HEADER HYDROLASE/MOTOR PROTEIN 02-NOV-15 5B0O
TITLE STRUCTURE OF THE FLIH-FLII COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAGELLUM-SPECIFIC ATP SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.6.3.14;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FLAGELLAR ASSEMBLY PROTEIN FLIH;
COMPND 8 CHAIN: E, F, G, H, I, J, K, L;
COMPND 9 FRAGMENT: UNP RESIDUES 99-235;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 /
SOURCE 3 ATCC 700720);
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 6 GENE: FLII, FLA AIII, FLAC, STM1972;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 13 ORGANISM_TAXID: 99287;
SOURCE 14 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 15 GENE: FLIH, FLA AII.3, FLA BIII, STM1971;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACTERIAL FLAGELLUM, TYPE III SECRETION, ATPASE, PERIPHERAL STALK,
KEYWDS 2 HYDROLASE-MOTOR PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.IMADA,Y.UCHIDA,M.KINOSHITA,K.NAMBA,T.MINAMINO
REVDAT 4 08-NOV-23 5B0O 1 REMARK
REVDAT 3 18-APR-18 5B0O 1 JRNL REMARK
REVDAT 2 20-APR-16 5B0O 1 JRNL
REVDAT 1 23-MAR-16 5B0O 0
JRNL AUTH K.IMADA,T.MINAMINO,Y.UCHIDA,M.KINOSHITA,K.NAMBA
JRNL TITL INSIGHT INTO THE FLAGELLA TYPE III EXPORT REVEALED BY THE
JRNL TITL 2 COMPLEX STRUCTURE OF THE TYPE III ATPASE AND ITS REGULATOR
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 3633 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26984495
JRNL DOI 10.1073/PNAS.1524025113
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.UCHIDA,T.MINAMINO,K.NAMBA,K.IMADA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
REMARK 1 TITL 2 FLIH-FLII COMPLEX RESPONSIBLE FOR BACTERIAL FLAGELLAR TYPE
REMARK 1 TITL 3 III PROTEIN EXPORT.
REMARK 1 REF ACTA CRYSTALLOGR. SECT. F V. 68 1311 2012
REMARK 1 REF 2 STRUCT. BIOL. CRYST. COMMUN.
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 23143238
REMARK 1 DOI 10.1107/S1744309112030801
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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) : 51.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 64990
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3292
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 51.3227 - 8.6404 0.91 2523 138 0.1823 0.2049
REMARK 3 2 8.6404 - 6.8634 0.98 2612 148 0.1842 0.2342
REMARK 3 3 6.8634 - 5.9973 0.99 2595 150 0.2276 0.2990
REMARK 3 4 5.9973 - 5.4496 0.99 2577 141 0.2049 0.2389
REMARK 3 5 5.4496 - 5.0594 0.99 2588 137 0.1902 0.2167
REMARK 3 6 5.0594 - 4.7613 1.00 2577 157 0.1698 0.1963
REMARK 3 7 4.7613 - 4.5230 1.00 2591 136 0.1662 0.2498
REMARK 3 8 4.5230 - 4.3262 1.00 2554 137 0.1685 0.2486
REMARK 3 9 4.3262 - 4.1598 1.00 2610 136 0.1809 0.2179
REMARK 3 10 4.1598 - 4.0163 1.00 2581 138 0.1909 0.2577
REMARK 3 11 4.0163 - 3.8907 1.00 2600 126 0.2136 0.2852
REMARK 3 12 3.8907 - 3.7796 1.00 2549 146 0.2106 0.2725
REMARK 3 13 3.7796 - 3.6801 1.00 2576 118 0.2788 0.3346
REMARK 3 14 3.6801 - 3.5903 1.00 2564 136 0.3700 0.4179
REMARK 3 15 3.5903 - 3.5087 1.00 2608 116 0.2764 0.3484
REMARK 3 16 3.5087 - 3.4341 1.00 2532 141 0.2523 0.3072
REMARK 3 17 3.4341 - 3.3654 1.00 2571 134 0.2490 0.3295
REMARK 3 18 3.3654 - 3.3019 1.00 2575 143 0.2494 0.3290
REMARK 3 19 3.3019 - 3.2429 1.00 2538 149 0.2434 0.3230
REMARK 3 20 3.2429 - 3.1880 1.00 2569 130 0.2527 0.3270
REMARK 3 21 3.1880 - 3.1366 1.00 2553 142 0.2446 0.3229
REMARK 3 22 3.1366 - 3.0883 1.00 2562 146 0.2611 0.3003
REMARK 3 23 3.0883 - 3.0429 1.00 2531 122 0.2676 0.3377
REMARK 3 24 3.0429 - 3.0000 0.99 2562 125 0.2949 0.3880
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.27
REMARK 3 B_SOL : 37.27
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.960
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.800
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) : -5.27680
REMARK 3 B22 (A**2) : 9.03960
REMARK 3 B33 (A**2) : -3.76280
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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 : 0.005 22369
REMARK 3 ANGLE : 0.998 30354
REMARK 3 CHIRALITY : 0.066 3476
REMARK 3 PLANARITY : 0.005 3990
REMARK 3 DIHEDRAL : 15.961 8410
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 5B0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1300000305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 40
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65054
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2DPY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5%(W/V) PEG400, 0.1M HEPES PH7.2 AND
REMARK 280 100MM MAGNESIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 66.83100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.11650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 73.65250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.11650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.83100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 73.65250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 98
REMARK 465 GLY A 99
REMARK 465 HIS A 100
REMARK 465 GLY A 101
REMARK 465 ASP A 102
REMARK 465 GLY A 103
REMARK 465 LEU A 104
REMARK 465 GLN A 105
REMARK 465 SER A 106
REMARK 465 VAL A 456
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 ASN C 98
REMARK 465 GLY C 99
REMARK 465 HIS C 100
REMARK 465 GLY C 101
REMARK 465 ASP C 102
REMARK 465 GLY C 103
REMARK 465 LEU C 104
REMARK 465 GLN C 105
REMARK 465 SER C 106
REMARK 465 GLY C 107
REMARK 465 MET D 1
REMARK 465 VAL D 456
REMARK 465 GLY E 96
REMARK 465 SER E 97
REMARK 465 HIS E 98
REMARK 465 ALA E 99
REMARK 465 LEU E 235
REMARK 465 GLY F 96
REMARK 465 SER F 97
REMARK 465 HIS F 98
REMARK 465 ALA F 99
REMARK 465 PRO F 100
REMARK 465 ILE F 101
REMARK 465 HIS F 102
REMARK 465 ALA F 103
REMARK 465 ARG F 104
REMARK 465 MET F 105
REMARK 465 GLN F 106
REMARK 465 GLN F 107
REMARK 465 VAL F 234
REMARK 465 LEU F 235
REMARK 465 GLY G 96
REMARK 465 SER G 97
REMARK 465 HIS G 98
REMARK 465 ALA G 99
REMARK 465 GLY H 96
REMARK 465 SER H 97
REMARK 465 HIS H 98
REMARK 465 ALA H 99
REMARK 465 GLY I 96
REMARK 465 SER I 97
REMARK 465 HIS I 98
REMARK 465 ALA I 99
REMARK 465 GLY I 233
REMARK 465 VAL I 234
REMARK 465 LEU I 235
REMARK 465 GLY J 96
REMARK 465 SER J 97
REMARK 465 HIS J 98
REMARK 465 ALA J 99
REMARK 465 GLY J 233
REMARK 465 VAL J 234
REMARK 465 LEU J 235
REMARK 465 GLY K 96
REMARK 465 SER K 97
REMARK 465 HIS K 98
REMARK 465 ALA K 99
REMARK 465 GLY K 233
REMARK 465 VAL K 234
REMARK 465 LEU K 235
REMARK 465 GLY L 96
REMARK 465 SER L 97
REMARK 465 HIS L 98
REMARK 465 ALA L 99
REMARK 465 THR L 142
REMARK 465 PRO L 143
REMARK 465 GLU L 212
REMARK 465 GLY L 213
REMARK 465 ASP L 214
REMARK 465 LEU L 215
REMARK 465 GLY L 233
REMARK 465 VAL L 234
REMARK 465 LEU L 235
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 NH1 ARG C 387 OD1 ASP C 450 1.93
REMARK 500 NH1 ARG I 194 OD2 ASP I 211 1.94
REMARK 500 O ALA A 196 NH1 ARG A 231 1.96
REMARK 500 O VAL B 163 ND2 ASN B 167 1.97
REMARK 500 O VAL G 172 N ASP G 198 2.01
REMARK 500 NH2 ARG A 197 O ILE A 436 2.01
REMARK 500 O VAL C 163 ND2 ASN C 167 2.01
REMARK 500 NH2 ARG D 4 OD1 ASP H 117 2.03
REMARK 500 O ASN C 167 OG1 THR C 171 2.07
REMARK 500 OE1 GLN G 113 NH1 ARG K 104 2.08
REMARK 500 NH1 ARG D 7 OD2 ASP H 120 2.09
REMARK 500 NH1 ARG L 126 OE1 GLN L 129 2.10
REMARK 500 NH1 ARG F 222 O VAL J 138 2.11
REMARK 500 NZ LYS D 188 OD2 ASP D 272 2.11
REMARK 500 O ASP D 333 NE2 GLN D 335 2.11
REMARK 500 OE1 GLN F 137 NE2 GLN J 153 2.13
REMARK 500 NH2 ARG B 119 O PRO B 132 2.13
REMARK 500 O GLN L 159 OG SER L 165 2.13
REMARK 500 NH1 ARG G 222 O VAL K 138 2.14
REMARK 500 NH2 ARG J 171 O GLY J 213 2.14
REMARK 500 OE1 GLU C 16 NH1 ARG K 126 2.14
REMARK 500 NH1 ARG A 7 OD2 ASP E 120 2.14
REMARK 500 O SER C 184 NH2 ARG C 355 2.15
REMARK 500 OD1 ASP B 13 NH2 ARG J 126 2.17
REMARK 500 OD1 ASP J 198 OG1 THR J 200 2.18
REMARK 500 OG SER B 189 O2B ADP B 601 2.19
REMARK 500 O ALA J 217 OG1 THR J 221 2.19
REMARK 500 OE1 GLU D 66 NH1 ARG D 97 2.19
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 OE2 GLU B 331 NH2 ARG L 196 3445 2.08
REMARK 500 OD2 ASP B 13 OG SER K 121 1655 2.10
REMARK 500 O SER J 125 OG SER K 125 1655 2.15
REMARK 500 OG1 THR A 6 OD1 ASN L 114 1655 2.16
REMARK 500 N GLY B 332 OD1 ASP L 211 3445 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 338 C - N - CA ANGL. DEV. = 10.2 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 THR A 294 -77.60 -84.98
REMARK 500 ASP A 334 -154.44 -157.34
REMARK 500 GLN A 335 -4.33 96.73
REMARK 500 ILE A 452 -75.98 -90.55
REMARK 500 PHE A 453 -71.30 -76.31
REMARK 500 THR B 35 -66.58 -102.33
REMARK 500 PRO B 60 47.69 -79.95
REMARK 500 ILE B 223 -61.00 -123.57
REMARK 500 PRO B 238 -178.12 -67.18
REMARK 500 THR B 294 -86.70 -58.50
REMARK 500 HIS B 317 -75.17 -55.53
REMARK 500 ASP B 415 71.43 57.54
REMARK 500 ILE B 452 -77.39 -93.31
REMARK 500 PRO C 60 47.30 -85.01
REMARK 500 GLU C 156 -63.38 -129.28
REMARK 500 GLU C 221 -62.16 -97.35
REMARK 500 ILE C 223 -64.59 -123.19
REMARK 500 PRO C 238 -179.85 -63.58
REMARK 500 LYS C 295 -74.72 -49.97
REMARK 500 ALA C 409 -122.28 41.53
REMARK 500 LYS C 412 -132.84 43.93
REMARK 500 ILE C 452 -76.14 -51.40
REMARK 500 PHE C 453 44.85 -142.25
REMARK 500 THR D 32 -61.52 -101.59
REMARK 500 PRO D 60 49.29 -88.41
REMARK 500 PHE D 453 -166.72 -128.55
REMARK 500 MET F 183 -73.05 -112.86
REMARK 500 HIS G 102 -61.27 -97.28
REMARK 500 SER G 165 -77.82 -94.38
REMARK 500 LYS G 167 57.03 26.72
REMARK 500 PRO H 143 -175.80 -67.15
REMARK 500 GLU H 182 -79.00 -81.34
REMARK 500 ASP J 211 -126.04 60.34
REMARK 500 ALA L 231 -179.63 -66.83
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 ASP A 333 ASP A 334 -145.54
REMARK 500 ILE C 452 PHE C 453 147.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP D 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DPY RELATED DB: PDB
DBREF 5B0O A 1 456 UNP P26465 FLII_SALTY 1 456
DBREF 5B0O B 1 456 UNP P26465 FLII_SALTY 1 456
DBREF 5B0O C 1 456 UNP P26465 FLII_SALTY 1 456
DBREF 5B0O D 1 456 UNP P26465 FLII_SALTY 1 456
DBREF 5B0O E 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O F 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O G 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O H 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O I 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O J 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O K 99 235 UNP P15934 FLIH_SALTY 99 235
DBREF 5B0O L 99 235 UNP P15934 FLIH_SALTY 99 235
SEQADV 5B0O GLY E 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER E 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS E 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY F 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER F 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS F 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY G 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER G 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS G 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY H 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER H 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS H 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY I 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER I 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS I 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY J 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER J 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS J 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY K 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER K 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS K 98 UNP P15934 EXPRESSION TAG
SEQADV 5B0O GLY L 96 UNP P15934 EXPRESSION TAG
SEQADV 5B0O SER L 97 UNP P15934 EXPRESSION TAG
SEQADV 5B0O HIS L 98 UNP P15934 EXPRESSION TAG
SEQRES 1 A 456 MET THR THR ARG LEU THR ARG TRP LEU THR ALA LEU ASP
SEQRES 2 A 456 ASN PHE GLU ALA LYS MET ALA LEU LEU PRO ALA VAL ARG
SEQRES 3 A 456 ARG TYR GLY ARG LEU THR ARG ALA THR GLY LEU VAL LEU
SEQRES 4 A 456 GLU ALA THR GLY LEU GLN LEU PRO LEU GLY ALA THR CYS
SEQRES 5 A 456 ILE ILE GLU ARG GLN ASP GLY PRO GLU THR LYS GLU VAL
SEQRES 6 A 456 GLU SER GLU VAL VAL GLY PHE ASN GLY GLN ARG LEU PHE
SEQRES 7 A 456 LEU MET PRO LEU GLU GLU VAL GLU GLY ILE LEU PRO GLY
SEQRES 8 A 456 ALA ARG VAL TYR ALA ARG ASN GLY HIS GLY ASP GLY LEU
SEQRES 9 A 456 GLN SER GLY LYS GLN LEU PRO LEU GLY PRO ALA LEU LEU
SEQRES 10 A 456 GLY ARG VAL LEU ASP GLY GLY GLY LYS PRO LEU ASP GLY
SEQRES 11 A 456 LEU PRO ALA PRO ASP THR LEU GLU THR GLY ALA LEU ILE
SEQRES 12 A 456 THR PRO PRO PHE ASN PRO LEU GLN ARG THR PRO ILE GLU
SEQRES 13 A 456 HIS VAL LEU ASP THR GLY VAL ARG ALA ILE ASN ALA LEU
SEQRES 14 A 456 LEU THR VAL GLY ARG GLY GLN ARG MET GLY LEU PHE ALA
SEQRES 15 A 456 GLY SER GLY VAL GLY LYS SER VAL LEU LEU GLY MET MET
SEQRES 16 A 456 ALA ARG TYR THR ARG ALA ASP VAL ILE VAL VAL GLY LEU
SEQRES 17 A 456 ILE GLY GLU ARG GLY ARG GLU VAL LYS ASP PHE ILE GLU
SEQRES 18 A 456 ASN ILE LEU GLY PRO ASP GLY ARG ALA ARG SER VAL VAL
SEQRES 19 A 456 ILE ALA ALA PRO ALA ASP VAL SER PRO LEU LEU ARG MET
SEQRES 20 A 456 GLN GLY ALA ALA TYR ALA THR ARG ILE ALA GLU ASP PHE
SEQRES 21 A 456 ARG ASP ARG GLY GLN HIS VAL LEU LEU ILE MET ASP SER
SEQRES 22 A 456 LEU THR ARG TYR ALA MET ALA GLN ARG GLU ILE ALA LEU
SEQRES 23 A 456 ALA ILE GLY GLU PRO PRO ALA THR LYS GLY TYR PRO PRO
SEQRES 24 A 456 SER VAL PHE ALA LYS LEU PRO ALA LEU VAL GLU ARG ALA
SEQRES 25 A 456 GLY ASN GLY ILE HIS GLY GLY GLY SER ILE THR ALA PHE
SEQRES 26 A 456 TYR THR VAL LEU THR GLU GLY ASP ASP GLN GLN ASP PRO
SEQRES 27 A 456 ILE ALA ASP SER ALA ARG ALA ILE LEU ASP GLY HIS ILE
SEQRES 28 A 456 VAL LEU SER ARG ARG LEU ALA GLU ALA GLY HIS TYR PRO
SEQRES 29 A 456 ALA ILE ASP ILE GLU ALA SER ILE SER ARG ALA MET THR
SEQRES 30 A 456 ALA LEU ILE THR GLU GLN HIS TYR ALA ARG VAL ARG LEU
SEQRES 31 A 456 PHE LYS GLN LEU LEU SER SER PHE GLN ARG ASN ARG ASP
SEQRES 32 A 456 LEU VAL SER VAL GLY ALA TYR ALA LYS GLY SER ASP PRO
SEQRES 33 A 456 MET LEU ASP LYS ALA ILE THR LEU TRP PRO GLN LEU GLU
SEQRES 34 A 456 ALA PHE LEU GLN GLN GLY ILE PHE GLU ARG ALA ASP TRP
SEQRES 35 A 456 GLU ASP SER LEU GLN ALA LEU ASP LEU ILE PHE PRO THR
SEQRES 36 A 456 VAL
SEQRES 1 B 456 MET THR THR ARG LEU THR ARG TRP LEU THR ALA LEU ASP
SEQRES 2 B 456 ASN PHE GLU ALA LYS MET ALA LEU LEU PRO ALA VAL ARG
SEQRES 3 B 456 ARG TYR GLY ARG LEU THR ARG ALA THR GLY LEU VAL LEU
SEQRES 4 B 456 GLU ALA THR GLY LEU GLN LEU PRO LEU GLY ALA THR CYS
SEQRES 5 B 456 ILE ILE GLU ARG GLN ASP GLY PRO GLU THR LYS GLU VAL
SEQRES 6 B 456 GLU SER GLU VAL VAL GLY PHE ASN GLY GLN ARG LEU PHE
SEQRES 7 B 456 LEU MET PRO LEU GLU GLU VAL GLU GLY ILE LEU PRO GLY
SEQRES 8 B 456 ALA ARG VAL TYR ALA ARG ASN GLY HIS GLY ASP GLY LEU
SEQRES 9 B 456 GLN SER GLY LYS GLN LEU PRO LEU GLY PRO ALA LEU LEU
SEQRES 10 B 456 GLY ARG VAL LEU ASP GLY GLY GLY LYS PRO LEU ASP GLY
SEQRES 11 B 456 LEU PRO ALA PRO ASP THR LEU GLU THR GLY ALA LEU ILE
SEQRES 12 B 456 THR PRO PRO PHE ASN PRO LEU GLN ARG THR PRO ILE GLU
SEQRES 13 B 456 HIS VAL LEU ASP THR GLY VAL ARG ALA ILE ASN ALA LEU
SEQRES 14 B 456 LEU THR VAL GLY ARG GLY GLN ARG MET GLY LEU PHE ALA
SEQRES 15 B 456 GLY SER GLY VAL GLY LYS SER VAL LEU LEU GLY MET MET
SEQRES 16 B 456 ALA ARG TYR THR ARG ALA ASP VAL ILE VAL VAL GLY LEU
SEQRES 17 B 456 ILE GLY GLU ARG GLY ARG GLU VAL LYS ASP PHE ILE GLU
SEQRES 18 B 456 ASN ILE LEU GLY PRO ASP GLY ARG ALA ARG SER VAL VAL
SEQRES 19 B 456 ILE ALA ALA PRO ALA ASP VAL SER PRO LEU LEU ARG MET
SEQRES 20 B 456 GLN GLY ALA ALA TYR ALA THR ARG ILE ALA GLU ASP PHE
SEQRES 21 B 456 ARG ASP ARG GLY GLN HIS VAL LEU LEU ILE MET ASP SER
SEQRES 22 B 456 LEU THR ARG TYR ALA MET ALA GLN ARG GLU ILE ALA LEU
SEQRES 23 B 456 ALA ILE GLY GLU PRO PRO ALA THR LYS GLY TYR PRO PRO
SEQRES 24 B 456 SER VAL PHE ALA LYS LEU PRO ALA LEU VAL GLU ARG ALA
SEQRES 25 B 456 GLY ASN GLY ILE HIS GLY GLY GLY SER ILE THR ALA PHE
SEQRES 26 B 456 TYR THR VAL LEU THR GLU GLY ASP ASP GLN GLN ASP PRO
SEQRES 27 B 456 ILE ALA ASP SER ALA ARG ALA ILE LEU ASP GLY HIS ILE
SEQRES 28 B 456 VAL LEU SER ARG ARG LEU ALA GLU ALA GLY HIS TYR PRO
SEQRES 29 B 456 ALA ILE ASP ILE GLU ALA SER ILE SER ARG ALA MET THR
SEQRES 30 B 456 ALA LEU ILE THR GLU GLN HIS TYR ALA ARG VAL ARG LEU
SEQRES 31 B 456 PHE LYS GLN LEU LEU SER SER PHE GLN ARG ASN ARG ASP
SEQRES 32 B 456 LEU VAL SER VAL GLY ALA TYR ALA LYS GLY SER ASP PRO
SEQRES 33 B 456 MET LEU ASP LYS ALA ILE THR LEU TRP PRO GLN LEU GLU
SEQRES 34 B 456 ALA PHE LEU GLN GLN GLY ILE PHE GLU ARG ALA ASP TRP
SEQRES 35 B 456 GLU ASP SER LEU GLN ALA LEU ASP LEU ILE PHE PRO THR
SEQRES 36 B 456 VAL
SEQRES 1 C 456 MET THR THR ARG LEU THR ARG TRP LEU THR ALA LEU ASP
SEQRES 2 C 456 ASN PHE GLU ALA LYS MET ALA LEU LEU PRO ALA VAL ARG
SEQRES 3 C 456 ARG TYR GLY ARG LEU THR ARG ALA THR GLY LEU VAL LEU
SEQRES 4 C 456 GLU ALA THR GLY LEU GLN LEU PRO LEU GLY ALA THR CYS
SEQRES 5 C 456 ILE ILE GLU ARG GLN ASP GLY PRO GLU THR LYS GLU VAL
SEQRES 6 C 456 GLU SER GLU VAL VAL GLY PHE ASN GLY GLN ARG LEU PHE
SEQRES 7 C 456 LEU MET PRO LEU GLU GLU VAL GLU GLY ILE LEU PRO GLY
SEQRES 8 C 456 ALA ARG VAL TYR ALA ARG ASN GLY HIS GLY ASP GLY LEU
SEQRES 9 C 456 GLN SER GLY LYS GLN LEU PRO LEU GLY PRO ALA LEU LEU
SEQRES 10 C 456 GLY ARG VAL LEU ASP GLY GLY GLY LYS PRO LEU ASP GLY
SEQRES 11 C 456 LEU PRO ALA PRO ASP THR LEU GLU THR GLY ALA LEU ILE
SEQRES 12 C 456 THR PRO PRO PHE ASN PRO LEU GLN ARG THR PRO ILE GLU
SEQRES 13 C 456 HIS VAL LEU ASP THR GLY VAL ARG ALA ILE ASN ALA LEU
SEQRES 14 C 456 LEU THR VAL GLY ARG GLY GLN ARG MET GLY LEU PHE ALA
SEQRES 15 C 456 GLY SER GLY VAL GLY LYS SER VAL LEU LEU GLY MET MET
SEQRES 16 C 456 ALA ARG TYR THR ARG ALA ASP VAL ILE VAL VAL GLY LEU
SEQRES 17 C 456 ILE GLY GLU ARG GLY ARG GLU VAL LYS ASP PHE ILE GLU
SEQRES 18 C 456 ASN ILE LEU GLY PRO ASP GLY ARG ALA ARG SER VAL VAL
SEQRES 19 C 456 ILE ALA ALA PRO ALA ASP VAL SER PRO LEU LEU ARG MET
SEQRES 20 C 456 GLN GLY ALA ALA TYR ALA THR ARG ILE ALA GLU ASP PHE
SEQRES 21 C 456 ARG ASP ARG GLY GLN HIS VAL LEU LEU ILE MET ASP SER
SEQRES 22 C 456 LEU THR ARG TYR ALA MET ALA GLN ARG GLU ILE ALA LEU
SEQRES 23 C 456 ALA ILE GLY GLU PRO PRO ALA THR LYS GLY TYR PRO PRO
SEQRES 24 C 456 SER VAL PHE ALA LYS LEU PRO ALA LEU VAL GLU ARG ALA
SEQRES 25 C 456 GLY ASN GLY ILE HIS GLY GLY GLY SER ILE THR ALA PHE
SEQRES 26 C 456 TYR THR VAL LEU THR GLU GLY ASP ASP GLN GLN ASP PRO
SEQRES 27 C 456 ILE ALA ASP SER ALA ARG ALA ILE LEU ASP GLY HIS ILE
SEQRES 28 C 456 VAL LEU SER ARG ARG LEU ALA GLU ALA GLY HIS TYR PRO
SEQRES 29 C 456 ALA ILE ASP ILE GLU ALA SER ILE SER ARG ALA MET THR
SEQRES 30 C 456 ALA LEU ILE THR GLU GLN HIS TYR ALA ARG VAL ARG LEU
SEQRES 31 C 456 PHE LYS GLN LEU LEU SER SER PHE GLN ARG ASN ARG ASP
SEQRES 32 C 456 LEU VAL SER VAL GLY ALA TYR ALA LYS GLY SER ASP PRO
SEQRES 33 C 456 MET LEU ASP LYS ALA ILE THR LEU TRP PRO GLN LEU GLU
SEQRES 34 C 456 ALA PHE LEU GLN GLN GLY ILE PHE GLU ARG ALA ASP TRP
SEQRES 35 C 456 GLU ASP SER LEU GLN ALA LEU ASP LEU ILE PHE PRO THR
SEQRES 36 C 456 VAL
SEQRES 1 D 456 MET THR THR ARG LEU THR ARG TRP LEU THR ALA LEU ASP
SEQRES 2 D 456 ASN PHE GLU ALA LYS MET ALA LEU LEU PRO ALA VAL ARG
SEQRES 3 D 456 ARG TYR GLY ARG LEU THR ARG ALA THR GLY LEU VAL LEU
SEQRES 4 D 456 GLU ALA THR GLY LEU GLN LEU PRO LEU GLY ALA THR CYS
SEQRES 5 D 456 ILE ILE GLU ARG GLN ASP GLY PRO GLU THR LYS GLU VAL
SEQRES 6 D 456 GLU SER GLU VAL VAL GLY PHE ASN GLY GLN ARG LEU PHE
SEQRES 7 D 456 LEU MET PRO LEU GLU GLU VAL GLU GLY ILE LEU PRO GLY
SEQRES 8 D 456 ALA ARG VAL TYR ALA ARG ASN GLY HIS GLY ASP GLY LEU
SEQRES 9 D 456 GLN SER GLY LYS GLN LEU PRO LEU GLY PRO ALA LEU LEU
SEQRES 10 D 456 GLY ARG VAL LEU ASP GLY GLY GLY LYS PRO LEU ASP GLY
SEQRES 11 D 456 LEU PRO ALA PRO ASP THR LEU GLU THR GLY ALA LEU ILE
SEQRES 12 D 456 THR PRO PRO PHE ASN PRO LEU GLN ARG THR PRO ILE GLU
SEQRES 13 D 456 HIS VAL LEU ASP THR GLY VAL ARG ALA ILE ASN ALA LEU
SEQRES 14 D 456 LEU THR VAL GLY ARG GLY GLN ARG MET GLY LEU PHE ALA
SEQRES 15 D 456 GLY SER GLY VAL GLY LYS SER VAL LEU LEU GLY MET MET
SEQRES 16 D 456 ALA ARG TYR THR ARG ALA ASP VAL ILE VAL VAL GLY LEU
SEQRES 17 D 456 ILE GLY GLU ARG GLY ARG GLU VAL LYS ASP PHE ILE GLU
SEQRES 18 D 456 ASN ILE LEU GLY PRO ASP GLY ARG ALA ARG SER VAL VAL
SEQRES 19 D 456 ILE ALA ALA PRO ALA ASP VAL SER PRO LEU LEU ARG MET
SEQRES 20 D 456 GLN GLY ALA ALA TYR ALA THR ARG ILE ALA GLU ASP PHE
SEQRES 21 D 456 ARG ASP ARG GLY GLN HIS VAL LEU LEU ILE MET ASP SER
SEQRES 22 D 456 LEU THR ARG TYR ALA MET ALA GLN ARG GLU ILE ALA LEU
SEQRES 23 D 456 ALA ILE GLY GLU PRO PRO ALA THR LYS GLY TYR PRO PRO
SEQRES 24 D 456 SER VAL PHE ALA LYS LEU PRO ALA LEU VAL GLU ARG ALA
SEQRES 25 D 456 GLY ASN GLY ILE HIS GLY GLY GLY SER ILE THR ALA PHE
SEQRES 26 D 456 TYR THR VAL LEU THR GLU GLY ASP ASP GLN GLN ASP PRO
SEQRES 27 D 456 ILE ALA ASP SER ALA ARG ALA ILE LEU ASP GLY HIS ILE
SEQRES 28 D 456 VAL LEU SER ARG ARG LEU ALA GLU ALA GLY HIS TYR PRO
SEQRES 29 D 456 ALA ILE ASP ILE GLU ALA SER ILE SER ARG ALA MET THR
SEQRES 30 D 456 ALA LEU ILE THR GLU GLN HIS TYR ALA ARG VAL ARG LEU
SEQRES 31 D 456 PHE LYS GLN LEU LEU SER SER PHE GLN ARG ASN ARG ASP
SEQRES 32 D 456 LEU VAL SER VAL GLY ALA TYR ALA LYS GLY SER ASP PRO
SEQRES 33 D 456 MET LEU ASP LYS ALA ILE THR LEU TRP PRO GLN LEU GLU
SEQRES 34 D 456 ALA PHE LEU GLN GLN GLY ILE PHE GLU ARG ALA ASP TRP
SEQRES 35 D 456 GLU ASP SER LEU GLN ALA LEU ASP LEU ILE PHE PRO THR
SEQRES 36 D 456 VAL
SEQRES 1 E 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 E 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 E 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 E 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 E 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 E 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 E 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 E 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 E 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 E 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 E 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 F 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 F 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 F 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 F 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 F 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 F 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 F 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 F 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 F 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 F 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 F 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 G 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 G 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 G 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 G 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 G 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 G 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 G 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 G 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 G 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 G 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 G 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 H 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 H 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 H 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 H 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 H 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 H 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 H 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 H 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 H 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 H 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 H 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 I 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 I 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 I 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 I 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 I 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 I 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 I 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 I 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 I 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 I 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 I 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 J 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 J 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 J 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 J 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 J 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 J 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 J 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 J 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 J 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 J 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 J 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 K 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 K 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 K 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 K 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 K 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 K 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 K 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 K 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 K 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 K 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 K 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
SEQRES 1 L 140 GLY SER HIS ALA PRO ILE HIS ALA ARG MET GLN GLN LEU
SEQRES 2 L 140 VAL SER GLU PHE GLN ASN THR LEU ASP ALA LEU ASP SER
SEQRES 3 L 140 VAL ILE ALA SER ARG LEU MET GLN MET ALA LEU GLU ALA
SEQRES 4 L 140 ALA ARG GLN VAL ILE GLY GLN THR PRO ALA VAL ASP ASN
SEQRES 5 L 140 SER ALA LEU ILE LYS GLN ILE GLN GLN LEU LEU GLN GLN
SEQRES 6 L 140 GLU PRO LEU PHE SER GLY LYS PRO GLN LEU ARG VAL HIS
SEQRES 7 L 140 PRO ASP ASP LEU GLN ARG VAL GLU GLU MET LEU GLY ALA
SEQRES 8 L 140 THR LEU SER LEU HIS GLY TRP ARG LEU ARG GLY ASP PRO
SEQRES 9 L 140 THR LEU HIS HIS GLY GLY CYS LYS VAL SER ALA ASP GLU
SEQRES 10 L 140 GLY ASP LEU ASP ALA SER VAL ALA THR ARG TRP GLN GLU
SEQRES 11 L 140 LEU CYS ARG LEU ALA ALA PRO GLY VAL LEU
HET ADP A 601 27
HET ADP B 601 27
HET ADP C 601 27
HET ADP D 601 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 13 ADP 4(C10 H15 N5 O10 P2)
HELIX 1 AA1 THR A 2 ALA A 20 1 19
HELIX 2 AA2 GLY A 113 LEU A 117 5 5
HELIX 3 AA3 ASN A 148 ARG A 152 5 5
HELIX 4 AA4 VAL A 163 LEU A 170 1 8
HELIX 5 AA5 GLY A 187 THR A 199 1 13
HELIX 6 AA6 ARG A 212 ILE A 223 1 12
HELIX 7 AA7 LEU A 224 ALA A 230 1 7
HELIX 8 AA8 SER A 242 ARG A 263 1 22
HELIX 9 AA9 SER A 273 ILE A 288 1 16
HELIX 10 AB1 SER A 300 ARG A 311 1 12
HELIX 11 AB2 ASP A 337 LEU A 347 1 11
HELIX 12 AB3 SER A 354 GLU A 359 1 6
HELIX 13 AB4 ALA A 375 ILE A 380 1 6
HELIX 14 AB5 THR A 381 GLY A 408 1 28
HELIX 15 AB6 ASP A 415 GLN A 433 1 19
HELIX 16 AB7 ASP A 441 PHE A 453 1 13
HELIX 17 AB8 THR B 3 MET B 19 1 17
HELIX 18 AB9 LEU B 104 GLY B 107 5 4
HELIX 19 AC1 GLY B 113 LEU B 117 5 5
HELIX 20 AC2 ASN B 148 ARG B 152 5 5
HELIX 21 AC3 VAL B 163 LEU B 170 1 8
HELIX 22 AC4 GLY B 187 THR B 199 1 13
HELIX 23 AC5 ARG B 212 ILE B 223 1 12
HELIX 24 AC6 LEU B 224 ARG B 231 1 8
HELIX 25 AC7 SER B 242 ASP B 262 1 21
HELIX 26 AC8 SER B 273 ILE B 288 1 16
HELIX 27 AC9 PRO B 298 GLU B 310 1 13
HELIX 28 AD1 ASP B 337 LEU B 347 1 11
HELIX 29 AD2 SER B 354 ALA B 360 1 7
HELIX 30 AD3 ALA B 375 ILE B 380 1 6
HELIX 31 AD4 THR B 381 ASN B 401 1 21
HELIX 32 AD5 ARG B 402 VAL B 407 1 6
HELIX 33 AD6 ASP B 415 GLN B 433 1 19
HELIX 34 AD7 ASP B 441 LEU B 451 1 11
HELIX 35 AD8 THR C 3 ALA C 20 1 18
HELIX 36 AD9 GLY C 113 LEU C 117 5 5
HELIX 37 AE1 VAL C 163 THR C 171 1 9
HELIX 38 AE2 GLY C 187 THR C 199 1 13
HELIX 39 AE3 ARG C 212 ILE C 223 1 12
HELIX 40 AE4 LEU C 224 ALA C 230 1 7
HELIX 41 AE5 SER C 242 ARG C 263 1 22
HELIX 42 AE6 SER C 273 GLY C 289 1 17
HELIX 43 AE7 PRO C 298 ARG C 311 1 14
HELIX 44 AE8 ASP C 337 LEU C 347 1 11
HELIX 45 AE9 SER C 354 ALA C 360 1 7
HELIX 46 AF1 ASP C 367 SER C 371 5 5
HELIX 47 AF2 ALA C 375 ILE C 380 1 6
HELIX 48 AF3 THR C 381 ASN C 401 1 21
HELIX 49 AF4 ASN C 401 VAL C 407 1 7
HELIX 50 AF5 ASP C 415 GLN C 433 1 19
HELIX 51 AF6 ASP C 441 LEU C 451 1 11
HELIX 52 AF7 THR D 3 LEU D 21 1 19
HELIX 53 AF8 GLY D 113 LEU D 117 5 5
HELIX 54 AF9 VAL D 163 LEU D 170 1 8
HELIX 55 AG1 GLY D 187 THR D 199 1 13
HELIX 56 AG2 ARG D 212 ASN D 222 1 11
HELIX 57 AG3 LEU D 224 ARG D 231 1 8
HELIX 58 AG4 SER D 242 ARG D 263 1 22
HELIX 59 AG5 SER D 273 ILE D 288 1 16
HELIX 60 AG6 SER D 300 ALA D 312 1 13
HELIX 61 AG7 ASP D 337 LEU D 347 1 11
HELIX 62 AG8 SER D 354 ALA D 360 1 7
HELIX 63 AG9 ALA D 375 ILE D 380 1 6
HELIX 64 AH1 THR D 381 ASN D 401 1 21
HELIX 65 AH2 ASN D 401 GLY D 408 1 8
HELIX 66 AH3 ASP D 415 GLN D 433 1 19
HELIX 67 AH4 ASP D 441 PHE D 453 1 13
HELIX 68 AH5 ILE E 101 THR E 142 1 42
HELIX 69 AH6 ASN E 147 GLN E 159 1 13
HELIX 70 AH7 HIS E 173 HIS E 191 1 19
HELIX 71 AH8 SER E 218 ALA E 231 1 14
HELIX 72 AH9 SER F 110 THR F 142 1 33
HELIX 73 AI1 ASN F 147 GLN F 160 1 14
HELIX 74 AI2 ASP F 175 GLU F 182 1 8
HELIX 75 AI3 LEU F 184 GLY F 192 1 9
HELIX 76 AI4 SER F 218 ALA F 231 1 14
HELIX 77 AI5 ALA G 103 THR G 142 1 40
HELIX 78 AI6 ASN G 147 GLN G 159 1 13
HELIX 79 AI7 HIS G 173 ASP G 175 5 3
HELIX 80 AI8 ASP G 176 GLY G 192 1 17
HELIX 81 AI9 SER G 218 ALA G 231 1 14
HELIX 82 AJ1 ILE H 101 MET H 105 1 5
HELIX 83 AJ2 MET H 105 ALA H 118 1 14
HELIX 84 AJ3 ALA H 118 THR H 142 1 25
HELIX 85 AJ4 ASN H 147 LEU H 158 1 12
HELIX 86 AJ5 HIS H 173 GLN H 178 1 6
HELIX 87 AJ6 ARG H 179 GLU H 182 5 4
HELIX 88 AJ7 ALA H 186 HIS H 191 1 6
HELIX 89 AJ8 SER H 218 ALA H 231 1 14
HELIX 90 AJ9 ILE I 101 ILE I 123 1 23
HELIX 91 AK1 ILE I 123 GLY I 140 1 18
HELIX 92 AK2 ASP I 146 GLN I 160 1 15
HELIX 93 AK3 GLU I 161 GLY I 166 1 6
HELIX 94 AK4 HIS I 173 HIS I 191 1 19
HELIX 95 AK5 ASP I 214 CYS I 227 1 14
HELIX 96 AK6 ILE J 101 GLY J 140 1 40
HELIX 97 AK7 ASP J 146 GLN J 159 1 14
HELIX 98 AK8 GLU J 161 GLY J 166 1 6
HELIX 99 AK9 ASP J 176 GLY J 192 1 17
HELIX 100 AL1 ASP J 214 CYS J 227 1 14
HELIX 101 AL2 HIS K 102 VAL K 122 1 21
HELIX 102 AL3 VAL K 122 GLY K 140 1 19
HELIX 103 AL4 ASP K 146 GLN K 159 1 14
HELIX 104 AL5 GLU K 161 GLY K 166 1 6
HELIX 105 AL6 HIS K 173 GLY K 185 1 13
HELIX 106 AL7 GLY K 185 GLY K 192 1 8
HELIX 107 AL8 ASP K 214 CYS K 227 1 14
HELIX 108 AL9 ARG L 104 GLY L 140 1 37
HELIX 109 AM1 ASN L 147 GLN L 160 1 14
HELIX 110 AM2 GLU L 161 GLY L 166 1 6
HELIX 111 AM3 ASP L 176 MET L 183 1 8
HELIX 112 AM4 MET L 183 HIS L 191 1 9
HELIX 113 AM5 ALA L 217 CYS L 227 1 11
SHEET 1 AA119 ARG E 194 GLY E 197 0
SHEET 2 AA119 GLN E 169 VAL E 172 1 N LEU E 170 O ARG E 194
SHEET 3 AA119 LYS E 207 SER E 209 -1 O SER E 209 N GLN E 169
SHEET 4 AA119 ASP E 214 ASP E 216 -1 O LEU E 215 N VAL E 208
SHEET 5 AA119 ARG A 26 ALA A 34 -1 N TYR A 28 O ASP E 214
SHEET 6 AA119 LEU A 39 THR A 42 -1 O THR A 42 N ARG A 30
SHEET 7 AA119 ARG A 76 PRO A 81 -1 O LEU A 77 N ALA A 41
SHEET 8 AA119 THR A 62 ASN A 73 -1 N GLY A 71 O PHE A 78
SHEET 9 AA119 THR A 51 GLN A 57 -1 N ILE A 54 O VAL A 65
SHEET 10 AA119 ALA A 92 ALA A 96 -1 O TYR A 95 N ILE A 53
SHEET 11 AA119 ARG A 26 ALA A 34 -1 N LEU A 31 O ALA A 92
SHEET 12 AA119 THR B 62 ASN B 73 -1 O PHE B 72 N ALA A 34
SHEET 13 AA119 THR B 51 GLN B 57 -1 N ARG B 56 O LYS B 63
SHEET 14 AA119 ARG B 93 ALA B 96 -1 O ARG B 93 N GLU B 55
SHEET 15 AA119 ARG B 26 ARG B 33 -1 N GLY B 29 O VAL B 94
SHEET 16 AA119 GLY F 213 ASP F 216 -1 O ASP F 216 N ARG B 26
SHEET 17 AA119 LYS F 207 SER F 209 -1 N VAL F 208 O LEU F 215
SHEET 18 AA119 GLN F 169 ARG F 171 -1 N ARG F 171 O LYS F 207
SHEET 19 AA119 ARG F 194 LEU F 195 1 O ARG F 194 N LEU F 170
SHEET 1 AA219 ARG E 194 GLY E 197 0
SHEET 2 AA219 GLN E 169 VAL E 172 1 N LEU E 170 O ARG E 194
SHEET 3 AA219 LYS E 207 SER E 209 -1 O SER E 209 N GLN E 169
SHEET 4 AA219 ASP E 214 ASP E 216 -1 O LEU E 215 N VAL E 208
SHEET 5 AA219 ARG A 26 ALA A 34 -1 N TYR A 28 O ASP E 214
SHEET 6 AA219 LEU A 39 THR A 42 -1 O THR A 42 N ARG A 30
SHEET 7 AA219 ARG A 76 PRO A 81 -1 O LEU A 77 N ALA A 41
SHEET 8 AA219 THR A 62 ASN A 73 -1 N GLY A 71 O PHE A 78
SHEET 9 AA219 THR A 51 GLN A 57 -1 N ILE A 54 O VAL A 65
SHEET 10 AA219 ALA A 92 ALA A 96 -1 O TYR A 95 N ILE A 53
SHEET 11 AA219 ARG A 26 ALA A 34 -1 N LEU A 31 O ALA A 92
SHEET 12 AA219 THR B 62 ASN B 73 -1 O PHE B 72 N ALA A 34
SHEET 13 AA219 ARG B 76 PRO B 81 -1 O ARG B 76 N ASN B 73
SHEET 14 AA219 LEU B 39 THR B 42 -1 N ALA B 41 O LEU B 77
SHEET 15 AA219 ARG B 26 ARG B 33 -1 N ARG B 30 O THR B 42
SHEET 16 AA219 GLY F 213 ASP F 216 -1 O ASP F 216 N ARG B 26
SHEET 17 AA219 LYS F 207 SER F 209 -1 N VAL F 208 O LEU F 215
SHEET 18 AA219 GLN F 169 ARG F 171 -1 N ARG F 171 O LYS F 207
SHEET 19 AA219 ARG F 194 LEU F 195 1 O ARG F 194 N LEU F 170
SHEET 1 AA3 2 GLN A 109 PRO A 111 0
SHEET 2 AA3 2 THR A 139 ALA A 141 -1 O GLY A 140 N LEU A 110
SHEET 1 AA4 6 VAL A 120 LEU A 121 0
SHEET 2 AA4 6 SER A 232 ALA A 237 1 O ALA A 236 N LEU A 121
SHEET 3 AA4 6 VAL A 203 ILE A 209 1 N LEU A 208 O ILE A 235
SHEET 4 AA4 6 HIS A 266 ASP A 272 1 O ASP A 272 N ILE A 209
SHEET 5 AA4 6 SER A 321 LEU A 329 1 O SER A 321 N VAL A 267
SHEET 6 AA4 6 GLY A 313 ASN A 314 -1 N GLY A 313 O ILE A 322
SHEET 1 AA5 7 VAL A 120 LEU A 121 0
SHEET 2 AA5 7 SER A 232 ALA A 237 1 O ALA A 236 N LEU A 121
SHEET 3 AA5 7 VAL A 203 ILE A 209 1 N LEU A 208 O ILE A 235
SHEET 4 AA5 7 HIS A 266 ASP A 272 1 O ASP A 272 N ILE A 209
SHEET 5 AA5 7 SER A 321 LEU A 329 1 O SER A 321 N VAL A 267
SHEET 6 AA5 7 ARG A 177 ALA A 182 1 N LEU A 180 O VAL A 328
SHEET 7 AA5 7 HIS A 350 VAL A 352 1 O ILE A 351 N GLY A 179
SHEET 1 AA6 2 GLN B 109 LEU B 112 0
SHEET 2 AA6 2 GLU B 138 ALA B 141 -1 O GLY B 140 N LEU B 110
SHEET 1 AA7 8 VAL B 120 LEU B 121 0
SHEET 2 AA7 8 SER B 232 ALA B 237 1 O VAL B 234 N LEU B 121
SHEET 3 AA7 8 VAL B 203 ILE B 209 1 N VAL B 206 O VAL B 233
SHEET 4 AA7 8 HIS B 266 ASP B 272 1 O ASP B 272 N ILE B 209
SHEET 5 AA7 8 SER B 321 LEU B 329 1 O SER B 321 N VAL B 267
SHEET 6 AA7 8 ARG B 177 ALA B 182 1 N MET B 178 O ALA B 324
SHEET 7 AA7 8 GLY B 349 VAL B 352 1 O GLY B 349 N GLY B 179
SHEET 8 AA7 8 ILE B 372 SER B 373 -1 O ILE B 372 N HIS B 350
SHEET 1 AA811 ARG G 194 GLY G 197 0
SHEET 2 AA811 GLN G 169 VAL G 172 1 N LEU G 170 O ARG G 196
SHEET 3 AA811 LYS G 207 SER G 209 -1 O LYS G 207 N ARG G 171
SHEET 4 AA811 ASP G 214 ASP G 216 -1 O LEU G 215 N VAL G 208
SHEET 5 AA811 ARG C 26 ARG C 33 -1 N ARG C 26 O ASP G 216
SHEET 6 AA811 ARG C 93 ALA C 96 -1 O VAL C 94 N GLY C 29
SHEET 7 AA811 THR C 51 GLN C 57 -1 N GLU C 55 O ARG C 93
SHEET 8 AA811 THR C 62 PHE C 72 -1 O LYS C 63 N ARG C 56
SHEET 9 AA811 LEU C 77 PRO C 81 -1 O PHE C 78 N GLY C 71
SHEET 10 AA811 LEU C 39 THR C 42 -1 N LEU C 39 O LEU C 79
SHEET 11 AA811 ARG C 26 ARG C 33 -1 N ARG C 30 O THR C 42
SHEET 1 AA9 2 GLN C 109 PRO C 111 0
SHEET 2 AA9 2 THR C 139 ALA C 141 -1 O GLY C 140 N LEU C 110
SHEET 1 AB1 8 VAL C 120 LEU C 121 0
SHEET 2 AB1 8 SER C 232 ALA C 237 1 O ALA C 236 N LEU C 121
SHEET 3 AB1 8 VAL C 203 ILE C 209 1 N LEU C 208 O ILE C 235
SHEET 4 AB1 8 HIS C 266 ASP C 272 1 O ASP C 272 N ILE C 209
SHEET 5 AB1 8 SER C 321 LEU C 329 1 O SER C 321 N VAL C 267
SHEET 6 AB1 8 ARG C 177 ALA C 182 1 N MET C 178 O ALA C 324
SHEET 7 AB1 8 GLY C 349 LEU C 353 1 O LEU C 353 N PHE C 181
SHEET 8 AB1 8 ILE C 372 SER C 373 -1 O ILE C 372 N HIS C 350
SHEET 1 AB2 2 VAL C 158 LEU C 159 0
SHEET 2 AB2 2 VAL C 172 GLY C 173 -1 O VAL C 172 N LEU C 159
SHEET 1 AB311 ARG H 194 ARG H 196 0
SHEET 2 AB311 GLN H 169 ARG H 171 1 N LEU H 170 O ARG H 194
SHEET 3 AB311 LYS H 207 SER H 209 -1 O SER H 209 N GLN H 169
SHEET 4 AB311 LEU H 215 ASP H 216 -1 O LEU H 215 N VAL H 208
SHEET 5 AB311 ARG D 26 ARG D 33 -1 N ARG D 26 O ASP H 216
SHEET 6 AB311 ARG D 93 ALA D 96 -1 O VAL D 94 N GLY D 29
SHEET 7 AB311 THR D 51 ASP D 58 -1 N ILE D 53 O TYR D 95
SHEET 8 AB311 GLU D 61 PHE D 72 -1 O SER D 67 N CYS D 52
SHEET 9 AB311 LEU D 77 PRO D 81 -1 O PHE D 78 N GLY D 71
SHEET 10 AB311 LEU D 39 THR D 42 -1 N ALA D 41 O LEU D 77
SHEET 11 AB311 ARG D 26 ARG D 33 -1 N THR D 32 O GLU D 40
SHEET 1 AB4 2 GLN D 109 LEU D 112 0
SHEET 2 AB4 2 GLU D 138 ALA D 141 -1 O GLY D 140 N LEU D 110
SHEET 1 AB5 8 VAL D 120 LEU D 121 0
SHEET 2 AB5 8 SER D 232 ALA D 237 1 O VAL D 234 N LEU D 121
SHEET 3 AB5 8 VAL D 203 ILE D 209 1 N VAL D 206 O ILE D 235
SHEET 4 AB5 8 HIS D 266 ASP D 272 1 O ASP D 272 N ILE D 209
SHEET 5 AB5 8 SER D 321 LEU D 329 1 O SER D 321 N VAL D 267
SHEET 6 AB5 8 ARG D 177 ALA D 182 1 N MET D 178 O TYR D 326
SHEET 7 AB5 8 GLY D 349 LEU D 353 1 O ILE D 351 N GLY D 179
SHEET 8 AB5 8 ILE D 366 SER D 373 -1 O ASP D 367 N VAL D 352
SHEET 1 AB6 3 ARG I 194 GLY I 197 0
SHEET 2 AB6 3 PRO I 168 VAL I 172 1 N VAL I 172 O ARG I 196
SHEET 3 AB6 3 CYS I 206 ALA I 210 -1 O SER I 209 N GLN I 169
SHEET 1 AB7 3 LEU J 195 GLY J 197 0
SHEET 2 AB7 3 GLN J 169 VAL J 172 1 N LEU J 170 O ARG J 196
SHEET 3 AB7 3 LYS J 207 SER J 209 -1 O SER J 209 N GLN J 169
SHEET 1 AB8 3 ARG K 194 GLY K 197 0
SHEET 2 AB8 3 PRO K 168 VAL K 172 1 N LEU K 170 O ARG K 196
SHEET 3 AB8 3 CYS K 206 ALA K 210 -1 O SER K 209 N GLN K 169
SHEET 1 AB9 3 LEU L 195 GLY L 197 0
SHEET 2 AB9 3 GLN L 169 VAL L 172 1 N LEU L 170 O ARG L 196
SHEET 3 AB9 3 CYS L 206 SER L 209 -1 O LYS L 207 N ARG L 171
CISPEP 1 ASP A 272 SER A 273 0 -2.05
CISPEP 2 TYR A 363 PRO A 364 0 -2.23
CISPEP 3 PRO A 454 THR A 455 0 4.47
CISPEP 4 ASP B 272 SER B 273 0 -3.15
CISPEP 5 TYR B 363 PRO B 364 0 -4.87
CISPEP 6 ASP C 272 SER C 273 0 1.22
CISPEP 7 TYR C 363 PRO C 364 0 -9.62
CISPEP 8 ASP D 272 SER D 273 0 0.93
CISPEP 9 TYR D 363 PRO D 364 0 -6.74
CISPEP 10 PHE D 453 PRO D 454 0 17.26
CISPEP 11 GLU E 161 PRO E 162 0 -2.10
CISPEP 12 GLU F 161 PRO F 162 0 -2.69
CISPEP 13 GLU G 161 PRO G 162 0 9.15
CISPEP 14 GLU H 161 PRO H 162 0 4.82
SITE 1 AC1 12 GLY A 183 GLY A 185 VAL A 186 GLY A 187
SITE 2 AC1 12 LYS A 188 SER A 189 VAL A 190 TYR A 363
SITE 3 AC1 12 GLN A 434 GLY A 435 ILE A 436 THR B 377
SITE 1 AC2 10 GLY B 185 VAL B 186 GLY B 187 LYS B 188
SITE 2 AC2 10 SER B 189 VAL B 190 TYR B 363 PRO B 364
SITE 3 AC2 10 GLN B 434 GLN L 159
SITE 1 AC3 7 GLY C 185 GLY C 187 LYS C 188 SER C 189
SITE 2 AC3 7 VAL C 190 MET C 194 TYR C 363
SITE 1 AC4 12 SER D 184 GLY D 185 VAL D 186 GLY D 187
SITE 2 AC4 12 LYS D 188 SER D 189 VAL D 190 MET D 194
SITE 3 AC4 12 TYR D 363 GLN D 434 ILE D 436 GLN J 156
CRYST1 133.662 147.305 164.233 90.00 90.00 90.00 P 21 21 21 32
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 0.007482 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006789 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006089 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
