HEADER TRANSFERASE 29-MAY-14 4TLE
TITLE CRYSTAL STRUCTURE OF N-TERMINAL C1 DOMAIN OF KAIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CIRCADIAN CLOCK PROTEIN KINASE KAIC;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-253;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS PCC 7942;
SOURCE 3 ORGANISM_TAXID: 1140;
SOURCE 4 STRAIN: PCC 7942;
SOURCE 5 GENE: KAIC, SYNPCC7942_1216, SEE0011;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ABE,T.B.HIYAMA,A.MUKAIYAMA,S.SON,S.AKIYAMA
REVDAT 5 20-MAR-24 4TLE 1 REMARK LINK
REVDAT 4 29-JAN-20 4TLE 1 SOURCE JRNL REMARK
REVDAT 3 29-JUL-15 4TLE 1 JRNL
REVDAT 2 08-JUL-15 4TLE 1 JRNL
REVDAT 1 01-JUL-15 4TLE 0
JRNL AUTH J.ABE,T.B.HIYAMA,A.MUKAIYAMA,S.SON,T.MORI,S.SAITO,M.OSAKO,
JRNL AUTH 2 J.WOLANIN,E.YAMASHITA,T.KONDO,S.AKIYAMA
JRNL TITL ATOMIC-SCALE ORIGINS OF SLOWNESS IN THE CYANOBACTERIAL
JRNL TITL 2 CIRCADIAN CLOCK
JRNL REF SCIENCE V. 349 312 2015
JRNL REFN ESSN 1095-9203
JRNL PMID 26113637
JRNL DOI 10.1126/SCIENCE.1261040
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 119305
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6002
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 42.6134 - 6.0101 0.93 3825 199 0.2127 0.2184
REMARK 3 2 6.0101 - 4.7725 1.00 3927 214 0.1712 0.2168
REMARK 3 3 4.7725 - 4.1698 1.00 3880 198 0.1416 0.1754
REMARK 3 4 4.1698 - 3.7888 1.00 3882 191 0.1652 0.1886
REMARK 3 5 3.7888 - 3.5174 1.00 3834 221 0.1778 0.1982
REMARK 3 6 3.5174 - 3.3101 1.00 3856 200 0.1857 0.2410
REMARK 3 7 3.3101 - 3.1444 1.00 3822 201 0.2064 0.2430
REMARK 3 8 3.1444 - 3.0075 1.00 3837 200 0.1912 0.2541
REMARK 3 9 3.0075 - 2.8918 1.00 3779 207 0.2041 0.2478
REMARK 3 10 2.8918 - 2.7920 1.00 3829 217 0.2010 0.2648
REMARK 3 11 2.7920 - 2.7047 1.00 3844 166 0.1986 0.2326
REMARK 3 12 2.7047 - 2.6274 1.00 3791 219 0.1945 0.2552
REMARK 3 13 2.6274 - 2.5583 1.00 3796 185 0.1915 0.2148
REMARK 3 14 2.5583 - 2.4958 1.00 3809 191 0.1967 0.2442
REMARK 3 15 2.4958 - 2.4391 1.00 3779 208 0.2008 0.2610
REMARK 3 16 2.4391 - 2.3872 1.00 3785 212 0.1895 0.2173
REMARK 3 17 2.3872 - 2.3395 1.00 3777 186 0.1920 0.2666
REMARK 3 18 2.3395 - 2.2953 1.00 3815 181 0.1920 0.2424
REMARK 3 19 2.2953 - 2.2543 1.00 3801 185 0.1902 0.2576
REMARK 3 20 2.2543 - 2.2161 1.00 3714 225 0.1979 0.2389
REMARK 3 21 2.2161 - 2.1804 1.00 3851 189 0.1948 0.2207
REMARK 3 22 2.1804 - 2.1468 1.00 3729 194 0.1956 0.2531
REMARK 3 23 2.1468 - 2.1153 1.00 3772 210 0.1978 0.2584
REMARK 3 24 2.1153 - 2.0855 1.00 3733 219 0.2027 0.2473
REMARK 3 25 2.0855 - 2.0573 1.00 3730 221 0.2114 0.2620
REMARK 3 26 2.0573 - 2.0306 0.99 3787 186 0.2269 0.2761
REMARK 3 27 2.0306 - 2.0052 0.99 3744 194 0.2243 0.2826
REMARK 3 28 2.0052 - 1.9810 0.99 3763 194 0.2286 0.2843
REMARK 3 29 1.9810 - 1.9580 0.99 3690 235 0.2277 0.2628
REMARK 3 30 1.9580 - 1.9360 0.82 3122 154 0.2419 0.2782
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 11097
REMARK 3 ANGLE : 1.246 15044
REMARK 3 CHIRALITY : 0.053 1710
REMARK 3 PLANARITY : 0.006 1911
REMARK 3 DIHEDRAL : 14.352 4198
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3269 15.6860 16.9092
REMARK 3 T TENSOR
REMARK 3 T11: 0.1805 T22: 0.2038
REMARK 3 T33: 0.1860 T12: 0.0157
REMARK 3 T13: -0.0325 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 0.4353 L22: 0.3882
REMARK 3 L33: 0.3798 L12: 0.0865
REMARK 3 L13: -0.2956 L23: -0.0660
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: -0.0943 S13: -0.0669
REMARK 3 S21: 0.0414 S22: 0.0560 S23: -0.0503
REMARK 3 S31: 0.1030 S32: 0.0323 S33: -0.0167
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 4TLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119433
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.936
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.0000
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, PEG 8000, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293.15K
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 39.96350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.52850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.66100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.52850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.96350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.66100
REMARK 290 SMTRY3 4 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -190.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 THR A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 5
REMARK 465 MET A 6
REMARK 465 THR A 7
REMARK 465 SER A 8
REMARK 465 PRO A 9
REMARK 465 ASN A 10
REMARK 465 ASN A 11
REMARK 465 ASN A 12
REMARK 465 SER A 13
REMARK 465 GLU A 113
REMARK 465 GLY A 114
REMARK 465 GLN A 115
REMARK 465 GLU A 116
REMARK 465 VAL A 117
REMARK 465 VAL A 118
REMARK 465 GLY A 119
REMARK 465 GLY A 120
REMARK 465 PHE A 121
REMARK 465 VAL A 147
REMARK 465 THR A 148
REMARK 465 SER A 149
REMARK 465 VAL A 150
REMARK 465 PHE A 151
REMARK 465 GLN A 152
REMARK 465 GLN A 153
REMARK 465 TYR A 154
REMARK 465 ASP A 155
REMARK 465 GLY A 250
REMARK 465 ALA A 251
REMARK 465 MET A 252
REMARK 465 ARG A 253
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 GLU B 5
REMARK 465 MET B 6
REMARK 465 THR B 7
REMARK 465 SER B 8
REMARK 465 PRO B 9
REMARK 465 ASN B 10
REMARK 465 ASN B 11
REMARK 465 ASN B 12
REMARK 465 SER B 13
REMARK 465 GLU B 14
REMARK 465 PRO B 112
REMARK 465 GLU B 113
REMARK 465 GLY B 114
REMARK 465 GLN B 115
REMARK 465 GLU B 116
REMARK 465 VAL B 117
REMARK 465 VAL B 118
REMARK 465 GLY B 119
REMARK 465 GLY B 120
REMARK 465 VAL B 147
REMARK 465 THR B 148
REMARK 465 SER B 149
REMARK 465 VAL B 150
REMARK 465 PHE B 151
REMARK 465 GLN B 152
REMARK 465 GLN B 153
REMARK 465 TYR B 154
REMARK 465 ASP B 155
REMARK 465 GLY B 250
REMARK 465 ALA B 251
REMARK 465 MET B 252
REMARK 465 ARG B 253
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 GLU C 5
REMARK 465 MET C 6
REMARK 465 THR C 7
REMARK 465 SER C 8
REMARK 465 PRO C 9
REMARK 465 ASN C 10
REMARK 465 ASN C 11
REMARK 465 ASN C 12
REMARK 465 GLY C 114
REMARK 465 GLN C 115
REMARK 465 GLU C 116
REMARK 465 VAL C 117
REMARK 465 VAL C 118
REMARK 465 GLY C 119
REMARK 465 VAL C 147
REMARK 465 THR C 148
REMARK 465 SER C 149
REMARK 465 VAL C 150
REMARK 465 PHE C 151
REMARK 465 GLN C 152
REMARK 465 GLN C 153
REMARK 465 TYR C 154
REMARK 465 ASP C 155
REMARK 465 GLY C 250
REMARK 465 ALA C 251
REMARK 465 MET C 252
REMARK 465 ARG C 253
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 GLU D 5
REMARK 465 MET D 6
REMARK 465 THR D 7
REMARK 465 SER D 8
REMARK 465 PRO D 9
REMARK 465 ASN D 10
REMARK 465 ASN D 11
REMARK 465 ASN D 12
REMARK 465 GLU D 113
REMARK 465 GLY D 114
REMARK 465 GLN D 115
REMARK 465 GLU D 116
REMARK 465 VAL D 117
REMARK 465 VAL D 118
REMARK 465 GLY D 119
REMARK 465 GLY D 120
REMARK 465 PHE D 121
REMARK 465 ASP D 122
REMARK 465 VAL D 147
REMARK 465 THR D 148
REMARK 465 SER D 149
REMARK 465 VAL D 150
REMARK 465 PHE D 151
REMARK 465 GLN D 152
REMARK 465 GLN D 153
REMARK 465 TYR D 154
REMARK 465 ASP D 155
REMARK 465 ALA D 251
REMARK 465 MET D 252
REMARK 465 ARG D 253
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 SER E 3
REMARK 465 ALA E 4
REMARK 465 GLU E 5
REMARK 465 MET E 6
REMARK 465 THR E 7
REMARK 465 SER E 8
REMARK 465 PRO E 9
REMARK 465 ASN E 10
REMARK 465 ASN E 11
REMARK 465 ASN E 12
REMARK 465 SER E 13
REMARK 465 GLU E 14
REMARK 465 PRO E 112
REMARK 465 GLU E 113
REMARK 465 GLY E 114
REMARK 465 GLN E 115
REMARK 465 GLU E 116
REMARK 465 VAL E 117
REMARK 465 VAL E 118
REMARK 465 GLY E 119
REMARK 465 GLY E 120
REMARK 465 PHE E 121
REMARK 465 VAL E 147
REMARK 465 THR E 148
REMARK 465 SER E 149
REMARK 465 VAL E 150
REMARK 465 PHE E 151
REMARK 465 GLN E 152
REMARK 465 GLN E 153
REMARK 465 TYR E 154
REMARK 465 ASP E 155
REMARK 465 ALA E 251
REMARK 465 MET E 252
REMARK 465 ARG E 253
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ALA F 4
REMARK 465 GLU F 5
REMARK 465 MET F 6
REMARK 465 THR F 7
REMARK 465 SER F 8
REMARK 465 PRO F 9
REMARK 465 ASN F 10
REMARK 465 ASN F 11
REMARK 465 ASN F 12
REMARK 465 SER F 13
REMARK 465 GLU F 14
REMARK 465 HIS F 15
REMARK 465 GLN F 16
REMARK 465 ASP F 111
REMARK 465 PRO F 112
REMARK 465 GLU F 113
REMARK 465 GLY F 114
REMARK 465 GLN F 115
REMARK 465 GLU F 116
REMARK 465 VAL F 117
REMARK 465 VAL F 118
REMARK 465 GLY F 119
REMARK 465 GLY F 120
REMARK 465 PHE F 121
REMARK 465 VAL F 147
REMARK 465 THR F 148
REMARK 465 SER F 149
REMARK 465 VAL F 150
REMARK 465 PHE F 151
REMARK 465 GLN F 152
REMARK 465 GLN F 153
REMARK 465 TYR F 154
REMARK 465 GLY F 250
REMARK 465 ALA F 251
REMARK 465 MET F 252
REMARK 465 ARG F 253
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR A 47 CA CB OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU B 183 NH1 ARG B 193 2.12
REMARK 500 OE2 GLU C 14 O HOH C 477 2.13
REMARK 500 NH2 ARG E 215 O HOH E 401 2.14
REMARK 500 OE2 GLU F 198 O HOH F 482 2.14
REMARK 500 NH2 ARG C 215 O HOH C 401 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS E 102 OE2 GLU F 212 4555 2.13
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 -174.17 -69.19
REMARK 500 GLU A 77 -59.61 -140.25
REMARK 500 THR B 47 -177.88 -65.41
REMARK 500 THR B 47 -176.23 -65.41
REMARK 500 GLU B 77 -66.15 -132.15
REMARK 500 ALA B 192 -139.94 -126.16
REMARK 500 GLU B 214 -0.18 73.96
REMARK 500 THR B 240 -166.43 -126.14
REMARK 500 PRO B 248 98.42 -68.68
REMARK 500 MET C 24 13.24 59.39
REMARK 500 THR C 47 -177.04 -66.35
REMARK 500 GLU C 77 -56.01 -141.13
REMARK 500 PRO C 112 0.96 -66.75
REMARK 500 GLU C 214 -6.37 73.25
REMARK 500 MET D 24 14.24 58.59
REMARK 500 THR D 47 -178.37 -65.36
REMARK 500 GLU D 77 -65.95 -131.00
REMARK 500 ALA D 192 -151.57 -131.73
REMARK 500 LEU D 249 -70.45 -109.24
REMARK 500 GLU E 77 -51.75 -133.98
REMARK 500 ALA E 192 -159.47 -135.80
REMARK 500 THR F 47 -179.32 -67.64
REMARK 500 GLU F 77 -59.89 -137.03
REMARK 500 ALA F 156 154.19 -49.76
REMARK 500 THR F 240 -168.00 -128.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 489 DISTANCE = 6.57 ANGSTROMS
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 53 OG1
REMARK 620 2 AGS A 303 O2B 88.9
REMARK 620 3 AGS A 303 O2G 175.3 89.1
REMARK 620 4 HOH A 456 O 84.3 87.2 91.4
REMARK 620 5 HOH A 457 O 83.0 168.5 98.4 83.9
REMARK 620 6 HOH A 458 O 93.1 93.8 91.3 177.2 94.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 53 OG1
REMARK 620 2 AGS B 303 O2B 90.2
REMARK 620 3 AGS B 303 O2G 177.1 88.8
REMARK 620 4 HOH B 497 O 88.9 89.0 93.7
REMARK 620 5 HOH B 498 O 88.6 177.4 92.5 88.7
REMARK 620 6 HOH B 499 O 86.9 92.9 90.5 175.4 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 53 OG1
REMARK 620 2 AGS C 303 O2G 172.0
REMARK 620 3 AGS C 303 O2B 90.8 92.4
REMARK 620 4 HOH C 492 O 95.5 91.9 89.9
REMARK 620 5 HOH C 493 O 83.1 94.4 171.7 85.1
REMARK 620 6 HOH C 494 O 85.2 87.4 91.1 178.7 94.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 53 OG1
REMARK 620 2 AGS D 303 O2G 174.3
REMARK 620 3 AGS D 303 O2B 89.7 92.8
REMARK 620 4 HOH D 495 O 86.5 88.4 89.5
REMARK 620 5 HOH D 496 O 82.3 95.7 170.7 94.7
REMARK 620 6 HOH D 497 O 94.8 90.3 88.3 177.5 87.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 53 OG1
REMARK 620 2 AGS E 303 O2G 174.5
REMARK 620 3 AGS E 303 O2B 92.8 91.4
REMARK 620 4 HOH E 473 O 88.5 87.5 94.8
REMARK 620 5 HOH E 474 O 88.6 87.6 174.1 91.0
REMARK 620 6 HOH E 475 O 90.8 92.9 90.1 175.0 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 53 OG1
REMARK 620 2 AGS F 303 O2G 174.2
REMARK 620 3 AGS F 303 O1B 88.6 93.1
REMARK 620 4 HOH F 477 O 84.6 89.7 94.5
REMARK 620 5 HOH F 478 O 89.0 89.8 173.0 91.8
REMARK 620 6 HOH F 479 O 92.3 93.3 87.2 176.5 86.4
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 MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AGS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AGS B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AGS C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AGS D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AGS E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AGS F 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TL6 RELATED DB: PDB
REMARK 900 RELATED ID: 4TL7 RELATED DB: PDB
REMARK 900 RELATED ID: 4TL8 RELATED DB: PDB
REMARK 900 RELATED ID: 4TL9 RELATED DB: PDB
REMARK 900 RELATED ID: 4TLA RELATED DB: PDB
REMARK 900 RELATED ID: 4TLB RELATED DB: PDB
REMARK 900 RELATED ID: 4TLC RELATED DB: PDB
REMARK 900 RELATED ID: 4TLD RELATED DB: PDB
DBREF 4TLE A 1 253 UNP Q79PF4 KAIC_SYNE7 1 253
DBREF 4TLE B 1 253 UNP Q79PF4 KAIC_SYNE7 1 253
DBREF 4TLE C 1 253 UNP Q79PF4 KAIC_SYNE7 1 253
DBREF 4TLE D 1 253 UNP Q79PF4 KAIC_SYNE7 1 253
DBREF 4TLE E 1 253 UNP Q79PF4 KAIC_SYNE7 1 253
DBREF 4TLE F 1 253 UNP Q79PF4 KAIC_SYNE7 1 253
SEQADV 4TLE CYS A 157 UNP Q79PF4 SER 157 ENGINEERED MUTATION
SEQADV 4TLE CYS B 157 UNP Q79PF4 SER 157 ENGINEERED MUTATION
SEQADV 4TLE CYS C 157 UNP Q79PF4 SER 157 ENGINEERED MUTATION
SEQADV 4TLE CYS D 157 UNP Q79PF4 SER 157 ENGINEERED MUTATION
SEQADV 4TLE CYS E 157 UNP Q79PF4 SER 157 ENGINEERED MUTATION
SEQADV 4TLE CYS F 157 UNP Q79PF4 SER 157 ENGINEERED MUTATION
SEQRES 1 A 253 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 A 253 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 A 253 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 A 253 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 A 253 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 A 253 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 A 253 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 A 253 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 A 253 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 A 253 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 A 253 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 A 253 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 A 253 CYS SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 A 253 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 A 253 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 A 253 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 A 253 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 A 253 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 A 253 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 A 253 PRO LEU GLY ALA MET ARG
SEQRES 1 B 253 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 B 253 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 B 253 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 B 253 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 B 253 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 B 253 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 B 253 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 B 253 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 B 253 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 B 253 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 B 253 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 B 253 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 B 253 CYS SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 B 253 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 B 253 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 B 253 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 B 253 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 B 253 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 B 253 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 B 253 PRO LEU GLY ALA MET ARG
SEQRES 1 C 253 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 C 253 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 C 253 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 C 253 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 C 253 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 C 253 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 C 253 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 C 253 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 C 253 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 C 253 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 C 253 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 C 253 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 C 253 CYS SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 C 253 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 C 253 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 C 253 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 C 253 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 C 253 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 C 253 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 C 253 PRO LEU GLY ALA MET ARG
SEQRES 1 D 253 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 D 253 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 D 253 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 D 253 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 D 253 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 D 253 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 D 253 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 D 253 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 D 253 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 D 253 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 D 253 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 D 253 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 D 253 CYS SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 D 253 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 D 253 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 D 253 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 D 253 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 D 253 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 D 253 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 D 253 PRO LEU GLY ALA MET ARG
SEQRES 1 E 253 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 E 253 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 E 253 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 E 253 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 E 253 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 E 253 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 E 253 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 E 253 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 E 253 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 E 253 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 E 253 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 E 253 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 E 253 CYS SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 E 253 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 E 253 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 E 253 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 E 253 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 E 253 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 E 253 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 E 253 PRO LEU GLY ALA MET ARG
SEQRES 1 F 253 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 F 253 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 F 253 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 F 253 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 F 253 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 F 253 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 F 253 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 F 253 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 F 253 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 F 253 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 F 253 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 F 253 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 F 253 CYS SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 F 253 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 F 253 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 F 253 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 F 253 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 F 253 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 F 253 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 F 253 PRO LEU GLY ALA MET ARG
HET MG A 301 1
HET CL A 302 1
HET AGS A 303 31
HET MG B 301 1
HET CL B 302 1
HET AGS B 303 31
HET MG C 301 1
HET CL C 302 1
HET AGS C 303 31
HET MG D 301 1
HET CL D 302 1
HET AGS D 303 31
HET MG E 301 1
HET CL E 302 1
HET AGS E 303 31
HET MG F 301 1
HET CL F 302 1
HET AGS F 303 31
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
HETSYN AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
HETSYN 2 AGS ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-
HETSYN 3 AGS DIPHOSPHATE MONOTHIOPHOSPHATE
FORMUL 7 MG 6(MG 2+)
FORMUL 8 CL 6(CL 1-)
FORMUL 9 AGS 6(C10 H16 N5 O12 P3 S)
FORMUL 25 HOH *567(H2 O)
HELIX 1 AA1 GLY A 27 SER A 32 1 6
HELIX 2 AA2 GLY A 51 ASP A 68 1 18
HELIX 3 AA3 THR A 79 ARG A 88 1 10
HELIX 4 AA4 SER A 89 GLY A 91 5 3
HELIX 5 AA5 ASP A 93 GLU A 100 1 8
HELIX 6 AA6 LEU A 123 ARG A 138 1 16
HELIX 7 AA7 CYS A 157 GLY A 175 1 19
HELIX 8 AA8 VAL A 196 SER A 201 1 6
HELIX 9 AA9 GLY B 27 SER B 32 1 6
HELIX 10 AB1 GLY B 51 ASP B 68 1 18
HELIX 11 AB2 THR B 79 ARG B 88 1 10
HELIX 12 AB3 SER B 89 GLY B 91 5 3
HELIX 13 AB4 ASP B 93 GLU B 100 1 8
HELIX 14 AB5 ASP B 122 ARG B 138 1 17
HELIX 15 AB6 CYS B 157 GLY B 175 1 19
HELIX 16 AB7 VAL B 196 SER B 201 1 6
HELIX 17 AB8 GLY C 27 SER C 32 1 6
HELIX 18 AB9 GLY C 51 ASP C 68 1 18
HELIX 19 AC1 THR C 79 ARG C 88 1 10
HELIX 20 AC2 SER C 89 GLY C 91 5 3
HELIX 21 AC3 ASP C 93 GLU C 100 1 8
HELIX 22 AC4 ASP C 122 ARG C 138 1 17
HELIX 23 AC5 CYS C 157 GLY C 175 1 19
HELIX 24 AC6 VAL C 196 SER C 201 1 6
HELIX 25 AC7 GLY D 27 SER D 32 1 6
HELIX 26 AC8 GLY D 51 ASP D 68 1 18
HELIX 27 AC9 THR D 79 ARG D 88 1 10
HELIX 28 AD1 SER D 89 GLY D 91 5 3
HELIX 29 AD2 ASP D 93 GLU D 100 1 8
HELIX 30 AD3 SER D 124 ARG D 138 1 15
HELIX 31 AD4 CYS D 157 GLY D 175 1 19
HELIX 32 AD5 VAL D 196 SER D 201 1 6
HELIX 33 AD6 GLY E 27 SER E 32 1 6
HELIX 34 AD7 GLY E 51 ASP E 68 1 18
HELIX 35 AD8 THR E 79 ARG E 88 1 10
HELIX 36 AD9 SER E 89 GLY E 91 5 3
HELIX 37 AE1 ASP E 93 GLU E 100 1 8
HELIX 38 AE2 LEU E 123 ARG E 138 1 16
HELIX 39 AE3 CYS E 157 GLY E 175 1 19
HELIX 40 AE4 VAL E 196 SER E 201 1 6
HELIX 41 AE5 GLY F 27 SER F 32 1 6
HELIX 42 AE6 GLY F 51 ASP F 68 1 18
HELIX 43 AE7 THR F 79 SER F 89 1 11
HELIX 44 AE8 ASP F 93 GLU F 100 1 8
HELIX 45 AE9 LEU F 123 ARG F 138 1 16
HELIX 46 AF1 ALA F 156 GLY F 175 1 20
HELIX 47 AF2 VAL F 196 SER F 201 1 6
SHEET 1 AA1 2 LYS A 20 MET A 21 0
SHEET 2 AA1 2 LEU A 36 PRO A 37 -1 O LEU A 36 N MET A 21
SHEET 1 AA2 9 LEU A 103 ASP A 107 0
SHEET 2 AA2 9 GLY A 71 THR A 75 1 N PHE A 73 O LEU A 106
SHEET 3 AA2 9 ARG A 141 ASP A 145 1 O SER A 143 N VAL A 74
SHEET 4 AA2 9 THR A 177 GLU A 183 1 O VAL A 179 N ILE A 144
SHEET 5 AA2 9 SER A 41 GLY A 46 1 N THR A 42 O THR A 178
SHEET 6 AA2 9 ASN A 203 GLU A 212 1 O VAL A 205 N LEU A 43
SHEET 7 AA2 9 ARG A 215 LEU A 225 -1 O THR A 219 N ARG A 208
SHEET 8 AA2 9 GLU A 234 THR A 240 -1 O TYR A 235 N LEU A 220
SHEET 9 AA2 9 GLY A 243 ILE A 246 -1 O ASN A 245 N THR A 238
SHEET 1 AA3 2 LYS B 20 MET B 21 0
SHEET 2 AA3 2 LEU B 36 PRO B 37 -1 O LEU B 36 N MET B 21
SHEET 1 AA4 9 LEU B 103 ASP B 107 0
SHEET 2 AA4 9 GLY B 71 THR B 75 1 N PHE B 73 O PHE B 104
SHEET 3 AA4 9 ARG B 141 ASP B 145 1 O SER B 143 N VAL B 74
SHEET 4 AA4 9 THR B 177 GLU B 183 1 O VAL B 179 N ILE B 144
SHEET 5 AA4 9 SER B 41 GLY B 46 1 N THR B 42 O THR B 178
SHEET 6 AA4 9 ASN B 203 GLU B 212 1 O VAL B 205 N LEU B 43
SHEET 7 AA4 9 ARG B 215 LEU B 225 -1 O GLU B 221 N ILE B 206
SHEET 8 AA4 9 GLU B 234 THR B 240 -1 O TYR B 235 N LEU B 220
SHEET 9 AA4 9 GLY B 243 ILE B 246 -1 O ASN B 245 N THR B 238
SHEET 1 AA5 2 LYS C 20 MET C 21 0
SHEET 2 AA5 2 LEU C 36 PRO C 37 -1 O LEU C 36 N MET C 21
SHEET 1 AA6 9 LEU C 103 ASP C 107 0
SHEET 2 AA6 9 GLY C 71 THR C 75 1 N PHE C 73 O LEU C 106
SHEET 3 AA6 9 ARG C 141 ASP C 145 1 O SER C 143 N VAL C 74
SHEET 4 AA6 9 THR C 177 GLU C 183 1 O VAL C 179 N ILE C 144
SHEET 5 AA6 9 SER C 41 GLY C 46 1 N THR C 42 O MET C 180
SHEET 6 AA6 9 ASN C 203 GLU C 212 1 O VAL C 205 N LEU C 43
SHEET 7 AA6 9 ARG C 215 LEU C 225 -1 O THR C 219 N ARG C 208
SHEET 8 AA6 9 GLU C 234 THR C 240 -1 O TYR C 235 N LEU C 220
SHEET 9 AA6 9 GLY C 243 ILE C 246 -1 O ASN C 245 N THR C 238
SHEET 1 AA7 2 LYS D 20 MET D 21 0
SHEET 2 AA7 2 LEU D 36 PRO D 37 -1 O LEU D 36 N MET D 21
SHEET 1 AA8 9 LEU D 103 ASP D 107 0
SHEET 2 AA8 9 GLY D 71 THR D 75 1 N PHE D 73 O LEU D 106
SHEET 3 AA8 9 ARG D 141 ASP D 145 1 O SER D 143 N VAL D 74
SHEET 4 AA8 9 THR D 177 GLU D 183 1 O VAL D 179 N ILE D 144
SHEET 5 AA8 9 SER D 41 GLY D 46 1 N THR D 42 O THR D 178
SHEET 6 AA8 9 ASN D 203 GLU D 212 1 O LEU D 207 N SER D 45
SHEET 7 AA8 9 ARG D 215 LEU D 225 -1 O THR D 219 N ARG D 208
SHEET 8 AA8 9 GLU D 234 THR D 240 -1 O TYR D 235 N LEU D 220
SHEET 9 AA8 9 GLY D 243 ILE D 246 -1 O ASN D 245 N THR D 238
SHEET 1 AA9 2 LYS E 20 MET E 21 0
SHEET 2 AA9 2 LEU E 36 PRO E 37 -1 O LEU E 36 N MET E 21
SHEET 1 AB1 9 LEU E 103 ASP E 107 0
SHEET 2 AB1 9 GLY E 71 THR E 75 1 N PHE E 73 O LEU E 106
SHEET 3 AB1 9 ARG E 141 ASP E 145 1 O SER E 143 N VAL E 74
SHEET 4 AB1 9 THR E 177 GLU E 183 1 O VAL E 179 N ILE E 144
SHEET 5 AB1 9 SER E 41 GLY E 46 1 N THR E 42 O THR E 178
SHEET 6 AB1 9 ASN E 203 GLU E 212 1 O VAL E 205 N LEU E 43
SHEET 7 AB1 9 ARG E 215 LEU E 225 -1 O ARG E 215 N GLU E 212
SHEET 8 AB1 9 GLU E 234 THR E 240 -1 O TYR E 235 N LEU E 220
SHEET 9 AB1 9 GLY E 243 ILE E 246 -1 O ASN E 245 N THR E 238
SHEET 1 AB2 2 LYS F 20 MET F 21 0
SHEET 2 AB2 2 LEU F 36 PRO F 37 -1 O LEU F 36 N MET F 21
SHEET 1 AB3 9 LEU F 103 ASP F 107 0
SHEET 2 AB3 9 GLY F 71 THR F 75 1 N PHE F 73 O LEU F 106
SHEET 3 AB3 9 ARG F 141 ASP F 145 1 O SER F 143 N VAL F 74
SHEET 4 AB3 9 THR F 177 GLU F 183 1 O VAL F 179 N ILE F 144
SHEET 5 AB3 9 SER F 41 GLY F 46 1 N THR F 42 O THR F 178
SHEET 6 AB3 9 ASN F 203 GLU F 212 1 O VAL F 205 N LEU F 43
SHEET 7 AB3 9 ARG F 215 LEU F 225 -1 O ARG F 215 N GLU F 212
SHEET 8 AB3 9 GLU F 234 THR F 240 -1 O TYR F 235 N LEU F 220
SHEET 9 AB3 9 GLY F 243 ILE F 246 -1 O ASN F 245 N THR F 238
LINK OG1 THR A 53 MG MG A 301 1555 1555 2.07
LINK MG MG A 301 O2B AGS A 303 1555 1555 2.13
LINK MG MG A 301 O2G AGS A 303 1555 1555 1.92
LINK MG MG A 301 O HOH A 456 1555 1555 2.11
LINK MG MG A 301 O HOH A 457 1555 1555 2.06
LINK MG MG A 301 O HOH A 458 1555 1555 2.02
LINK OG1 THR B 53 MG MG B 301 1555 1555 1.94
LINK MG MG B 301 O2B AGS B 303 1555 1555 2.07
LINK MG MG B 301 O2G AGS B 303 1555 1555 1.96
LINK MG MG B 301 O HOH B 497 1555 1555 2.02
LINK MG MG B 301 O HOH B 498 1555 1555 2.07
LINK MG MG B 301 O HOH B 499 1555 1555 2.15
LINK OG1 THR C 53 MG MG C 301 1555 1555 2.07
LINK MG MG C 301 O2G AGS C 303 1555 1555 1.89
LINK MG MG C 301 O2B AGS C 303 1555 1555 1.98
LINK MG MG C 301 O HOH C 492 1555 1555 1.97
LINK MG MG C 301 O HOH C 493 1555 1555 2.10
LINK MG MG C 301 O HOH C 494 1555 1555 2.26
LINK OG1 THR D 53 MG MG D 301 1555 1555 2.03
LINK MG MG D 301 O2G AGS D 303 1555 1555 1.93
LINK MG MG D 301 O2B AGS D 303 1555 1555 2.08
LINK MG MG D 301 O HOH D 495 1555 1555 2.06
LINK MG MG D 301 O HOH D 496 1555 1555 2.19
LINK MG MG D 301 O HOH D 497 1555 1555 2.09
LINK OG1 THR E 53 MG MG E 301 1555 1555 2.07
LINK MG MG E 301 O2G AGS E 303 1555 1555 1.87
LINK MG MG E 301 O2B AGS E 303 1555 1555 2.03
LINK MG MG E 301 O HOH E 473 1555 1555 2.11
LINK MG MG E 301 O HOH E 474 1555 1555 2.05
LINK MG MG E 301 O HOH E 475 1555 1555 2.15
LINK OG1 THR F 53 MG MG F 301 1555 1555 1.98
LINK MG MG F 301 O2G AGS F 303 1555 1555 1.86
LINK MG MG F 301 O1B AGS F 303 1555 1555 2.04
LINK MG MG F 301 O HOH F 477 1555 1555 2.10
LINK MG MG F 301 O HOH F 478 1555 1555 1.98
LINK MG MG F 301 O HOH F 479 1555 1555 2.15
CISPEP 1 ASP A 145 SER A 146 0 4.14
CISPEP 2 ASP B 145 SER B 146 0 7.12
CISPEP 3 ASP C 145 SER C 146 0 -1.33
CISPEP 4 ASP D 145 SER D 146 0 0.32
CISPEP 5 ASP E 145 SER E 146 0 -4.45
CISPEP 6 ASP F 145 SER F 146 0 -1.84
SITE 1 AC1 6 THR A 53 ASP A 145 AGS A 303 HOH A 456
SITE 2 AC1 6 HOH A 457 HOH A 458
SITE 1 AC2 3 ARG A 218 ILE A 239 HOH B 444
SITE 1 AC3 28 SER A 48 GLY A 49 THR A 50 GLY A 51
SITE 2 AC3 28 LYS A 52 THR A 53 LEU A 54 SER A 89
SITE 3 AC3 28 PHE A 90 ARG A 218 ILE A 239 THR A 240
SITE 4 AC3 28 ASP A 241 MG A 301 HOH A 408 HOH A 420
SITE 5 AC3 28 HOH A 434 HOH A 456 HOH A 457 HOH A 458
SITE 6 AC3 28 PHE B 199 LYS B 224 LEU B 225 ARG B 226
SITE 7 AC3 28 THR B 228 SER B 229 HIS B 230 HOH B 444
SITE 1 AC4 5 THR B 53 AGS B 303 HOH B 497 HOH B 498
SITE 2 AC4 5 HOH B 499
SITE 1 AC5 4 ARG B 218 THR B 238 ILE B 239 HOH C 439
SITE 1 AC6 27 SER B 48 GLY B 49 THR B 50 GLY B 51
SITE 2 AC6 27 LYS B 52 THR B 53 LEU B 54 SER B 89
SITE 3 AC6 27 PHE B 90 ARG B 218 ILE B 239 THR B 240
SITE 4 AC6 27 ASP B 241 MG B 301 HOH B 419 HOH B 466
SITE 5 AC6 27 HOH B 497 HOH B 498 HOH B 499 PHE C 199
SITE 6 AC6 27 LYS C 224 LEU C 225 ARG C 226 THR C 228
SITE 7 AC6 27 SER C 229 HIS C 230 HOH C 439
SITE 1 AC7 5 THR C 53 AGS C 303 HOH C 492 HOH C 493
SITE 2 AC7 5 HOH C 494
SITE 1 AC8 3 ARG C 218 ILE C 239 LYS D 232
SITE 1 AC9 29 SER C 48 GLY C 49 THR C 50 GLY C 51
SITE 2 AC9 29 LYS C 52 THR C 53 LEU C 54 SER C 89
SITE 3 AC9 29 PHE C 90 ARG C 218 ILE C 239 ASP C 241
SITE 4 AC9 29 MG C 301 HOH C 424 HOH C 425 HOH C 440
SITE 5 AC9 29 HOH C 460 HOH C 480 HOH C 492 HOH C 493
SITE 6 AC9 29 HOH C 494 PHE D 199 LYS D 224 LEU D 225
SITE 7 AC9 29 ARG D 226 THR D 228 SER D 229 HIS D 230
SITE 8 AC9 29 LYS D 232
SITE 1 AD1 5 THR D 53 AGS D 303 HOH D 495 HOH D 496
SITE 2 AD1 5 HOH D 497
SITE 1 AD2 3 ARG D 218 THR D 238 ILE D 239
SITE 1 AD3 28 SER D 48 GLY D 49 THR D 50 GLY D 51
SITE 2 AD3 28 LYS D 52 THR D 53 LEU D 54 SER D 89
SITE 3 AD3 28 PHE D 90 ARG D 218 ILE D 239 THR D 240
SITE 4 AD3 28 ASP D 241 MG D 301 HOH D 427 HOH D 435
SITE 5 AD3 28 HOH D 455 HOH D 495 HOH D 496 HOH D 497
SITE 6 AD3 28 PHE E 199 LYS E 224 LEU E 225 ARG E 226
SITE 7 AD3 28 THR E 228 SER E 229 HIS E 230 HOH E 447
SITE 1 AD4 5 THR E 53 AGS E 303 HOH E 473 HOH E 474
SITE 2 AD4 5 HOH E 475
SITE 1 AD5 3 ARG E 218 THR E 238 ILE E 239
SITE 1 AD6 28 SER E 48 GLY E 49 THR E 50 GLY E 51
SITE 2 AD6 28 LYS E 52 THR E 53 LEU E 54 SER E 89
SITE 3 AD6 28 PHE E 90 ARG E 218 ILE E 239 ASP E 241
SITE 4 AD6 28 MG E 301 HOH E 417 HOH E 440 HOH E 450
SITE 5 AD6 28 HOH E 473 HOH E 474 HOH E 475 HOH E 476
SITE 6 AD6 28 PHE F 199 LYS F 224 LEU F 225 ARG F 226
SITE 7 AD6 28 THR F 228 SER F 229 HIS F 230 HOH F 446
SITE 1 AD7 5 THR F 53 AGS F 303 HOH F 477 HOH F 478
SITE 2 AD7 5 HOH F 479
SITE 1 AD8 3 HOH A 415 ARG F 218 ILE F 239
SITE 1 AD9 29 PHE A 199 LYS A 224 LEU A 225 ARG A 226
SITE 2 AD9 29 THR A 228 SER A 229 HIS A 230 LYS A 232
SITE 3 AD9 29 HOH A 415 SER F 48 GLY F 49 THR F 50
SITE 4 AD9 29 GLY F 51 LYS F 52 THR F 53 LEU F 54
SITE 5 AD9 29 SER F 89 PHE F 90 ARG F 218 ILE F 239
SITE 6 AD9 29 THR F 240 ASP F 241 MG F 301 HOH F 427
SITE 7 AD9 29 HOH F 448 HOH F 450 HOH F 477 HOH F 478
SITE 8 AD9 29 HOH F 479
CRYST1 79.927 133.322 151.057 90.00 90.00 90.00 P 21 21 21 24
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 0.012511 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
