK 465 LYS D 151
REMARK 465 VAL D 152
REMARK 465 VAL D 153
REMARK 465 ARG D 154
REMARK 465 ALA D 155
REMARK 465 GLY D 156
REMARK 465 ALA D 157
REMARK 465 GLU D 158
REMARK 465 GLY D 159
REMARK 465 GLY D 160
REMARK 465 SER D 161
REMARK 465 GLY D 162
REMARK 465 LEU D 163
REMARK 465 PHE D 164
REMARK 465 GLY D 165
REMARK 465 VAL D 166
REMARK 465 ASP D 167
REMARK 465 TYR D 168
REMARK 465 PHE D 169
REMARK 465 GLU D 170
REMARK 465 LYS D 171
REMARK 465 ARG D 172
REMARK 465 ALA D 173
REMARK 465 TYR D 174
REMARK 465 LEU D 175
REMARK 465 ALA D 176
REMARK 465 GLN D 177
REMARK 465 SER D 178
REMARK 465 PRO D 179
REMARK 465 MET D 202
REMARK 465 GLU D 203
REMARK 465 GLU D 204
REMARK 465 HIS D 205
REMARK 465 HIS D 206
REMARK 465 THR D 207
REMARK 465 SER D 208
REMARK 465 ARG D 209
REMARK 465 HIS D 210
REMARK 465 LYS D 364
REMARK 465 ALA D 365
REMARK 465 LYS D 366
REMARK 465 GLY D 367
REMARK 465 MET D 368
REMARK 465 ASP D 369
REMARK 465 ARG D 417
REMARK 465 HIS D 418
REMARK 465 ARG D 419
REMARK 465 LEU D 420
REMARK 465 THR D 421
REMARK 465 PRO D 422
REMARK 465 MET E 1
REMARK 465 ALA E 470
REMARK 465 LEU E 471
REMARK 465 ARG F 254
REMARK 465 THR F 255
REMARK 465 LYS F 256
REMARK 465 GLU F 257
REMARK 465 GLU F 258
REMARK 465 GLU F 259
REMARK 465 UNK F 660
REMARK 465 UNK F 661
REMARK 465 UNK F 662
REMARK 465 UNK F 663
REMARK 465 UNK F 664
REMARK 465 UNK F 665
REMARK 465 UNK F 666
REMARK 465 UNK F 667
REMARK 465 UNK F 668
REMARK 465 UNK F 669
REMARK 465 UNK F 670
REMARK 465 UNK F 671
REMARK 465 UNK F 672
REMARK 465 MET G -1
REMARK 465 PRO G 0
REMARK 465 GLY G 1
REMARK 465 MET G 2
REMARK 465 LEU G 89
REMARK 465 GLU G 90
REMARK 465 MET H 1
REMARK 465 GLU H 469
REMARK 465 ALA H 470
REMARK 465 LEU H 471
REMARK 465 MET I 1
REMARK 465 ARG I 195
REMARK 465 VAL I 196
REMARK 465 GLY I 197
REMARK 465 GLU I 198
REMARK 465 PRO I 199
REMARK 465 THR I 255
REMARK 465 LYS I 256
REMARK 465 GLU I 257
REMARK 465 GLU I 258
REMARK 465 GLU I 259
REMARK 465 PRO I 590
REMARK 465 GLU I 591
REMARK 465 ALA I 592
REMARK 465 UNK I 593
REMARK 465 UNK I 594
REMARK 465 UNK I 595
REMARK 465 UNK I 596
REMARK 465 UNK I 597
REMARK 465 UNK I 598
REMARK 465 UNK I 599
REMARK 465 UNK I 600
REMARK 465 MET J -1
REMARK 465 PRO J 0
REMARK 465 GLY J 1
REMARK 465 MET J 2
REMARK 465 GLY J 48
REMARK 465 GLY J 49
REMARK 465 ALA J 50
REMARK 465 LEU J 89
REMARK 465 GLU J 90
REMARK 465 C K 16
REMARK 465 A K 17
REMARK 465 C L 16
REMARK 465 A L 17
REMARK 465 C M 16
REMARK 465 A M 17
REMARK 465 C M 74
REMARK 465 C M 75
REMARK 465 A M 76
REMARK 465 C N 16
REMARK 465 A N 17
REMARK 465 C N 74
REMARK 465 C N 75
REMARK 465 A N 76
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 464 CG CD CE NZ
REMARK 470 PRO E 466 CG CD
REMARK 470 LEU E 467 CG CD1 CD2
REMARK 470 GLU E 469 CG CD OE1 OE2
REMARK 470 LEU H 463 CG CD1 CD2
REMARK 470 LYS H 464 CG CD CE NZ
REMARK 470 PRO H 466 CG CD
REMARK 470 LEU H 467 CG CD1 CD2
REMARK 470 GLN I 392 CG CD OE1 NE2
REMARK 470 ASP I 393 CG OD1 OD2
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 OE2 GLU F 120 O HOH F 675 1.70
REMARK 500 OE2 GLU I 120 O HOH I 469 1.93
REMARK 500 O GLU H 455 O THR H 458 2.10
REMARK 500 O LEU F 370 O ARG F 373 2.15
REMARK 500 O LEU I 370 O ARG I 373 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 U K 1 P U K 1 OP3 -0.128
REMARK 500 U L 1 P U L 1 OP3 -0.127
REMARK 500 U M 1 P U M 1 OP3 -0.127
REMARK 500 A M 21 P A M 21 OP1 -0.147
REMARK 500 A M 21 P A M 21 OP2 -0.149
REMARK 500 U N 1 P U N 1 OP3 -0.128
REMARK 500 A N 21 P A N 21 OP1 -0.149
REMARK 500 A N 21 P A N 21 OP2 -0.146
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 THR A 47 -160.03 -163.75
REMARK 500 LEU A 50 134.51 -27.95
REMARK 500 ASN A 68 113.75 -162.39
REMARK 500 LYS A 98 31.65 -89.50
REMARK 500 TRP A 101 -178.40 -63.19
REMARK 500 ARG A 102 -14.26 76.57
REMARK 500 TYR A 113 1.46 -65.62
REMARK 500 VAL A 114 -30.08 -147.75
REMARK 500 GLU A 191 -43.94 73.19
REMARK 500 ALA A 249 26.80 -140.44
REMARK 500 ARG A 316 61.27 60.38
REMARK 500 THR B 47 -157.09 -165.85
REMARK 500 LEU B 50 141.94 -38.39
REMARK 500 GLU B 56 4.41 90.03
REMARK 500 ASN B 68 117.08 -164.51
REMARK 500 SER B 86 105.29 -167.38
REMARK 500 TRP B 101 179.35 -52.33
REMARK 500 ARG B 102 -8.90 76.48
REMARK 500 VAL B 114 -38.05 -131.85
REMARK 500 GLU B 191 -45.15 70.10
REMARK 500 ARG B 316 74.06 59.12
REMARK 500 PRO B 323 159.99 -45.48
REMARK 500 PHE B 373 44.63 -94.97
REMARK 500 TYR B 382 79.60 -115.25
REMARK 500 THR C 47 -159.37 -163.44
REMARK 500 LEU C 50 134.27 -28.12
REMARK 500 ASN C 68 113.90 -162.43
REMARK 500 LYS C 98 31.24 -89.73
REMARK 500 TRP C 101 -178.11 -62.57
REMARK 500 ARG C 102 -14.02 75.95
REMARK 500 TYR C 113 1.38 -65.74
REMARK 500 VAL C 114 -29.64 -147.66
REMARK 500 GLU C 191 -43.48 71.57
REMARK 500 ASN C 212 -99.55 69.19
REMARK 500 ARG C 316 60.99 60.60
REMARK 500 THR D 47 -157.19 -165.52
REMARK 500 LEU D 50 142.24 -38.35
REMARK 500 GLU D 56 4.54 89.65
REMARK 500 ASN D 68 116.99 -165.06
REMARK 500 SER D 86 105.50 -167.50
REMARK 500 TRP D 101 179.82 -52.18
REMARK 500 ARG D 102 -8.43 75.63
REMARK 500 VAL D 114 -37.69 -132.01
REMARK 500 GLU D 191 -45.02 70.38
REMARK 500 TRP D 200 -76.08 -135.19
REMARK 500 ARG D 316 74.45 58.67
REMARK 500 PRO D 323 159.80 -45.51
REMARK 500 PHE D 373 44.83 -95.02
REMARK 500 TYR D 382 79.63 -115.32
REMARK 500 ARG D 415 -97.39 -51.12
REMARK 500
REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 673 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 22 SG
REMARK 620 2 CYS F 24 SG 127.9
REMARK 620 3 CYS F 38 SG 111.8 110.2
REMARK 620 4 CYS F 41 SG 94.1 110.9 95.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 674 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 120 OE1
REMARK 620 2 GLU F 120 OE2 56.7
REMARK 620 3 GLU F 146 OE1 88.7 66.9
REMARK 620 4 HOH F 675 O 85.0 44.5 99.8
REMARK 620 5 HOH F 676 O 166.8 111.4 80.7 89.2
REMARK 620 6 HOH F 677 O 87.7 122.5 164.5 94.8 104.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 467 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 22 SG
REMARK 620 2 CYS I 24 SG 130.0
REMARK 620 3 CYS I 38 SG 111.4 107.3
REMARK 620 4 CYS I 41 SG 96.5 110.6 94.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 468 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 120 OE1
REMARK 620 2 GLU I 120 OE2 53.6
REMARK 620 3 GLU I 146 OE1 87.5 63.7
REMARK 620 4 HOH I 469 O 79.7 49.0 104.0
REMARK 620 5 HOH I 470 O 151.2 127.8 119.8 84.6
REMARK 620 6 HOH I 471 O 76.8 105.9 164.3 73.8 75.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 468
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT THE C-TERMINAL RESIDUES FOR CHAINS F AND I
REMARK 999 HAVE ONLY WEAK ELECTRON DENSITY SO IT WAS NOT POSSIBLE TO
REMARK 999 ACCURATELY ASSIGN THE SIDE CHAINS. THE C-TERMINI WERE MODELED AS
REMARK 999 ALA, BUT THE SEQUENCE ALIGNMENT IS UNKNOWN, AND WERE THEREFORE
REMARK 999 CHANGED TO UNK IN THIS ENTRY. THE UNK CORRESPOND TO RESIDUES WITHIN
REMARK 999 THE SEQUENCE LVRERGLKVVADEGALKALVAEAIAAMPEAAESVRQGKVKALDALVGQVMRK
REMARK 999 TRGQARPDLVRRLLLEALGVG BUT CANNOT BE NUMBERED FOR CERTAINTY SINCE
REMARK 999 THEY ARE NOT SURE OF THE FRAME.
DBREF 3KFU A 1 422 UNP Q5SIC2 Q5SIC2_THET8 1 422
DBREF 3KFU B 1 422 UNP Q5SIC2 Q5SIC2_THET8 1 422
DBREF 3KFU C 1 422 UNP Q5SIC2 Q5SIC2_THET8 1 422
DBREF 3KFU D 1 422 UNP Q5SIC2 Q5SIC2_THET8 1 422
DBREF 3KFU E 1 471 UNP Q9LCX3 GATA_THET8 1 471
DBREF 3KFU F 1 672 UNP Q9LCX2 GATB_THET8 1 466
DBREF 3KFU G 2 90 UNP Q9LCX4 GATC_THET8 1 89
DBREF 3KFU H 1 471 UNP Q9LCX3 GATA_THET8 1 471
DBREF 3KFU I 1 671 UNP Q9LCX2 GATB_THET8 1 466
DBREF 3KFU J 2 90 UNP Q9LCX4 GATC_THET8 1 89
DBREF 3KFU K 1 76 PDB 3KFU 3KFU 1 76
DBREF 3KFU L 1 76 PDB 3KFU 3KFU 1 76
DBREF 3KFU M 1 76 PDB 3KFU 3KFU 1 76
DBREF 3KFU N 1 76 PDB 3KFU 3KFU 1 76
SEQADV 3KFU MET G -1 UNP Q9LCX4 EXPRESSION TAG
SEQADV 3KFU PRO G 0 UNP Q9LCX4 EXPRESSION TAG
SEQADV 3KFU GLY G 1 UNP Q9LCX4 EXPRESSION TAG
SEQADV 3KFU MET J -1 UNP Q9LCX4 EXPRESSION TAG
SEQADV 3KFU PRO J 0 UNP Q9LCX4 EXPRESSION TAG
SEQADV 3KFU GLY J 1 UNP Q9LCX4 EXPRESSION TAG
SEQRES 1 A 422 MET ARG VAL LEU VAL ARG ASP LEU LYS ALA HIS VAL GLY
SEQRES 2 A 422 GLN GLU VAL GLU LEU LEU GLY PHE LEU HIS TRP ARG ARG
SEQRES 3 A 422 ASP LEU GLY ARG ILE GLN PHE LEU LEU LEU ARG ASP ARG
SEQRES 4 A 422 SER GLY VAL VAL GLN VAL VAL THR GLY GLY LEU LYS LEU
SEQRES 5 A 422 PRO LEU PRO GLU SER ALA LEU ARG VAL ARG GLY LEU VAL
SEQRES 6 A 422 VAL GLU ASN ALA LYS ALA PRO GLY GLY LEU GLU VAL GLN
SEQRES 7 A 422 ALA LYS GLU VAL GLU VAL LEU SER PRO ALA LEU GLU PRO
SEQRES 8 A 422 THR PRO VAL GLU ILE PRO LYS GLU GLU TRP ARG ALA ASN
SEQRES 9 A 422 PRO ASP THR LEU LEU GLU TYR ARG TYR VAL THR LEU ARG
SEQRES 10 A 422 GLY GLU LYS ALA ARG ALA PRO LEU LYS VAL GLN ALA ALA
SEQRES 11 A 422 LEU VAL ARG GLY PHE ARG ARG TYR LEU ASP ARG GLN ASP
SEQRES 12 A 422 PHE THR GLU ILE PHE THR PRO LYS VAL VAL ARG ALA GLY
SEQRES 13 A 422 ALA GLU GLY GLY SER GLY LEU PHE GLY VAL ASP TYR PHE
SEQRES 14 A 422 GLU LYS ARG ALA TYR LEU ALA GLN SER PRO GLN LEU TYR
SEQRES 15 A 422 LYS GLN ILE MET VAL GLY VAL PHE GLU ARG VAL TYR GLU
SEQRES 16 A 422 VAL ALA PRO VAL TRP ARG MET GLU GLU HIS HIS THR SER
SEQRES 17 A 422 ARG HIS LEU ASN GLU TYR LEU SER LEU ASP VAL GLU MET
SEQRES 18 A 422 GLY PHE ILE ALA ASP GLU GLU ASP LEU MET ARG LEU GLU
SEQRES 19 A 422 GLU ALA LEU LEU ALA GLU MET LEU GLU GLU ALA LEU ASN
SEQRES 20 A 422 THR ALA GLY ASP GLU ILE ARG LEU LEU GLY ALA THR TRP
SEQRES 21 A 422 PRO SER PHE PRO GLN ASP ILE PRO ARG LEU THR HIS ALA
SEQRES 22 A 422 GLU ALA LYS ARG ILE LEU LYS GLU GLU LEU GLY TYR PRO
SEQRES 23 A 422 VAL GLY GLN ASP LEU SER GLU GLU ALA GLU ARG LEU LEU
SEQRES 24 A 422 GLY GLU TYR ALA LYS GLU ARG TRP GLY SER ASP TRP LEU
SEQRES 25 A 422 PHE VAL THR ARG TYR PRO ARG SER VAL ARG PRO PHE TYR
SEQRES 26 A 422 THR TYR PRO GLU GLU ASP GLY THR THR ARG SER PHE ASP
SEQRES 27 A 422 LEU LEU PHE ARG GLY LEU GLU ILE THR SER GLY GLY GLN
SEQRES 28 A 422 ARG ILE HIS ARG TYR GLU GLU LEU LEU GLU SER LEU LYS
SEQRES 29 A 422 ALA LYS GLY MET ASP PRO GLU ALA PHE HIS GLY TYR LEU
SEQRES 30 A 422 GLU VAL PHE LYS TYR GLY MET PRO PRO HIS GLY GLY PHE
SEQRES 31 A 422 ALA ILE GLY ALA GLU ARG LEU THR GLN LYS LEU LEU GLY
SEQRES 32 A 422 LEU PRO ASN VAL ARG TYR ALA ARG ALA PHE PRO ARG ASP
SEQRES 33 A 422 ARG HIS ARG LEU THR PRO
SEQRES 1 B 422 MET ARG VAL LEU VAL ARG ASP LEU LYS ALA HIS VAL GLY
SEQRES 2 B 422 GLN GLU VAL GLU LEU LEU GLY PHE LEU HIS TRP ARG ARG
SEQRES 3 B 422 ASP LEU GLY ARG ILE GLN PHE LEU LEU LEU ARG ASP ARG
SEQRES 4 B 422 SER GLY VAL VAL GLN VAL VAL THR GLY GLY LEU LYS LEU
SEQRES 5 B 422 PRO LEU PRO GLU SER ALA LEU ARG VAL ARG GLY LEU VAL
SEQRES 6 B 422 VAL GLU ASN ALA LYS ALA PRO GLY GLY LEU GLU VAL GLN
SEQRES 7 B 422 ALA LYS GLU VAL GLU VAL LEU SER PRO ALA LEU GLU PRO
SEQRES 8 B 422 THR PRO VAL GLU ILE PRO LYS GLU GLU TRP ARG ALA ASN
SEQRES 9 B 422 PRO ASP THR LEU LEU GLU TYR ARG TYR VAL THR LEU ARG
SEQRES 10 B 422 GLY GLU LYS ALA ARG ALA PRO LEU LYS VAL GLN ALA ALA
SEQRES 11 B 422 LEU VAL ARG GLY PHE ARG ARG TYR LEU ASP ARG GLN ASP
SEQRES 12 B 422 PHE THR GLU ILE PHE THR PRO LYS VAL VAL ARG ALA GLY
SEQRES 13 B 422 ALA GLU GLY GLY SER GLY LEU PHE GLY VAL ASP TYR PHE
SEQRES 14 B 422 GLU LYS ARG ALA TYR LEU ALA GLN SER PRO GLN LEU TYR
SEQRES 15 B 422 LYS GLN ILE MET VAL GLY VAL PHE GLU ARG VAL TYR GLU
SEQRES 16 B 422 VAL ALA PRO VAL TRP ARG MET GLU GLU HIS HIS THR SER
SEQRES 17 B 422 ARG HIS LEU ASN GLU TYR LEU SER LEU ASP VAL GLU MET
SEQRES 18 B 422 GLY PHE ILE ALA ASP GLU GLU ASP LEU MET ARG LEU GLU
SEQRES 19 B 422 GLU ALA LEU LEU ALA GLU MET LEU GLU GLU ALA LEU ASN
SEQRES 20 B 422 THR ALA GLY ASP GLU ILE ARG LEU LEU GLY ALA THR TRP
SEQRES 21 B 422 PRO SER PHE PRO GLN ASP ILE PRO ARG LEU THR HIS ALA
SEQRES 22 B 422 GLU ALA LYS ARG ILE LEU LYS GLU GLU LEU GLY TYR PRO
SEQRES 23 B 422 VAL GLY GLN ASP LEU SER GLU GLU ALA GLU ARG LEU LEU
SEQRES 24 B 422 GLY GLU TYR ALA LYS GLU ARG TRP GLY SER ASP TRP LEU
SEQRES 25 B 422 PHE VAL THR ARG TYR PRO ARG SER VAL ARG PRO PHE TYR
SEQRES 26 B 422 THR TYR PRO GLU GLU ASP GLY THR THR ARG SER PHE ASP
SEQRES 27 B 422 LEU LEU PHE ARG GLY LEU GLU ILE THR SER GLY GLY GLN
SEQRES 28 B 422 ARG ILE HIS ARG TYR GLU GLU LEU LEU GLU SER LEU LYS
SEQRES 29 B 422 ALA LYS GLY MET ASP PRO GLU ALA PHE HIS GLY TYR LEU
SEQRES 30 B 422 GLU VAL PHE LYS TYR GLY MET PRO PRO HIS GLY GLY PHE
SEQRES 31 B 422 ALA ILE GLY ALA GLU ARG LEU THR GLN LYS LEU LEU GLY
SEQRES 32 B 422 LEU PRO ASN VAL ARG TYR ALA ARG ALA PHE PRO ARG ASP
SEQRES 33 B 422 ARG HIS ARG LEU THR PRO
SEQRES 1 C 422 MET ARG VAL LEU VAL ARG ASP LEU LYS ALA HIS VAL GLY
SEQRES 2 C 422 GLN GLU VAL GLU LEU LEU GLY PHE LEU HIS TRP ARG ARG
SEQRES 3 C 422 ASP LEU GLY ARG ILE GLN PHE LEU LEU LEU ARG ASP ARG
SEQRES 4 C 422 SER GLY VAL VAL GLN VAL VAL THR GLY GLY LEU LYS LEU
SEQRES 5 C 422 PRO LEU PRO GLU SER ALA LEU ARG VAL ARG GLY LEU VAL
SEQRES 6 C 422 VAL GLU ASN ALA LYS ALA PRO GLY GLY LEU GLU VAL GLN
SEQRES 7 C 422 ALA LYS GLU VAL GLU VAL LEU SER PRO ALA LEU GLU PRO
SEQRES 8 C 422 THR PRO VAL GLU ILE PRO LYS GLU GLU TRP ARG ALA ASN
SEQRES 9 C 422 PRO ASP THR LEU LEU GLU TYR ARG TYR VAL THR LEU ARG
SEQRES 10 C 422 GLY GLU LYS ALA ARG ALA PRO LEU LYS VAL GLN ALA ALA
SEQRES 11 C 422 LEU VAL ARG GLY PHE ARG ARG TYR LEU ASP ARG GLN ASP
SEQRES 12 C 422 PHE THR GLU ILE PHE THR PRO LYS VAL VAL ARG ALA GLY
SEQRES 13 C 422 ALA GLU GLY GLY SER GLY LEU PHE GLY VAL ASP TYR PHE
SEQRES 14 C 422 GLU LYS ARG ALA TYR LEU ALA GLN SER PRO GLN LEU TYR
SEQRES 15 C 422 LYS GLN ILE MET VAL GLY VAL PHE GLU ARG VAL TYR GLU
SEQRES 16 C 422 VAL ALA PRO VAL TRP ARG MET GLU GLU HIS HIS THR SER
SEQRES 17 C 422 ARG HIS LEU ASN GLU TYR LEU SER LEU ASP VAL GLU MET
SEQRES 18 C 422 GLY PHE ILE ALA ASP GLU GLU ASP LEU MET ARG LEU GLU
SEQRES 19 C 422 GLU ALA LEU LEU ALA GLU MET LEU GLU GLU ALA LEU ASN
SEQRES 20 C 422 THR ALA GLY ASP GLU ILE ARG LEU LEU GLY ALA THR TRP
SEQRES 21 C 422 PRO SER PHE PRO GLN ASP ILE PRO ARG LEU THR HIS ALA
SEQRES 22 C 422 GLU ALA LYS ARG ILE LEU LYS GLU GLU LEU GLY TYR PRO
SEQRES 23 C 422 VAL GLY GLN ASP LEU SER GLU GLU ALA GLU ARG LEU LEU
SEQRES 24 C 422 GLY GLU TYR ALA LYS GLU ARG TRP GLY SER ASP TRP LEU
SEQRES 25 C 422 PHE VAL THR ARG TYR PRO ARG SER VAL ARG PRO PHE TYR
SEQRES 26 C 422 THR TYR PRO GLU GLU ASP GLY THR THR ARG SER PHE ASP
SEQRES 27 C 422 LEU LEU PHE ARG GLY LEU GLU ILE THR SER GLY GLY GLN
SEQRES 28 C 422 ARG ILE HIS ARG TYR GLU GLU LEU LEU GLU SER LEU LYS
SEQRES 29 C 422 ALA LYS GLY MET ASP PRO GLU ALA PHE HIS GLY TYR LEU
SEQRES 30 C 422 GLU VAL PHE LYS TYR GLY MET PRO PRO HIS GLY GLY PHE
SEQRES 31 C 422 ALA ILE GLY ALA GLU ARG LEU THR GLN LYS LEU LEU GLY
SEQRES 32 C 422 LEU PRO ASN VAL ARG TYR ALA ARG ALA PHE PRO ARG ASP
SEQRES 33 C 422 ARG HIS ARG LEU THR PRO
SEQRES 1 D 422 MET ARG VAL LEU VAL ARG ASP LEU LYS ALA HIS VAL GLY
SEQRES 2 D 422 GLN GLU VAL GLU LEU LEU GLY PHE LEU HIS TRP ARG ARG
SEQRES 3 D 422 ASP LEU GLY ARG ILE GLN PHE LEU LEU LEU ARG ASP ARG
SEQRES 4 D 422 SER GLY VAL VAL GLN VAL VAL THR GLY GLY LEU LYS LEU
SEQRES 5 D 422 PRO LEU PRO GLU SER ALA LEU ARG VAL ARG GLY LEU VAL
SEQRES 6 D 422 VAL GLU ASN ALA LYS ALA PRO GLY GLY LEU GLU VAL GLN
SEQRES 7 D 422 ALA LYS GLU VAL GLU VAL LEU SER PRO ALA LEU GLU PRO
SEQRES 8 D 422 THR PRO VAL GLU ILE PRO LYS GLU GLU TRP ARG ALA ASN
SEQRES 9 D 422 PRO ASP THR LEU LEU GLU TYR ARG TYR VAL THR LEU ARG
SEQRES 10 D 422 GLY GLU LYS ALA ARG ALA PRO LEU LYS VAL GLN ALA ALA
SEQRES 11 D 422 LEU VAL ARG GLY PHE ARG ARG TYR LEU ASP ARG GLN ASP
SEQRES 12 D 422 PHE THR GLU ILE PHE THR PRO LYS VAL VAL ARG ALA GLY
SEQRES 13 D 422 ALA GLU GLY GLY SER GLY LEU PHE GLY VAL ASP TYR PHE
SEQRES 14 D 422 GLU LYS ARG ALA TYR LEU ALA GLN SER PRO GLN LEU TYR
SEQRES 15 D 422 LYS GLN ILE MET VAL GLY VAL PHE GLU ARG VAL TYR GLU
SEQRES 16 D 422 VAL ALA PRO VAL TRP ARG MET GLU GLU HIS HIS THR SER
SEQRES 17 D 422 ARG HIS LEU ASN GLU TYR LEU SER LEU ASP VAL GLU MET
SEQRES 18 D 422 GLY PHE ILE ALA ASP GLU GLU ASP LEU MET ARG LEU GLU
SEQRES 19 D 422 GLU ALA LEU LEU ALA GLU MET LEU GLU GLU ALA LEU ASN
SEQRES 20 D 422 THR ALA GLY ASP GLU ILE ARG LEU LEU GLY ALA THR TRP
SEQRES 21 D 422 PRO SER PHE PRO GLN ASP ILE PRO ARG LEU THR HIS ALA
SEQRES 22 D 422 GLU ALA LYS ARG ILE LEU LYS GLU GLU LEU GLY TYR PRO
SEQRES 23 D 422 VAL GLY GLN ASP LEU SER GLU GLU ALA GLU ARG LEU LEU
SEQRES 24 D 422 GLY GLU TYR ALA LYS GLU ARG TRP GLY SER ASP TRP LEU
SEQRES 25 D 422 PHE VAL THR ARG TYR PRO ARG SER VAL ARG PRO PHE TYR
SEQRES 26 D 422 THR TYR PRO GLU GLU ASP GLY THR THR ARG SER PHE ASP
SEQRES 27 D 422 LEU LEU PHE ARG GLY LEU GLU ILE THR SER GLY GLY GLN
SEQRES 28 D 422 ARG ILE HIS ARG TYR GLU GLU LEU LEU GLU SER LEU LYS
SEQRES 29 D 422 ALA LYS GLY MET ASP PRO GLU ALA PHE HIS GLY TYR LEU
SEQRES 30 D 422 GLU VAL PHE LYS TYR GLY MET PRO PRO HIS GLY GLY PHE
SEQRES 31 D 422 ALA ILE GLY ALA GLU ARG LEU THR GLN LYS LEU LEU GLY
SEQRES 32 D 422 LEU PRO ASN VAL ARG TYR ALA ARG ALA PHE PRO ARG ASP
SEQRES 33 D 422 ARG HIS ARG LEU THR PRO
SEQRES 1 E 471 MET LEU ALA HIS GLU ILE ARG ALA ARG VAL ALA ARG GLY
SEQRES 2 E 471 GLU VAL SER PRO LEU GLU VAL ALA GLN ALA TYR LEU LYS
SEQRES 3 E 471 ARG VAL GLN GLU LEU ASP PRO GLY LEU GLY ALA PHE LEU
SEQRES 4 E 471 SER LEU ASN GLU ARG LEU LEU GLU GLU ALA GLU ALA VAL
SEQRES 5 E 471 ASP PRO GLY LEU PRO LEU ALA GLY LEU VAL VAL ALA VAL
SEQRES 6 E 471 LYS ASP ASN ILE ALA THR ARG GLY LEU ARG THR THR ALA
SEQRES 7 E 471 GLY SER ARG LEU LEU GLU ASN PHE VAL PRO PRO TYR GLU
SEQRES 8 E 471 ALA THR ALA VAL ALA ARG LEU LYS ALA LEU GLY ALA LEU
SEQRES 9 E 471 VAL LEU GLY LYS THR ASN LEU ASP GLU PHE GLY MET GLY
SEQRES 10 E 471 SER SER THR GLU HIS SER ALA PHE PHE PRO THR LYS ASN
SEQRES 11 E 471 PRO PHE ASP PRO ASP ARG VAL PRO GLY GLY SER SER GLY
SEQRES 12 E 471 GLY SER ALA ALA ALA LEU ALA ALA ASP LEU ALA PRO LEU
SEQRES 13 E 471 ALA LEU GLY SER ASP THR GLY GLY SER VAL ARG GLN PRO
SEQRES 14 E 471 ALA ALA PHE CYS GLY VAL TYR GLY LEU LYS PRO THR TYR
SEQRES 15 E 471 GLY ARG VAL SER ARG PHE GLY LEU ILE ALA TYR ALA SER
SEQRES 16 E 471 SER LEU ASP GLN ILE GLY PRO MET ALA ARG SER VAL ARG
SEQRES 17 E 471 ASP LEU ALA LEU LEU MET ASP ALA ALA ALA GLY PRO ASP
SEQRES 18 E 471 PRO LEU ASP ALA THR SER LEU ASP LEU PRO PRO ARG PHE
SEQRES 19 E 471 GLN GLU ALA LEU GLU GLY PRO LEU PRO PRO LEU ARG LEU
SEQRES 20 E 471 GLY VAL VAL ARG GLU ALA LEU ALA GLY ASN SER PRO GLY
SEQRES 21 E 471 VAL GLU ARG ALA LEU GLU GLU ALA LEU LYS VAL PHE ARG
SEQRES 22 E 471 GLU LEU GLY LEU SER VAL ARG GLU VAL SER TRP PRO SER
SEQRES 23 E 471 LEU PRO GLN ALA LEU ALA ALA TYR TYR ILE LEU ALA PRO
SEQRES 24 E 471 ALA GLU ALA SER SER ASN LEU ALA ARG TYR ASP GLY THR
SEQRES 25 E 471 LEU TYR GLY ARG ARG ALA ALA GLY GLU GLU VAL GLU GLY
SEQRES 26 E 471 MET MET GLU ALA THR ARG ALA LEU PHE GLY LEU GLU VAL
SEQRES 27 E 471 LYS ARG ARG VAL LEU VAL GLY THR PHE VAL LEU SER SER
SEQRES 28 E 471 GLY TYR TYR GLU ALA TYR TYR GLY ARG ALA GLN ALA PHE
SEQRES 29 E 471 ARG ARG ARG LEU LYS ALA GLU ALA GLN ALA LEU PHE ARG
SEQRES 30 E 471 GLU VAL ASP LEU LEU LEU LEU PRO THR THR PRO HIS PRO
SEQRES 31 E 471 ALA PHE PRO PHE GLY ALA ARG ARG ASP PRO LEU ALA MET
SEQRES 32 E 471 TYR ARG GLU ASP LEU TYR THR VAL GLY ALA ASN LEU THR
SEQRES 33 E 471 GLY LEU PRO ALA LEU SER PHE PRO ALA GLY PHE GLU GLY
SEQRES 34 E 471 HIS LEU PRO VAL GLY LEU GLN LEU LEU ALA PRO TRP GLY
SEQRES 35 E 471 GLU ASP GLU ARG LEU LEU ARG ALA ALA LEU ALA PHE GLU
SEQRES 36 E 471 GLU ALA THR ALA ARG ALA HIS LEU LYS ALA PRO LEU GLY
SEQRES 37 E 471 GLU ALA LEU
SEQRES 1 F 466 MET TYR GLU ALA VAL ILE GLY LEU GLU VAL HIS LEU HIS
SEQRES 2 F 466 LEU LYS THR ARG THR LYS MET PHE CYS GLY CYS ARG ALA
SEQRES 3 F 466 ASP TYR PHE GLY ALA GLU PRO ASN THR HIS THR CYS PRO
SEQRES 4 F 466 VAL CYS LEU GLY LEU PRO GLY ALA LEU PRO VAL PRO ASN
SEQRES 5 F 466 ARG VAL ALA VAL GLU HIS GLY LEU ARG LEU ALA LEU ALA
SEQRES 6 F 466 LEU GLY ALA GLU VAL PRO GLU ARG LEU VAL PHE HIS ARG
SEQRES 7 F 466 LYS ASN TYR PHE TYR PRO ASP LEU PRO LYS ASN TYR GLN
SEQRES 8 F 466 ILE SER GLN TYR ASP LEU PRO LEU GLY ARG GLY GLY SER
SEQRES 9 F 466 LEU PRO LEU GLY GLU ARG ARG VAL ARG ILE LYS ARG LEU
SEQRES 10 F 466 HIS LEU GLU GLU ASP ALA GLY LYS SER LEU HIS LEU GLU
SEQRES 11 F 466 GLY ARG THR LEU LEU ASP LEU ASN ARG ALA GLY SER PRO
SEQRES 12 F 466 LEU ILE GLU LEU VAL THR GLU PRO ASP LEU LYS THR PRO
SEQRES 13 F 466 GLU GLU ALA ARG LEU PHE LEU GLN ARG ILE GLN ALA LEU
SEQRES 14 F 466 VAL GLN THR LEU GLY ILE SER ASP ALA SER PRO GLU GLU
SEQRES 15 F 466 GLY LYS LEU ARG ALA ASP VAL ASN VAL SER VAL ARG ARG
SEQRES 16 F 466 VAL GLY GLU PRO LEU GLY THR LYS VAL GLU ILE LYS ASN
SEQRES 17 F 466 LEU ASN SER PHE LYS SER VAL GLN ARG ALA LEU GLU TYR
SEQRES 18 F 466 GLU ILE ARG ARG GLN THR GLU ILE LEU ARG ARG GLY GLU
SEQRES 19 F 466 LYS VAL LYS GLN ALA THR MET GLY PHE GLU GLU GLY SER
SEQRES 20 F 466 GLY LYS THR TYR PRO MET ARG THR LYS GLU GLU GLU ALA
SEQRES 21 F 466 ASP TYR ARG TYR PHE PRO GLU PRO ASP LEU PRO PRO VAL
SEQRES 22 F 466 ALA ILE PRO ARG ASP TRP LEU GLU GLU VAL ARG ARG SER
SEQRES 23 F 466 LEU PRO GLU LEU PRO TRP GLU LYS GLU ALA ARG TYR ARG
SEQRES 24 F 466 ALA LEU GLY ILE LYS GLU LYS ASP ALA GLU VAL LEU ALA
SEQRES 25 F 466 TYR THR PRO SER LEU ALA ARG PHE LEU ASP GLN ALA LEU
SEQRES 26 F 466 PRO LEU GLY LEU ALA SER PRO GLN ALA LEU ALA ASN TRP
SEQRES 27 F 466 LEU LEU ALA ASP VAL ALA GLY LEU LEU HIS GLU ARG GLY
SEQRES 28 F 466 LEU ARG LEU GLU GLU THR ARG LEU SER PRO GLU GLY LEU
SEQRES 29 F 466 ALA ARG LEU VAL GLY LEU PHE GLU ARG GLY GLU VAL THR
SEQRES 30 F 466 SER ARG VAL ALA LYS SER LEU LEU PRO GLU VAL LEU GLU
SEQRES 31 F 466 GLY GLN ASP PRO GLU ALA UNK UNK UNK UNK UNK UNK UNK
SEQRES 32 F 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 33 F 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 34 F 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 35 F 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 36 F 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 G 92 MET PRO GLY MET GLU LEU SER PRO GLU LEU LEU ARG LYS
SEQRES 2 G 92 LEU GLU THR LEU ALA LYS ILE ARG LEU SER PRO GLU GLU
SEQRES 3 G 92 GLU ALA LEU LEU LEU GLN ASP LEU LYS ARG ILE LEU ASP
SEQRES 4 G 92 PHE VAL ASP ALA LEU PRO ARG VAL GLU GLU GLY GLY ALA
SEQRES 5 G 92 GLU GLU ALA LEU GLY ARG LEU ARG GLU ASP GLU PRO ARG
SEQRES 6 G 92 PRO SER LEU PRO GLN ALA GLU ALA LEU ALA LEU ALA PRO
SEQRES 7 G 92 GLU ALA GLU ASP GLY PHE PHE ARG VAL PRO PRO VAL LEU
SEQRES 8 G 92 GLU
SEQRES 1 H 471 MET LEU ALA HIS GLU ILE ARG ALA ARG VAL ALA ARG GLY
SEQRES 2 H 471 GLU VAL SER PRO LEU GLU VAL ALA GLN ALA TYR LEU LYS
SEQRES 3 H 471 ARG VAL GLN GLU LEU ASP PRO GLY LEU GLY ALA PHE LEU
SEQRES 4 H 471 SER LEU ASN GLU ARG LEU LEU GLU GLU ALA GLU ALA VAL
SEQRES 5 H 471 ASP PRO GLY LEU PRO LEU ALA GLY LEU VAL VAL ALA VAL
SEQRES 6 H 471 LYS ASP ASN ILE ALA THR ARG GLY LEU ARG THR THR ALA
SEQRES 7 H 471 GLY SER ARG LEU LEU GLU ASN PHE VAL PRO PRO TYR GLU
SEQRES 8 H 471 ALA THR ALA VAL ALA ARG LEU LYS ALA LEU GLY ALA LEU
SEQRES 9 H 471 VAL LEU GLY LYS THR ASN LEU ASP GLU PHE GLY MET GLY
SEQRES 10 H 471 SER SER THR GLU HIS SER ALA PHE PHE PRO THR LYS ASN
SEQRES 11 H 471 PRO PHE ASP PRO ASP ARG VAL PRO GLY GLY SER SER GLY
SEQRES 12 H 471 GLY SER ALA ALA ALA LEU ALA ALA ASP LEU ALA PRO LEU
SEQRES 13 H 471 ALA LEU GLY SER ASP THR GLY GLY SER VAL ARG GLN PRO
SEQRES 14 H 471 ALA ALA PHE CYS GLY VAL TYR GLY LEU LYS PRO THR TYR
SEQRES 15 H 471 GLY ARG VAL SER ARG PHE GLY LEU ILE ALA TYR ALA SER
SEQRES 16 H 471 SER LEU ASP GLN ILE GLY PRO MET ALA ARG SER VAL ARG
SEQRES 17 H 471 ASP LEU ALA LEU LEU MET ASP ALA ALA ALA GLY PRO ASP
SEQRES 18 H 471 PRO LEU ASP ALA THR SER LEU ASP LEU PRO PRO ARG PHE
SEQRES 19 H 471 GLN GLU ALA LEU GLU GLY PRO LEU PRO PRO LEU ARG LEU
SEQRES 20 H 471 GLY VAL VAL ARG GLU ALA LEU ALA GLY ASN SER PRO GLY
SEQRES 21 H 471 VAL GLU ARG ALA LEU GLU GLU ALA LEU LYS VAL PHE ARG
SEQRES 22 H 471 GLU LEU GLY LEU SER VAL ARG GLU VAL SER TRP PRO SER
SEQRES 23 H 471 LEU PRO GLN ALA LEU ALA ALA TYR TYR ILE LEU ALA PRO
SEQRES 24 H 471 ALA GLU ALA SER SER ASN LEU ALA ARG TYR ASP GLY THR
SEQRES 25 H 471 LEU TYR GLY ARG ARG ALA ALA GLY GLU GLU VAL GLU GLY
SEQRES 26 H 471 MET MET GLU ALA THR ARG ALA LEU PHE GLY LEU GLU VAL
SEQRES 27 H 471 LYS ARG ARG VAL LEU VAL GLY THR PHE VAL LEU SER SER
SEQRES 28 H 471 GLY TYR TYR GLU ALA TYR TYR GLY ARG ALA GLN ALA PHE
SEQRES 29 H 471 ARG ARG ARG LEU LYS ALA GLU ALA GLN ALA LEU PHE ARG
SEQRES 30 H 471 GLU VAL ASP LEU LEU LEU LEU PRO THR THR PRO HIS PRO
SEQRES 31 H 471 ALA PHE PRO PHE GLY ALA ARG ARG ASP PRO LEU ALA MET
SEQRES 32 H 471 TYR ARG GLU ASP LEU TYR THR VAL GLY ALA ASN LEU THR
SEQRES 33 H 471 GLY LEU PRO ALA LEU SER PHE PRO ALA GLY PHE GLU GLY
SEQRES 34 H 471 HIS LEU PRO VAL GLY LEU GLN LEU LEU ALA PRO TRP GLY
SEQRES 35 H 471 GLU ASP GLU ARG LEU LEU ARG ALA ALA LEU ALA PHE GLU
SEQRES 36 H 471 GLU ALA THR ALA ARG ALA HIS LEU LYS ALA PRO LEU GLY
SEQRES 37 H 471 GLU ALA LEU
SEQRES 1 I 466 MET TYR GLU ALA VAL ILE GLY LEU GLU VAL HIS LEU HIS
SEQRES 2 I 466 LEU LYS THR ARG THR LYS MET PHE CYS GLY CYS ARG ALA
SEQRES 3 I 466 ASP TYR PHE GLY ALA GLU PRO ASN THR HIS THR CYS PRO
SEQRES 4 I 466 VAL CYS LEU GLY LEU PRO GLY ALA LEU PRO VAL PRO ASN
SEQRES 5 I 466 ARG VAL ALA VAL GLU HIS GLY LEU ARG LEU ALA LEU ALA
SEQRES 6 I 466 LEU GLY ALA GLU VAL PRO GLU ARG LEU VAL PHE HIS ARG
SEQRES 7 I 466 LYS ASN TYR PHE TYR PRO ASP LEU PRO LYS ASN TYR GLN
SEQRES 8 I 466 ILE SER GLN TYR ASP LEU PRO LEU GLY ARG GLY GLY SER
SEQRES 9 I 466 LEU PRO LEU GLY GLU ARG ARG VAL ARG ILE LYS ARG LEU
SEQRES 10 I 466 HIS LEU GLU GLU ASP ALA GLY LYS SER LEU HIS LEU GLU
SEQRES 11 I 466 GLY ARG THR LEU LEU ASP LEU ASN ARG ALA GLY SER PRO
SEQRES 12 I 466 LEU ILE GLU LEU VAL THR GLU PRO ASP LEU LYS THR PRO
SEQRES 13 I 466 GLU GLU ALA ARG LEU PHE LEU GLN ARG ILE GLN ALA LEU
SEQRES 14 I 466 VAL GLN THR LEU GLY ILE SER ASP ALA SER PRO GLU GLU
SEQRES 15 I 466 GLY LYS LEU ARG ALA ASP VAL ASN VAL SER VAL ARG ARG
SEQRES 16 I 466 VAL GLY GLU PRO LEU GLY THR LYS VAL GLU ILE LYS ASN
SEQRES 17 I 466 LEU ASN SER PHE LYS SER VAL GLN ARG ALA LEU GLU TYR
SEQRES 18 I 466 GLU ILE ARG ARG GLN THR GLU ILE LEU ARG ARG GLY GLU
SEQRES 19 I 466 LYS VAL LYS GLN ALA THR MET GLY PHE GLU GLU GLY SER
SEQRES 20 I 466 GLY LYS THR TYR PRO MET ARG THR LYS GLU GLU GLU ALA
SEQRES 21 I 466 ASP TYR ARG TYR PHE PRO GLU PRO ASP LEU PRO PRO VAL
SEQRES 22 I 466 ALA ILE PRO ARG ASP TRP LEU GLU GLU VAL ARG ARG SER
SEQRES 23 I 466 LEU PRO GLU LEU PRO TRP GLU LYS GLU ALA ARG TYR ARG
SEQRES 24 I 466 ALA LEU GLY ILE LYS GLU LYS ASP ALA GLU VAL LEU ALA
SEQRES 25 I 466 TYR THR PRO SER LEU ALA ARG PHE LEU ASP GLN ALA LEU
SEQRES 26 I 466 PRO LEU GLY LEU ALA SER PRO GLN ALA LEU ALA ASN TRP
SEQRES 27 I 466 LEU LEU ALA ASP VAL ALA GLY LEU LEU HIS GLU ARG GLY
SEQRES 28 I 466 LEU ARG LEU GLU GLU THR ARG LEU SER PRO GLU GLY LEU
SEQRES 29 I 466 ALA ARG LEU VAL GLY LEU PHE GLU ARG GLY GLU VAL THR
SEQRES 30 I 466 SER ARG VAL ALA LYS SER LEU LEU PRO GLU VAL LEU GLU
SEQRES 31 I 466 GLY GLN ASP PRO GLU ALA UNK UNK UNK UNK UNK UNK UNK
SEQRES 32 I 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 33 I 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 34 I 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 35 I 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 36 I 466 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 J 92 MET PRO GLY MET GLU LEU SER PRO GLU LEU LEU ARG LYS
SEQRES 2 J 92 LEU GLU THR LEU ALA LYS ILE ARG LEU SER PRO GLU GLU
SEQRES 3 J 92 GLU ALA LEU LEU LEU GLN ASP LEU LYS ARG ILE LEU ASP
SEQRES 4 J 92 PHE VAL ASP ALA LEU PRO ARG VAL GLU GLU GLY GLY ALA
SEQRES 5 J 92 GLU GLU ALA LEU GLY ARG LEU ARG GLU ASP GLU PRO ARG
SEQRES 6 J 92 PRO SER LEU PRO GLN ALA GLU ALA LEU ALA LEU ALA PRO
SEQRES 7 J 92 GLU ALA GLU ASP GLY PHE PHE ARG VAL PRO PRO VAL LEU
SEQRES 8 J 92 GLU
SEQRES 1 K 76 U C C G C G G U A G C U C
SEQRES 2 K 76 A G C A G G H2U A G A G C A
SEQRES 3 K 76 G C C G G C U G U U A A C
SEQRES 4 K 76 C G G U A G G U C G C A G
SEQRES 5 K 76 G 5MU PSU C G A G U C C U G C
SEQRES 6 K 76 C C G C G G A G C C A
SEQRES 1 L 76 U C C G C G G U A G C U C
SEQRES 2 L 76 A G C A G G H2U A G A G C A
SEQRES 3 L 76 G C C G G C U G U U A A C
SEQRES 4 L 76 C G G U A G G U C G C A G
SEQRES 5 L 76 G 5MU PSU C G A G U C C U G C
SEQRES 6 L 76 C C G C G G A G C C A
SEQRES 1 M 76 U C C G C G G U A G C U C
SEQRES 2 M 76 A G C A G G H2U A G A G C A
SEQRES 3 M 76 G C C G G C U G U U A A C
SEQRES 4 M 76 C G G U A G G U C G C A G
SEQRES 5 M 76 G 5MU PSU C G A G U C C U G C
SEQRES 6 M 76 C C G C G G A G C C A
SEQRES 1 N 76 U C C G C G G U A G C U C
SEQRES 2 N 76 A G C A G G H2U A G A G C A
SEQRES 3 N 76 G C C G G C U G U U A A C
SEQRES 4 N 76 C G G U A G G U C G C A G
SEQRES 5 N 76 G 5MU PSU C G A G U C C U G C
SEQRES 6 N 76 C C G C G G A G C C A
MODRES 3KFU H2U K 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU 5MU K 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 3KFU PSU K 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU H2U L 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU 5MU L 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 3KFU PSU L 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU H2U M 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU 5MU M 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 3KFU PSU M 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU H2U N 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 3KFU 5MU N 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 3KFU PSU N 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
HET H2U K 20 20
HET 5MU K 54 21
HET PSU K 55 20
HET H2U L 20 20
HET 5MU L 54 21
HET PSU L 55 20
HET H2U M 20 20
HET 5MU M 54 21
HET PSU M 55 20
HET H2U N 20 20
HET 5MU N 54 21
HET PSU N 55 20
HET ZN F 673 1
HET MG F 674 1
HET ZN I 467 1
HET MG I 468 1
HETNAM H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 11 H2U 4(C9 H15 N2 O9 P)
FORMUL 11 5MU 4(C10 H15 N2 O9 P)
FORMUL 11 PSU 4(C9 H13 N2 O9 P)
FORMUL 15 ZN 2(ZN 2+)
FORMUL 16 MG 2(MG 2+)
FORMUL 19 HOH *6(H2 O)
HELIX 1 1 LEU A 4 VAL A 12 5 9
HELIX 2 2 GLU A 95 GLU A 99 5 5
HELIX 3 3 ASP A 106 TYR A 111 1 6
HELIX 4 4 TYR A 111 LEU A 116 1 6
HELIX 5 5 GLY A 118 GLN A 142 1 25
HELIX 6 6 PRO A 179 GLU A 191 1 13
HELIX 7 7 ASP A 226 ALA A 249 1 24
HELIX 8 8 ALA A 249 LEU A 256 1 8
HELIX 9 9 HIS A 272 GLU A 282 1 11
HELIX 10 10 SER A 292 TRP A 307 1 16
HELIX 11 11 PRO A 318 ARG A 322 5 5
HELIX 12 12 ARG A 355 LYS A 366 1 12
HELIX 13 13 ASP A 369 ALA A 372 5 4
HELIX 14 14 PHE A 373 GLU A 378 1 6
HELIX 15 15 VAL A 379 TYR A 382 5 4
HELIX 16 16 ALA A 394 GLY A 403 1 10
HELIX 17 17 ASN A 406 ARG A 411 5 6
HELIX 18 18 LEU B 4 VAL B 12 5 9
HELIX 19 19 ALA B 71 GLY B 73 5 3
HELIX 20 20 GLU B 95 GLU B 99 5 5
HELIX 21 21 ASN B 104 TYR B 111 1 8
HELIX 22 22 TYR B 111 LEU B 116 1 6
HELIX 23 23 GLY B 118 GLN B 142 1 25
HELIX 24 24 GLN B 180 MET B 186 1 7
HELIX 25 25 MET B 186 GLU B 191 1 6
HELIX 26 26 ASP B 226 ALA B 249 1 24
HELIX 27 27 ALA B 249 LEU B 256 1 8
HELIX 28 28 HIS B 272 GLU B 282 1 11
HELIX 29 29 SER B 292 TRP B 307 1 16
HELIX 30 30 SER B 320 ARG B 322 5 3
HELIX 31 31 ARG B 355 SER B 362 1 8
HELIX 32 32 ASP B 369 ALA B 372 5 4
HELIX 33 33 PHE B 373 GLU B 378 1 6
HELIX 34 34 VAL B 379 TYR B 382 5 4
HELIX 35 35 ALA B 394 LEU B 402 1 9
HELIX 36 36 ASN B 406 ARG B 411 5 6
HELIX 37 37 LEU C 4 VAL C 12 5 9
HELIX 38 38 GLU C 95 GLU C 99 5 5
HELIX 39 39 ASP C 106 TYR C 111 1 6
HELIX 40 40 TYR C 111 LEU C 116 1 6
HELIX 41 41 GLY C 118 GLN C 142 1 25
HELIX 42 42 PRO C 179 GLU C 191 1 13
HELIX 43 43 ASP C 226 ALA C 249 1 24
HELIX 44 44 ALA C 249 LEU C 256 1 8
HELIX 45 45 HIS C 272 GLU C 282 1 11
HELIX 46 46 SER C 292 TRP C 307 1 16
HELIX 47 47 PRO C 318 ARG C 322 5 5
HELIX 48 48 ARG C 355 LYS C 366 1 12
HELIX 49 49 ASP C 369 ALA C 372 5 4
HELIX 50 50 PHE C 373 GLU C 378 1 6
HELIX 51 51 VAL C 379 TYR C 382 5 4
HELIX 52 52 ALA C 394 GLY C 403 1 10
HELIX 53 53 ASN C 406 ARG C 411 5 6
HELIX 54 54 LEU D 4 VAL D 12 5 9
HELIX 55 55 ALA D 71 GLY D 73 5 3
HELIX 56 56 GLU D 95 GLU D 99 5 5
HELIX 57 57 ASN D 104 TYR D 111 1 8
HELIX 58 58 TYR D 111 LEU D 116 1 6
HELIX 59 59 GLY D 118 GLN D 142 1 25
HELIX 60 60 GLN D 180 MET D 186 1 7
HELIX 61 61 MET D 186 GLU D 191 1 6
HELIX 62 62 ASP D 226 ALA D 249 1 24
HELIX 63 63 ALA D 249 LEU D 256 1 8
HELIX 64 64 HIS D 272 GLU D 282 1 11
HELIX 65 65 SER D 292 TRP D 307 1 16
HELIX 66 66 SER D 320 ARG D 322 5 3
HELIX 67 67 ARG D 355 SER D 362 1 8
HELIX 68 68 PRO D 370 ALA D 372 5 3
HELIX 69 69 PHE D 373 GLU D 378 1 6
HELIX 70 70 VAL D 379 TYR D 382 5 4
HELIX 71 71 ALA D 394 LEU D 402 1 9
HELIX 72 72 ASN D 406 ARG D 411 5 6
HELIX 73 73 LEU E 2 ARG E 12 1 11
HELIX 74 74 SER E 16 GLY E 36 1 21
HELIX 75 75 LEU E 46 ALA E 51 1 6
HELIX 76 76 ALA E 92 ALA E 100 1 9
HELIX 77 77 ASP E 112 MET E 116 5 5
HELIX 78 78 SER E 142 ALA E 151 1 10
HELIX 79 79 VAL E 166 CYS E 173 1 8
HELIX 80 80 SER E 206 ALA E 218 1 13
HELIX 81 81 GLU E 252 LEU E 254 5 3
HELIX 82 82 SER E 258 GLU E 274 1 17
HELIX 83 83 SER E 286 PRO E 288 5 3
HELIX 84 84 GLN E 289 LEU E 306 1 18
HELIX 85 85 ALA E 307 TYR E 309 5 3
HELIX 86 86 VAL E 323 ALA E 332 1 10
HELIX 87 87 GLY E 335 SER E 350 1 16
HELIX 88 88 TYR E 357 PHE E 376 1 20
HELIX 89 89 ASP E 399 ARG E 405 1 7
HELIX 90 90 GLU E 406 LEU E 408 5 3
HELIX 91 91 THR E 410 GLY E 417 1 8
HELIX 92 92 GLU E 443 THR E 458 1 16
HELIX 93 93 ASN F 52 GLY F 67 1 16
HELIX 94 94 THR F 155 GLY F 174 1 20
HELIX 95 95 SER F 179 GLY F 183 5 5
HELIX 96 96 SER F 211 ARG F 231 1 21
HELIX 97 97 PRO F 276 ARG F 285 1 10
HELIX 98 98 LEU F 290 ARG F 299 1 10
HELIX 99 99 LYS F 304 TYR F 313 1 10
HELIX 100 100 THR F 314 LEU F 325 1 12
HELIX 101 101 SER F 331 ALA F 341 1 11
HELIX 102 102 ALA F 341 GLY F 351 1 11
HELIX 103 103 SER F 360 ARG F 373 1 14
HELIX 104 104 THR F 377 LEU F 389 1 13
HELIX 105 105 UNK F 605 UNK F 617 1 13
HELIX 106 106 UNK F 618 UNK F 620 5 3
HELIX 107 107 UNK F 621 UNK F 626 1 6
HELIX 108 108 UNK F 631 UNK F 641 1 11
HELIX 109 109 UNK F 646 UNK F 659 1 14
HELIX 110 110 SER G 5 ALA G 16 1 12
HELIX 111 111 SER G 21 ALA G 41 1 21
HELIX 112 112 PRO G 67 ALA G 73 1 7
HELIX 113 113 LEU H 2 ARG H 12 1 11
HELIX 114 114 SER H 16 GLY H 36 1 21
HELIX 115 115 LEU H 46 ALA H 51 1 6
HELIX 116 116 ALA H 92 ALA H 100 1 9
HELIX 117 117 ASP H 112 MET H 116 5 5
HELIX 118 118 SER H 142 ALA H 151 1 10
HELIX 119 119 VAL H 166 CYS H 173 1 8
HELIX 120 120 SER H 206 ALA H 218 1 13
HELIX 121 121 GLU H 252 LEU H 254 5 3
HELIX 122 122 SER H 258 GLU H 274 1 17
HELIX 123 123 SER H 286 PRO H 288 5 3
HELIX 124 124 GLN H 289 LEU H 306 1 18
HELIX 125 125 ALA H 307 TYR H 309 5 3
HELIX 126 126 VAL H 323 ALA H 332 1 10
HELIX 127 127 GLY H 335 SER H 350 1 16
HELIX 128 128 TYR H 357 PHE H 376 1 20
HELIX 129 129 ASP H 399 ARG H 405 1 7
HELIX 130 130 GLU H 406 LEU H 408 5 3
HELIX 131 131 THR H 410 GLY H 417 1 8
HELIX 132 132 GLU H 443 THR H 458 1 16
HELIX 133 133 ASN I 52 GLY I 67 1 16
HELIX 134 134 THR I 155 GLY I 174 1 20
HELIX 135 135 SER I 179 GLY I 183 5 5
HELIX 136 136 SER I 211 ARG I 231 1 21
HELIX 137 137 PRO I 276 ARG I 285 1 10
HELIX 138 138 LEU I 290 ARG I 299 1 10
HELIX 139 139 LYS I 304 TYR I 313 1 10
HELIX 140 140 THR I 314 LEU I 325 1 12
HELIX 141 141 SER I 331 ALA I 341 1 11
HELIX 142 142 ALA I 341 GLY I 351 1 11
HELIX 143 143 SER I 360 ARG I 373 1 14
HELIX 144 144 THR I 377 LEU I 389 1 13
HELIX 145 149 SER J 5 ALA J 16 1 12
HELIX 146 150 SER J 21 ALA J 41 1 21
HELIX 147 151 PRO J 67 ALA J 73 1 7
SHEET 1 A 6 GLU A 15 ASP A 27 0
SHEET 2 A 6 GLN A 32 ASP A 38 -1 O LEU A 35 N TRP A 24
SHEET 3 A 6 GLY A 41 THR A 47 -1 O VAL A 45 N LEU A 34
SHEET 4 A 6 LEU A 75 SER A 86 1 O ALA A 79 N VAL A 46
SHEET 5 A 6 ALA A 58 GLU A 67 -1 N ARG A 62 O LYS A 80
SHEET 6 A 6 GLU A 15 ASP A 27 -1 N GLY A 20 O LEU A 59
SHEET 1 B 8 THR A 145 GLU A 146 0
SHEET 2 B 8 ARG A 192 VAL A 199 1 O ARG A 192 N THR A 145
SHEET 3 B 8 TYR A 214 GLY A 222 -1 O GLU A 220 N VAL A 193
SHEET 4 B 8 HIS A 387 GLY A 393 -1 O PHE A 390 N VAL A 219
SHEET 5 B 8 LEU A 344 GLN A 351 -1 N ILE A 346 O GLY A 393
SHEET 6 B 8 SER A 336 PHE A 341 -1 N LEU A 339 O THR A 347
SHEET 7 B 8 TRP A 311 THR A 315 -1 N LEU A 312 O LEU A 340
SHEET 8 B 8 ARG A 269 THR A 271 1 N LEU A 270 O PHE A 313
SHEET 1 C 6 GLU B 15 ASP B 27 0
SHEET 2 C 6 GLN B 32 ASP B 38 -1 O LEU B 35 N TRP B 24
SHEET 3 C 6 GLY B 41 THR B 47 -1 O VAL B 45 N LEU B 34
SHEET 4 C 6 LEU B 75 SER B 86 1 O VAL B 77 N VAL B 46
SHEET 5 C 6 ALA B 58 GLU B 67 -1 N ARG B 62 O LYS B 80
SHEET 6 C 6 GLU B 15 ASP B 27 -1 N LEU B 18 O VAL B 61
SHEET 1 D 8 THR B 145 GLU B 146 0
SHEET 2 D 8 ARG B 192 VAL B 199 1 O ARG B 192 N THR B 145
SHEET 3 D 8 TYR B 214 GLY B 222 -1 O GLU B 220 N VAL B 193
SHEET 4 D 8 HIS B 387 GLY B 393 -1 O PHE B 390 N VAL B 219
SHEET 5 D 8 LEU B 344 GLN B 351 -1 N ILE B 346 O GLY B 393
SHEET 6 D 8 THR B 333 PHE B 341 -1 N PHE B 337 O GLY B 349
SHEET 7 D 8 PHE B 313 PRO B 318 -1 N VAL B 314 O ASP B 338
SHEET 8 D 8 ARG B 269 THR B 271 1 N LEU B 270 O THR B 315
SHEET 1 E 6 GLU C 15 ASP C 27 0
SHEET 2 E 6 GLN C 32 ASP C 38 -1 O LEU C 35 N TRP C 24
SHEET 3 E 6 GLY C 41 THR C 47 -1 O VAL C 45 N LEU C 34
SHEET 4 E 6 LEU C 75 SER C 86 1 O ALA C 79 N VAL C 46
SHEET 5 E 6 ALA C 58 GLU C 67 -1 N ARG C 62 O LYS C 80
SHEET 6 E 6 GLU C 15 ASP C 27 -1 N GLY C 20 O LEU C 59
SHEET 1 F 8 THR C 145 GLU C 146 0
SHEET 2 F 8 ARG C 192 VAL C 199 1 O ARG C 192 N THR C 145
SHEET 3 F 8 TYR C 214 GLY C 222 -1 O GLU C 220 N VAL C 193
SHEET 4 F 8 HIS C 387 GLY C 393 -1 O PHE C 390 N VAL C 219
SHEET 5 F 8 LEU C 344 GLN C 351 -1 N ILE C 346 O GLY C 393
SHEET 6 F 8 SER C 336 PHE C 341 -1 N LEU C 339 O THR C 347
SHEET 7 F 8 TRP C 311 THR C 315 -1 N LEU C 312 O LEU C 340
SHEET 8 F 8 ARG C 269 THR C 271 1 N LEU C 270 O PHE C 313
SHEET 1 G 6 GLU D 15 ASP D 27 0
SHEET 2 G 6 GLN D 32 ASP D 38 -1 O LEU D 35 N TRP D 24
SHEET 3 G 6 GLY D 41 THR D 47 -1 O VAL D 45 N LEU D 34
SHEET 4 G 6 LEU D 75 SER D 86 1 O VAL D 77 N VAL D 46
SHEET 5 G 6 ALA D 58 GLU D 67 -1 N ARG D 62 O LYS D 80
SHEET 6 G 6 GLU D 15 ASP D 27 -1 N LEU D 18 O VAL D 61
SHEET 1 H 8 THR D 145 GLU D 146 0
SHEET 2 H 8 ARG D 192 VAL D 199 1 O ARG D 192 N THR D 145
SHEET 3 H 8 TYR D 214 GLY D 222 -1 O GLU D 220 N VAL D 193
SHEET 4 H 8 HIS D 387 GLY D 393 -1 O PHE D 390 N VAL D 219
SHEET 5 H 8 LEU D 344 GLN D 351 -1 N ILE D 346 O GLY D 393
SHEET 6 H 8 THR D 333 PHE D 341 -1 N PHE D 337 O GLY D 349
SHEET 7 H 8 PHE D 313 PRO D 318 -1 N VAL D 314 O ASP D 338
SHEET 8 H 8 ARG D 269 THR D 271 1 N LEU D 270 O THR D 315
SHEET 1 I11 PHE E 38 LEU E 41 0
SHEET 2 I11 LEU E 104 THR E 109 -1 O LYS E 108 N LEU E 39
SHEET 3 I11 VAL E 62 LYS E 66 1 N VAL E 65 O THR E 109
SHEET 4 I11 LEU E 156 ASP E 161 1 O LEU E 158 N ALA E 64
SHEET 5 I11 GLN E 199 ALA E 204 -1 O GLY E 201 N GLY E 159
SHEET 6 I11 TYR E 176 LYS E 179 -1 N TYR E 176 O ALA E 204
SHEET 7 I11 ALA E 420 GLU E 428 -1 O ALA E 420 N LYS E 179
SHEET 8 I11 LEU E 431 LEU E 438 -1 O LEU E 437 N LEU E 421
SHEET 9 I11 LEU E 381 PRO E 385 -1 N LEU E 384 O GLN E 436
SHEET 10 I11 ARG E 246 VAL E 250 1 N GLY E 248 O LEU E 381
SHEET 11 I11 SER E 278 VAL E 282 1 O VAL E 282 N VAL E 249
SHEET 1 J 4 ALA F 68 GLU F 69 0
SHEET 2 J 4 GLY F 100 GLY F 102 -1 O ARG F 101 N GLU F 69
SHEET 3 J 4 ARG F 110 GLU F 121 -1 O LYS F 115 N GLY F 102
SHEET 4 J 4 SER F 104 LEU F 107 -1 N LEU F 107 O ARG F 110
SHEET 1 K 8 ALA F 68 GLU F 69 0
SHEET 2 K 8 GLY F 100 GLY F 102 -1 O ARG F 101 N GLU F 69
SHEET 3 K 8 ARG F 110 GLU F 121 -1 O LYS F 115 N GLY F 102
SHEET 4 K 8 PRO F 143 THR F 149 -1 O LEU F 144 N GLU F 120
SHEET 5 K 8 ALA F 4 HIS F 13 -1 N LEU F 8 O THR F 149
SHEET 6 K 8 LEU F 185 VAL F 193 -1 O SER F 192 N VAL F 5
SHEET 7 K 8 VAL F 204 LEU F 209 -1 O VAL F 204 N VAL F 191
SHEET 8 K 8 THR F 240 MET F 241 1 O MET F 241 N GLU F 205
SHEET 1 L 2 ARG F 73 LEU F 74 0
SHEET 2 L 2 VAL F 273 ALA F 274 -1 O VAL F 273 N LEU F 74
SHEET 1 M 3 TYR F 90 SER F 93 0
SHEET 2 M 3 HIS F 77 ASN F 80 -1 N HIS F 77 O SER F 93
SHEET 3 M 3 PHE F 265 PRO F 266 -1 O PHE F 265 N ARG F 78
SHEET 1 N 4 LYS F 125 LEU F 129 0
SHEET 2 N 4 ARG F 132 ASP F 136 -1 O ASP F 136 N LYS F 125
SHEET 3 N 4 PHE G 82 VAL G 85 -1 O VAL G 85 N THR F 133
SHEET 4 N 4 ALA G 78 GLU G 79 -1 N GLU G 79 O PHE G 82
SHEET 1 O 2 PHE F 243 GLU F 244 0
SHEET 2 O 2 LYS F 249 THR F 250 -1 O LYS F 249 N GLU F 244
SHEET 1 P11 PHE H 38 LEU H 41 0
SHEET 2 P11 LEU H 104 THR H 109 -1 O LYS H 108 N LEU H 39
SHEET 3 P11 VAL H 62 LYS H 66 1 N VAL H 65 O THR H 109
SHEET 4 P11 LEU H 156 ASP H 161 1 O LEU H 158 N ALA H 64
SHEET 5 P11 GLN H 199 ALA H 204 -1 O GLY H 201 N GLY H 159
SHEET 6 P11 TYR H 176 LYS H 179 -1 N TYR H 176 O ALA H 204
SHEET 7 P11 ALA H 420 PHE H 427 -1 O ALA H 420 N LYS H 179
SHEET 8 P11 PRO H 432 LEU H 438 -1 O LEU H 437 N LEU H 421
SHEET 9 P11 LEU H 381 PRO H 385 -1 N LEU H 384 O GLN H 436
SHEET 10 P11 ARG H 246 VAL H 250 1 N GLY H 248 O LEU H 381
SHEET 11 P11 SER H 278 VAL H 282 1 O VAL H 282 N VAL H 249
SHEET 1 Q 4 ALA I 68 GLU I 69 0
SHEET 2 Q 4 GLY I 100 GLY I 102 -1 O ARG I 101 N GLU I 69
SHEET 3 Q 4 ARG I 110 GLU I 121 -1 O LYS I 115 N GLY I 102
SHEET 4 Q 4 SER I 104 LEU I 107 -1 N LEU I 105 O VAL I 112
SHEET 1 R 8 ALA I 68 GLU I 69 0
SHEET 2 R 8 GLY I 100 GLY I 102 -1 O ARG I 101 N GLU I 69
SHEET 3 R 8 ARG I 110 GLU I 121 -1 O LYS I 115 N GLY I 102
SHEET 4 R 8 PRO I 143 THR I 149 -1 O LEU I 144 N GLU I 120
SHEET 5 R 8 ALA I 4 HIS I 13 -1 N LEU I 8 O THR I 149
SHEET 6 R 8 LEU I 185 VAL I 193 -1 O SER I 192 N VAL I 5
SHEET 7 R 8 VAL I 204 LEU I 209 -1 O VAL I 204 N VAL I 191
SHEET 8 R 8 THR I 240 MET I 241 1 O MET I 241 N GLU I 205
SHEET 1 S 2 ARG I 73 LEU I 74 0
SHEET 2 S 2 VAL I 273 ALA I 274 -1 O VAL I 273 N LEU I 74
SHEET 1 T 3 TYR I 90 SER I 93 0
SHEET 2 T 3 HIS I 77 ASN I 80 -1 N HIS I 77 O SER I 93
SHEET 3 T 3 PHE I 265 PRO I 266 -1 O PHE I 265 N ARG I 78
SHEET 1 U 4 LYS I 125 LEU I 129 0
SHEET 2 U 4 ARG I 132 ASP I 136 -1 O ASP I 136 N LYS I 125
SHEET 3 U 4 PHE J 82 VAL J 85 -1 O VAL J 85 N THR I 133
SHEET 4 U 4 ALA J 78 GLU J 79 -1 N GLU J 79 O PHE J 82
SHEET 1 V 2 PHE I 243 GLU I 244 0
SHEET 2 V 2 LYS I 249 THR I 250 -1 O LYS I 249 N GLU I 244
LINK O3' G K 19 P H2U K 20 1555 1555 1.60
LINK O3' H2U K 20 P A K 21 1555 1555 1.61
LINK O3' G K 53 P 5MU K 54 1555 1555 1.60
LINK O3' 5MU K 54 P PSU K 55 1555 1555 1.60
LINK O3' PSU K 55 P C K 56 1555 1555 1.61
LINK O3' G L 19 P H2U L 20 1555 1555 1.61
LINK O3' H2U L 20 P A L 21 1555 1555 1.61
LINK O3' G L 53 P 5MU L 54 1555 1555 1.61
LINK O3' 5MU L 54 P PSU L 55 1555 1555 1.60
LINK O3' PSU L 55 P C L 56 1555 1555 1.60
LINK O3' G M 19 P H2U M 20 1555 1555 1.61
LINK O3' H2U M 20 P A M 21 1555 1555 1.60
LINK O3' G M 53 P 5MU M 54 1555 1555 1.61
LINK O3' 5MU M 54 P PSU M 55 1555 1555 1.61
LINK O3' PSU M 55 P C M 56 1555 1555 1.61
LINK O3' G N 19 P H2U N 20 1555 1555 1.61
LINK O3' H2U N 20 P A N 21 1555 1555 1.60
LINK O3' G N 53 P 5MU N 54 1555 1555 1.61
LINK O3' 5MU N 54 P PSU N 55 1555 1555 1.61
LINK O3' PSU N 55 P C N 56 1555 1555 1.61
LINK SG CYS F 22 ZN ZN F 673 1555 1555 2.19
LINK SG CYS F 24 ZN ZN F 673 1555 1555 2.13
LINK SG CYS F 38 ZN ZN F 673 1555 1555 2.16
LINK SG CYS F 41 ZN ZN F 673 1555 1555 2.02
LINK OE1 GLU F 120 MG MG F 674 1555 1555 2.18
LINK OE2 GLU F 120 MG MG F 674 1555 1555 2.37
LINK OE1 GLU F 146 MG MG F 674 1555 1555 2.19
LINK MG MG F 674 O HOH F 675 1555 1555 2.07
LINK MG MG F 674 O HOH F 676 1555 1555 2.07
LINK MG MG F 674 O HOH F 677 1555 1555 2.08
LINK SG CYS I 22 ZN ZN I 467 1555 1555 2.11
LINK SG CYS I 24 ZN ZN I 467 1555 1555 2.10
LINK SG CYS I 38 ZN ZN I 467 1555 1555 2.19
LINK SG CYS I 41 ZN ZN I 467 1555 1555 1.99
LINK OE1 GLU I 120 MG MG I 468 1555 1555 2.33
LINK OE2 GLU I 120 MG MG I 468 1555 1555 2.48
LINK OE1 GLU I 146 MG MG I 468 1555 1555 2.02
LINK MG MG I 468 O HOH I 469 1555 1555 2.10
LINK MG MG I 468 O HOH I 470 1555 1555 2.08
LINK MG MG I 468 O HOH I 471 1555 1555 2.08
CISPEP 1 GLU A 99 GLU A 100 0 5.86
CISPEP 2 GLU B 99 GLU B 100 0 3.57
CISPEP 3 GLU C 99 GLU C 100 0 5.73
CISPEP 4 GLU D 99 GLU D 100 0 3.51
CISPEP 5 GLY E 140 SER E 141 0 6.02
CISPEP 6 LEU E 242 PRO E 243 0 15.66
CISPEP 7 PRO E 243 PRO E 244 0 -3.27
CISPEP 8 MET F 1 TYR F 2 0 -1.58
CISPEP 9 VAL F 196 GLY F 197 0 0.59
CISPEP 10 GLY F 197 GLU F 198 0 1.48
CISPEP 11 UNK F 645 UNK F 646 0 -3.04
CISPEP 12 GLY H 140 SER H 141 0 6.41
CISPEP 13 LEU H 242 PRO H 243 0 16.05
CISPEP 14 PRO H 243 PRO H 244 0 -3.13
CISPEP 15 UNK I 643 UNK I 644 0 0.15
SITE 1 AC1 4 CYS F 22 CYS F 24 CYS F 38 CYS F 41
SITE 1 AC2 6 HIS F 11 GLU F 120 GLU F 146 HOH F 675
SITE 2 AC2 6 HOH F 676 HOH F 677
SITE 1 AC3 4 CYS I 22 CYS I 24 CYS I 38 CYS I 41
SITE 1 AC4 6 HIS I 11 GLU I 120 GLU I 146 HOH I 469
SITE 2 AC4 6 HOH I 470 HOH I 471
CRYST1 115.920 214.000 127.840 90.00 93.36 90.00 P 1 21 1 8
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 0.008627 0.000000 0.000506 0.00000
SCALE2 0.000000 0.004673 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007836 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
