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HEADER HYDROLASE 29-NOV-18 6N8E
TITLE CRYSTAL STRUCTURE OF HOLO-OBIF1, A FIVE DOMAIN NONRIBOSOMAL PEPTIDE
TITLE 2 SYNTHETASE FROM BURKHOLDERIA DIFFUSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOLO-OBIF1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA DIFFUSA;
SOURCE 3 ORGANISM_TAXID: 488732;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS NRPS, BETA-LACTONE, MODULE, THIOESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.F.KREITLER,T.A.WENCEWICZ,A.M.GULICK
REVDAT 1 24-JUL-19 6N8E 0
JRNL AUTH D.F.KREITLER,J.E.SCHAFFER,E.M.GEMMELL,T.A.WENCEWICZ,
JRNL AUTH 2 A.M.GULICK
JRNL TITL THE STRUCTURAL BASIS OF N-ACYL-ALPHA-AMINO-BETA-LACTONE
JRNL TITL 2 FORMATION CATALYZED BY A NONRIBOSOMAL PEPTIDE SYNTHETASE
JRNL REF NAT COMMUN 2019
JRNL REFN ESSN 2041-1723
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 47061
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7068 - 7.2170 1.00 3430 153 0.1809 0.1770
REMARK 3 2 7.2170 - 5.7339 1.00 3286 145 0.2070 0.2397
REMARK 3 3 5.7339 - 5.0107 1.00 3253 144 0.1923 0.2206
REMARK 3 4 5.0107 - 4.5533 1.00 3230 143 0.1675 0.2034
REMARK 3 5 4.5533 - 4.2273 1.00 3220 143 0.1816 0.2136
REMARK 3 6 4.2273 - 3.9783 1.00 3221 143 0.2037 0.2471
REMARK 3 7 3.9783 - 3.7792 1.00 3183 141 0.2091 0.2205
REMARK 3 8 3.7792 - 3.6148 1.00 3198 142 0.2271 0.3003
REMARK 3 9 3.6148 - 3.4758 1.00 3178 140 0.2369 0.2672
REMARK 3 10 3.4758 - 3.3559 1.00 3170 140 0.2509 0.2782
REMARK 3 11 3.3559 - 3.2510 1.00 3170 141 0.2554 0.2499
REMARK 3 12 3.2510 - 3.1581 1.00 3192 142 0.2668 0.3276
REMARK 3 13 3.1581 - 3.0750 1.00 3175 141 0.2927 0.3679
REMARK 3 14 3.0750 - 3.0000 1.00 3157 140 0.3113 0.3693
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.00
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 4:169 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.482 -41.907 7.755
REMARK 3 T TENSOR
REMARK 3 T11: 0.2849 T22: 0.4980
REMARK 3 T33: 0.3790 T12: -0.0742
REMARK 3 T13: -0.0048 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 2.4259 L22: 2.3184
REMARK 3 L33: 1.8774 L12: -0.2027
REMARK 3 L13: 0.0825 L23: -0.3097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0358 S12: -0.0103 S13: -0.0030
REMARK 3 S21: -0.0187 S22: 0.0166 S23: -0.1896
REMARK 3 S31: 0.0238 S32: 0.4046 S33: -0.0090
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 170:379 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.054 -33.785 22.540
REMARK 3 T TENSOR
REMARK 3 T11: 0.3765 T22: 0.4026
REMARK 3 T33: 0.4354 T12: -0.1056
REMARK 3 T13: -0.0017 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.1090 L22: 1.0213
REMARK 3 L33: 2.2917 L12: -0.1948
REMARK 3 L13: -0.1030 L23: 0.6273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0248 S12: -0.0207 S13: 0.0700
REMARK 3 S21: 0.0895 S22: -0.0041 S23: 0.0783
REMARK 3 S31: 0.1186 S32: -0.2847 S33: 0.0014
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 380:453 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.278 -33.210 39.511
REMARK 3 T TENSOR
REMARK 3 T11: 0.4698 T22: 0.4880
REMARK 3 T33: 0.4497 T12: 0.0150
REMARK 3 T13: -0.0187 T23: -0.0833
REMARK 3 L TENSOR
REMARK 3 L11: 1.6778 L22: 2.3556
REMARK 3 L33: 1.5236 L12: -0.4240
REMARK 3 L13: -0.2334 L23: 1.0696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0300 S12: -0.1502 S13: 0.2111
REMARK 3 S21: 0.3208 S22: 0.1262 S23: -0.1036
REMARK 3 S31: 0.2441 S32: 0.1187 S33: -0.1074
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 454:616 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.696 12.606 75.784
REMARK 3 T TENSOR
REMARK 3 T11: 0.5793 T22: 0.4712
REMARK 3 T33: 0.4640 T12: 0.1233
REMARK 3 T13: -0.0969 T23: -0.1587
REMARK 3 L TENSOR
REMARK 3 L11: 1.9111 L22: 2.7251
REMARK 3 L33: 2.3755 L12: -1.0396
REMARK 3 L13: -0.7514 L23: 1.1366
REMARK 3 S TENSOR
REMARK 3 S11: -0.1318 S12: -0.0066 S13: -0.1200
REMARK 3 S21: 0.4885 S22: 0.2768 S23: -0.1812
REMARK 3 S31: 0.2592 S32: 0.1932 S33: -0.1170
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 617:776 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.332 7.930 60.843
REMARK 3 T TENSOR
REMARK 3 T11: 0.5861 T22: 0.8556
REMARK 3 T33: 0.7157 T12: 0.0936
REMARK 3 T13: -0.0494 T23: -0.3036
REMARK 3 L TENSOR
REMARK 3 L11: 1.5988 L22: 3.4325
REMARK 3 L33: 1.9045 L12: -0.1933
REMARK 3 L13: -0.6241 L23: 0.6258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0785 S12: 0.2717 S13: 0.0031
REMARK 3 S21: -0.2581 S22: 0.2391 S23: -0.8155
REMARK 3 S31: 0.0933 S32: 0.5231 S33: -0.2768
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 777:870 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.138 -11.670 55.233
REMARK 3 T TENSOR
REMARK 3 T11: 0.5440 T22: 0.5446
REMARK 3 T33: 0.6100 T12: 0.0544
REMARK 3 T13: -0.0506 T23: -0.1780
REMARK 3 L TENSOR
REMARK 3 L11: 1.2391 L22: 3.5543
REMARK 3 L33: 2.8573 L12: -0.2339
REMARK 3 L13: 0.3988 L23: 2.1887
REMARK 3 S TENSOR
REMARK 3 S11: -0.2199 S12: -0.0972 S13: 0.3071
REMARK 3 S21: 0.2555 S22: 0.2768 S23: -0.3458
REMARK 3 S31: -0.0273 S32: 0.4956 S33: -0.0774
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 1059:1131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.869 -16.538 21.075
REMARK 3 T TENSOR
REMARK 3 T11: 0.4330 T22: 0.4791
REMARK 3 T33: 0.7740 T12: -0.0177
REMARK 3 T13: 0.0949 T23: -0.1728
REMARK 3 L TENSOR
REMARK 3 L11: 3.6170 L22: 2.4130
REMARK 3 L33: 4.5642 L12: -0.8188
REMARK 3 L13: -1.8651 L23: 0.5106
REMARK 3 S TENSOR
REMARK 3 S11: 0.4804 S12: -0.2011 S13: 0.9830
REMARK 3 S21: -0.1821 S22: -0.2129 S23: -0.2702
REMARK 3 S31: -0.5591 S32: -0.3488 S33: -0.2635
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN A AND RESID 1132:1303 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.548 -25.089 28.432
REMARK 3 T TENSOR
REMARK 3 T11: 0.3890 T22: 0.8250
REMARK 3 T33: 0.5370 T12: -0.1012
REMARK 3 T13: 0.0031 T23: -0.1422
REMARK 3 L TENSOR
REMARK 3 L11: 2.8427 L22: 1.7076
REMARK 3 L33: 2.5391 L12: -0.7320
REMARK 3 L13: -0.9918 L23: 0.7070
REMARK 3 S TENSOR
REMARK 3 S11: 0.1386 S12: -0.9164 S13: 0.6234
REMARK 3 S21: 0.2453 S22: 0.0289 S23: -0.1875
REMARK 3 S31: -0.0944 S32: 0.4015 S33: -0.1473
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN A AND RESID 1313:1370 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.122 -19.584 55.082
REMARK 3 T TENSOR
REMARK 3 T11: 0.7353 T22: 0.6254
REMARK 3 T33: 0.5756 T12: -0.0941
REMARK 3 T13: 0.1254 T23: -0.2045
REMARK 3 L TENSOR
REMARK 3 L11: 2.5097 L22: 1.5266
REMARK 3 L33: 2.0186 L12: -0.3014
REMARK 3 L13: -0.6469 L23: -1.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.3381 S12: -0.2974 S13: 0.1224
REMARK 3 S21: 0.4252 S22: 0.2232 S23: 0.2869
REMARK 3 S31: 0.3953 S32: -0.4164 S33: 0.1237
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 6N8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000238305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47131
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.703
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 FOR THE DATA SET : 11.4000
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) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40700
REMARK 200 FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5U89, 5T3D, 3FLB
REMARK 200
REMARK 200 REMARK: 3D BRICKS WITH FACETS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION: 90 MM HEPES PH 6.8, 5%
REMARK 280 W/V 1,3-DIMETHYLIMIDAZOLIUM DIMETHYL PHOSPHATE, 27% W/V PEG3350;
REMARK 280 PROTEIN SAMPLE: 25 MM HEPES PH 8.0, 25 MM NACL, 0.4 MM TCEP, 5%
REMARK 280 V/V GLYCEROL, 36.5 MG/ML HOLO-OBIF1; DROP COMPOSITION: 2 UL
REMARK 280 PROTEIN: 1 UL WELL SOLUTION UNDER PARAFFIN OIL, MICROBATCH,
REMARK 280 TEMPERATURE 287K
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 40.66250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.95250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.17250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.95250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.66250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.17250
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 ALA A 3
REMARK 465 ASP A 73
REMARK 465 GLY A 74
REMARK 465 GLU A 75
REMARK 465 GLY A 76
REMARK 465 GLY A 619
REMARK 465 SER A 620
REMARK 465 THR A 621
REMARK 465 GLY A 622
REMARK 465 GLY A 924
REMARK 465 GLU A 925
REMARK 465 CYS A 926
REMARK 465 LEU A 927
REMARK 465 ASP A 928
REMARK 465 THR A 973
REMARK 465 ALA A 974
REMARK 465 THR A 975
REMARK 465 GLU A 976
REMARK 465 ARG A 977
REMARK 465 ALA A 1051
REMARK 465 ASP A 1052
REMARK 465 GLY A 1053
REMARK 465 ALA A 1054
REMARK 465 GLY A 1055
REMARK 465 ASP A 1056
REMARK 465 ALA A 1057
REMARK 465 ALA A 1058
REMARK 465 PRO A 1304
REMARK 465 ALA A 1305
REMARK 465 SER A 1306
REMARK 465 ARG A 1307
REMARK 465 ALA A 1308
REMARK 465 PRO A 1309
REMARK 465 GLU A 1310
REMARK 465 ARG A 1311
REMARK 465 GLU A 1312
REMARK 465 ASN A 1371
REMARK 465 PRO A 1372
REMARK 465 PRO A 1373
REMARK 465 ILE A 1374
REMARK 465 GLY A 1375
REMARK 465 VAL A 1376
REMARK 465 SER A 1377
REMARK 465 ALA A 1378
REMARK 465 ALA A 1379
REMARK 465 VAL A 1380
REMARK 465 ALA A 1381
REMARK 465 ALA A 1382
REMARK 465 ARG A 1383
REMARK 465 GLU A 1384
REMARK 465 THR A 1385
REMARK 465 ALA A 1386
REMARK 465 GLU A 1387
REMARK 465 HIS A 1388
REMARK 465 CYS A 1389
REMARK 465 VAL A 1390
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 4 CG CD1 CD2
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 450 CG CD1 CD2
REMARK 470 LYS A 455 CG CD CE NZ
REMARK 470 ARG A 468 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 601 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 623 CG CD CE NZ
REMARK 470 LYS A 625 CG CD CE NZ
REMARK 470 ARG A 687 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 713 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 726 CG CD OE1 NE2
REMARK 470 ARG A 729 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 746 CG CD CE NZ
REMARK 470 ASP A 754 CG OD1 OD2
REMARK 470 SER A 755 OG
REMARK 470 ARG A 780 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 879 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 881 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 887 CG CD OE1 OE2
REMARK 470 ARG A 891 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 894 CG CD OE1 OE2
REMARK 470 ARG A 906 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 907 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 910 CG1 CG2
REMARK 470 ASP A 912 CG OD1 OD2
REMARK 470 GLN A 914 CG CD OE1 NE2
REMARK 470 LEU A 936 CG CD1 CD2
REMARK 470 ARG A 937 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 938 CG CD OE1 OE2
REMARK 470 ARG A 939 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 952 CG CD1 CD2
REMARK 470 ARG A 959 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 962 CG CD CE NZ
REMARK 470 VAL A 963 CG1 CG2
REMARK 470 LYS A 966 CG CD CE NZ
REMARK 470 VAL A 978 CG1 CG2
REMARK 470 VAL A 979 CG1 CG2
REMARK 470 GLU A 988 CG CD OE1 OE2
REMARK 470 GLU A 992 CG CD OE1 OE2
REMARK 470 GLU A 996 CG CD OE1 OE2
REMARK 470 ASP A1000 CG OD1 OD2
REMARK 470 VAL A1001 CG1 CG2
REMARK 470 ILE A1005 CG1 CG2 CD1
REMARK 470 ARG A1024 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1027 CG OD1 OD2
REMARK 470 ARG A1047 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1048 CG OD1 OD2
REMARK 470 LEU A1050 CG CD1 CD2
REMARK 470 ASP A1059 CG OD1 OD2
REMARK 470 GLN A1070 CG CD OE1 NE2
REMARK 470 ARG A1072 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1158 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1313 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1336 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL A 840 H MET A 851 1.53
REMARK 500 H VAL A 840 O MET A 851 1.57
REMARK 500 O ARG A 1190 HZ3 LYS A 1222 1.59
REMARK 500 HE ARG A 551 OD2 ASP A 573 1.60
REMARK 500 OE2 GLU A 1235 OH TYR A 1270 2.02
REMARK 500 O ALA A 545 NH1 ARG A 571 2.16
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 CYS A 432 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 CYS A1365 CA - CB - SG ANGL. DEV. = 6.8 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 ALA A 42 166.57 175.81
REMARK 500 ASP A 61 -56.61 -122.67
REMARK 500 THR A 220 -68.52 -107.42
REMARK 500 CYS A 293 -173.35 -172.72
REMARK 500 GLU A 345 97.81 -52.21
REMARK 500 ASP A 382 -113.55 38.39
REMARK 500 ALA A 460 -62.45 -94.91
REMARK 500 ALA A 478 -61.77 -120.25
REMARK 500 ASP A 482 -117.85 54.51
REMARK 500 HIS A 646 73.58 61.80
REMARK 500 ALA A 658 153.12 -48.03
REMARK 500 ARG A 729 60.27 -164.73
REMARK 500 THR A 766 -19.90 -47.90
REMARK 500 THR A 769 81.11 62.02
REMARK 500 ILE A 770 -56.48 52.24
REMARK 500 SER A 899 -61.77 -93.52
REMARK 500 ALA A 909 -120.20 39.34
REMARK 500 VAL A 910 66.86 -112.60
REMARK 500 ASP A 912 -73.56 -78.71
REMARK 500 ARG A 922 -61.11 -128.82
REMARK 500 PRO A 946 159.02 -41.11
REMARK 500 ARG A 983 -65.97 -123.93
REMARK 500 PRO A1037 56.89 -91.82
REMARK 500 PHE A1065 -62.04 -93.51
REMARK 500 GLN A1070 49.92 -97.55
REMARK 500 PHE A1080 -166.68 -75.18
REMARK 500 PRO A1096 162.69 -48.64
REMARK 500 ALA A1113 66.16 -117.83
REMARK 500 LEU A1121 -70.30 -53.22
REMARK 500 CYS A1146 -127.48 48.00
REMARK 500 ASN A1165 33.81 -86.13
REMARK 500 ALA A1234 -74.69 -47.24
REMARK 500 THR A1236 -155.59 -93.48
REMARK 500 PRO A1239 -177.14 -64.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 283 0.24 SIDE CHAIN
REMARK 500 ARG A 871 0.09 SIDE CHAIN
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 PNS A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KFG A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KFJ A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1406
DBREF 6N8E A -19 1390 PDB 6N8E 6N8E -19 1390
SEQRES 1 A 1410 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 1410 LEU VAL PRO ARG GLY SER HIS MET GLN ALA LEU ASN PRO
SEQRES 3 A 1410 ALA ASP VAL LEU PRO LEU THR ALA ALA GLN ASN ALA ILE
SEQRES 4 A 1410 TRP ILE GLY HIS GLN LEU ASP PRO ALA SER ALA ALA TYR
SEQRES 5 A 1410 ASN VAL ALA ALA HIS VAL GLY VAL ASP ALA ALA LEU ASP
SEQRES 6 A 1410 ALA ASP LEU LEU ARG ARG ALA PHE ASP ILE THR ALA ASN
SEQRES 7 A 1410 GLU THR ASP CYS LEU ARG MET ARG PHE VAL GLU THR GLY
SEQRES 8 A 1410 SER ASP GLY GLU GLY ALA VAL ARG GLN THR PHE VAL ALA
SEQRES 9 A 1410 ARG ALA GLU THR ALA PHE VAL MET ARG ASP PHE ARG ALA
SEQRES 10 A 1410 GLU PRO ASP SER THR GLY ALA ALA HIS ALA TRP MET ALA
SEQRES 11 A 1410 ALA ASP VAL ARG ARG ARG ILE ASP LEU SER SER GLY CYS
SEQRES 12 A 1410 LEU VAL HIS ALA ALA LEU LEU ARG THR GLY THR ARG ASP
SEQRES 13 A 1410 TYR VAL TYR LEU ARG SER HIS HIS ILE ALA LEU ASP GLY
SEQRES 14 A 1410 PHE GLY LEU ALA MET VAL LEU ARG ARG VAL ALA HIS VAL
SEQRES 15 A 1410 TYR GLY ALA LEU VAL ALA GLY ARG GLU PRO ALA ALA ALA
SEQRES 16 A 1410 ALA PHE GLY ALA PHE ALA GLU VAL ILE ASP ALA ASP ARG
SEQRES 17 A 1410 ALA TYR HIS ALA SER ALA ALA CYS GLU ALA ASP ARG ALA
SEQRES 18 A 1410 TYR TRP ARG ALA TYR CYS ALA GLY LEU ASP ASP VAL PRO
SEQRES 19 A 1410 THR LEU CYS ALA GLY THR SER LEU PRO SER GLU ILE ALA
SEQRES 20 A 1410 VAL CYS HIS THR ALA PRO VAL PRO ALA ALA LEU VAL GLU
SEQRES 21 A 1410 ARG LEU HIS ASP PHE ALA ASN GLU CYS GLY THR HIS TRP
SEQRES 22 A 1410 ILE ASN VAL VAL VAL ALA ALA PHE GLY ALA PHE VAL GLY
SEQRES 23 A 1410 ARG ALA THR SER ARG ARG ASP ILE THR ILE GLY VAL PRO
SEQRES 24 A 1410 MET MET ASN ARG LEU GLY GLY VAL ALA ALA SER VAL PRO
SEQRES 25 A 1410 CYS THR THR ALA ASN VAL LEU PRO LEU SER LEU ASP VAL
SEQRES 26 A 1410 ARG PRO GLY ALA ARG ALA GLU ALA LEU VAL GLU ALA VAL
SEQRES 27 A 1410 ASP THR GLY LEU ALA GLY MET ARG ARG HIS GLN ARG TYR
SEQRES 28 A 1410 ARG ALA GLU ASP ILE ARG ARG ASP CYS HIS LEU ILE GLY
SEQRES 29 A 1410 GLU GLY ARG ARG LEU THR GLY PRO GLN ILE ASN VAL ASP
SEQRES 30 A 1410 VAL TYR THR ASP PRO ILE ALA PHE GLY ASP ALA SER GLY
SEQRES 31 A 1410 ILE ALA ARG VAL VAL SER ALA GLY PRO ALA ASP ASP VAL
SEQRES 32 A 1410 SER LEU MET ILE GLN ARG GLY ASP MET ALA ASP ALA LEU
SEQRES 33 A 1410 THR ILE VAL GLY MET ALA ASN PRO ALA LEU TYR ARG PRO
SEQRES 34 A 1410 HIS GLU LEU ALA ARG TRP ILE GLU ARG PHE VAL ALA PHE
SEQRES 35 A 1410 THR THR ALA PHE VAL ALA ASP PRO SER CYS PRO VAL GLY
SEQRES 36 A 1410 ARG LEU ASP ALA TYR LEU PRO GLY ASP GLY VAL GLU VAL
SEQRES 37 A 1410 HIS LEU PRO GLU PRO ALA LYS ARG SER LEU GLY ALA THR
SEQRES 38 A 1410 LEU VAL GLU VAL PHE GLU ARG ARG VAL ALA GLU ARG PRO
SEQRES 39 A 1410 HIS ALA SER ALA VAL THR LEU ASP HIS THR THR TRP ASP
SEQRES 40 A 1410 TYR ALA GLU LEU ASP ALA ARG ALA ASN ARG LEU ALA ARG
SEQRES 41 A 1410 HIS PHE ALA ALA SER THR PRO ALA ARG GLY ASN LEU ARG
SEQRES 42 A 1410 VAL ALA LEU LEU LEU PRO ARG THR LEU ASP ALA ILE VAL
SEQRES 43 A 1410 ALA ILE LEU ALA THR LEU LYS PHE GLY ALA ALA TYR VAL
SEQRES 44 A 1410 PRO ILE ASP PRO ASP ALA PRO ALA GLU ARG ILE ARG ALA
SEQRES 45 A 1410 ILE ILE ASP ASP CYS ASP ALA ALA LEU VAL VAL THR THR
SEQRES 46 A 1410 VAL ASP LEU ALA SER ARG ILE ASP ALA SER GLY ARG ARG
SEQRES 47 A 1410 LEU VAL VAL LEU ASP ALA PRO ASP THR ARG ALA ALA VAL
SEQRES 48 A 1410 ALA ALA ALA SER ALA ALA PRO PRO SER ARG ASP GLY GLU
SEQRES 49 A 1410 GLY PRO ARG ALA ASP ASP LEU ALA TYR ILE ILE PHE THR
SEQRES 50 A 1410 SER GLY SER THR GLY LYS PRO LYS GLY VAL LYS ILE THR
SEQRES 51 A 1410 HIS ARG ASN VAL VAL ARG LEU PHE GLU ALA THR ASP ALA
SEQRES 52 A 1410 TRP PHE HIS TYR ARG ASP ASP ASP VAL TRP THR MET CYS
SEQRES 53 A 1410 HIS ALA TYR VAL PHE ASP ALA SER VAL TRP GLU MET TRP
SEQRES 54 A 1410 GLY ALA LEU LEU HIS GLY GLY ARG LEU VAL VAL VAL PRO
SEQRES 55 A 1410 PRO GLU THR THR ARG ALA PRO ASP ALA LEU LEU GLU LEU
SEQRES 56 A 1410 VAL VAL ARG GLU GLY VAL THR VAL PHE GLY GLN ILE PRO
SEQRES 57 A 1410 SER ALA PHE TYR ARG PHE MET GLU ALA GLN ALA ASP HIS
SEQRES 58 A 1410 PRO ALA LEU ARG GLN ALA LEU ARG LEU ARG TYR GLN CYS
SEQRES 59 A 1410 PHE GLY GLY GLU ALA LEU ASP PRO SER ARG LEU LYS PRO
SEQRES 60 A 1410 TRP PHE ASP TRP HIS ARG ASP SER GLY THR ARG LEU LEU
SEQRES 61 A 1410 ASN MET TYR GLY ILE THR GLU THR THR ILE ASN ALA THR
SEQRES 62 A 1410 TYR ARG PHE ILE ASP GLU ARG ASP VAL ASP THR GLY ARG
SEQRES 63 A 1410 GLY SER LEU ILE GLY GLU VAL TYR ALA ASP LEU GLY ILE
SEQRES 64 A 1410 VAL VAL LEU ASP ASP ALA LEU ARG PRO VAL PRO ALA GLY
SEQRES 65 A 1410 ALA TYR GLY GLU MET TYR VAL THR GLY ALA GLY LEU ALA
SEQRES 66 A 1410 GLN GLY TYR LEU ASN ARG PRO ASP LEU ASP ALA VAL ARG
SEQRES 67 A 1410 PHE VAL ALA ASN PRO TYR GLY PRO ALA GLY THR ARG MET
SEQRES 68 A 1410 TYR ARG SER GLY ASP VAL ALA ARG LEU HIS PRO ASP GLY
SEQRES 69 A 1410 VAL LEU GLU TYR VAL GLY ARG ALA ASP GLN GLN VAL LYS
SEQRES 70 A 1410 VAL ARG GLY TYR ARG ILE GLU LEU GLY GLU VAL GLU ALA
SEQRES 71 A 1410 ARG LEU ARG GLU TYR ALA PRO VAL SER ASP ALA VAL VAL
SEQRES 72 A 1410 SER VAL ARG ARG ASP ALA VAL GLY ASP VAL GLN LEU VAL
SEQRES 73 A 1410 ALA HIS VAL VAL ALA ARG ARG GLY GLU CYS LEU ASP VAL
SEQRES 74 A 1410 GLU ALA LEU ARG ALA HIS LEU ARG GLU ARG VAL PRO ALA
SEQRES 75 A 1410 TYR MET VAL PRO ALA ALA PHE GLY THR LEU ASP ALA LEU
SEQRES 76 A 1410 PRO MET THR ARG ASN GLY LYS VAL ASP ARG LYS ALA LEU
SEQRES 77 A 1410 PRO ASP ILE SER THR ALA THR GLU ARG VAL VAL GLU PRO
SEQRES 78 A 1410 PRO ARG ASP ALA LEU ASP GLU ARG ILE VAL GLU LEU TRP
SEQRES 79 A 1410 ARG GLU GLN CYS GLY ASP VAL ALA ILE GLY ILE ASP ASP
SEQRES 80 A 1410 ASN PHE PHE ASP VAL GLY GLY ASP SER ILE LYS ALA ILE
SEQRES 81 A 1410 ARG VAL ALA ARG ALA LEU ASP MET PRO VAL MET ALA LEU
SEQRES 82 A 1410 PHE ASP ALA PRO THR VAL ARG ALA CYS ALA ASP TYR LEU
SEQRES 83 A 1410 ARG ASP ALA LEU ALA ASP GLY ALA GLY ASP ALA ALA ASP
SEQRES 84 A 1410 ARG THR LEU HIS HIS PHE LYS ARG PRO ALA GLN ALA ARG
SEQRES 85 A 1410 VAL HIS MET VAL CYS VAL PRO PHE ALA GLY GLY SER ALA
SEQRES 86 A 1410 LEU SER TYR ARG GLU LEU ALA ARG ALA LEU PRO ASP GLY
SEQRES 87 A 1410 PHE ALA CYS SER ALA LEU GLN LEU PRO GLY HIS ASP PRO
SEQRES 88 A 1410 ALA ALA PRO ASP GLU ALA PHE VAL ASP LEU ASP THR THR
SEQRES 89 A 1410 ILE ASP ARG ALA VAL ASP ARG LEU LEU ALA GLU ALA ALA
SEQRES 90 A 1410 ALA PRO ILE VAL VAL TYR GLY HIS CYS ALA GLY ASN ALA
SEQRES 91 A 1410 LEU ALA VAL ALA LEU VAL ARG ARG LEU ALA GLY ALA GLY
SEQRES 92 A 1410 ALA ASN VAL ILE GLY LEU ALA ILE GLY GLY MET LEU LEU
SEQRES 93 A 1410 ASP GLU ASP ALA ASP ALA VAL LEU ASP GLU VAL GLY ALA
SEQRES 94 A 1410 ARG SER GLY GLU ASN ILE VAL ASP PHE LEU ARG GLN ILE
SEQRES 95 A 1410 GLY GLY PHE LYS ASP VAL LEU ASP ALA GLY THR LEU ALA
SEQRES 96 A 1410 ALA ILE ALA ARG MET THR LYS HIS ASP ALA MET GLN ALA
SEQRES 97 A 1410 ALA THR PHE PHE ALA ALA GLU THR ARG ALA PRO ALA ARG
SEQRES 98 A 1410 LEU ASP VAL PRO LEU HIS VAL VAL ILE GLY GLY GLN ASP
SEQRES 99 A 1410 PRO LEU THR PRO ASP TYR ALA ARG ARG TYR LEU ASP TRP
SEQRES 100 A 1410 ARG ARG TYR SER ASP ALA VAL GLU LEU ASP VAL ILE PRO
SEQRES 101 A 1410 ASP GLY GLY HIS TYR PHE VAL THR GLU HIS ALA ASP THR
SEQRES 102 A 1410 LEU ALA GLY LEU LEU ALA ALA ARG TRP LEU PRO ALA SER
SEQRES 103 A 1410 ARG ALA PRO GLU ARG GLU ARG GLN ALA LEU ARG ALA PHE
SEQRES 104 A 1410 LEU ASN PRO PHE ASP ASP GLU ASP GLU VAL HIS TYR LEU
SEQRES 105 A 1410 LEU ALA ASN ASP LEU GLY ALA HIS SER LEU TRP PRO ALA
SEQRES 106 A 1410 PHE VAL PRO LEU PRO GLY GLY TRP ARG VAL VAL ALA GLY
SEQRES 107 A 1410 PRO ALA SER ARG ASP ALA CYS LEU GLY ALA LEU PRO ASN
SEQRES 108 A 1410 PRO PRO ILE GLY VAL SER ALA ALA VAL ALA ALA ARG GLU
SEQRES 109 A 1410 THR ALA GLU HIS CYS VAL
HET PNS A1401 41
HET KFG A1402 13
HET KFJ A1403 28
HET CL A1404 1
HET PO4 A1405 5
HET PO4 A1406 5
HETNAM PNS 4'-PHOSPHOPANTETHEINE
HETNAM KFG DIMETHYL HYDROGEN PHOSPHATE
HETNAM KFJ 4-(4-NITROPHENYL)-L-THREONINE
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PNS C11 H23 N2 O7 P S
FORMUL 3 KFG C2 H7 O4 P
FORMUL 4 KFJ C10 H12 N2 O5
FORMUL 5 CL CL 1-
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 8 HOH *11(H2 O)
HELIX 1 AA1 THR A 13 ASP A 26 1 14
HELIX 2 AA2 ASP A 45 THR A 60 1 16
HELIX 3 AA3 ASP A 61 LEU A 63 5 3
HELIX 4 AA4 ASP A 100 VAL A 113 1 14
HELIX 5 AA5 ASP A 148 ALA A 168 1 21
HELIX 6 AA6 PHE A 180 SER A 193 1 14
HELIX 7 AA7 SER A 193 CYS A 207 1 15
HELIX 8 AA8 PRO A 235 GLY A 250 1 16
HELIX 9 AA9 HIS A 252 SER A 270 1 19
HELIX 10 AB1 GLY A 286 VAL A 291 5 6
HELIX 11 AB2 ARG A 310 GLN A 329 1 20
HELIX 12 AB3 ARG A 332 CYS A 340 1 9
HELIX 13 AB4 ARG A 408 VAL A 427 1 20
HELIX 14 AB5 PRO A 433 LEU A 437 5 5
HELIX 15 AB6 LEU A 441 GLY A 445 5 5
HELIX 16 AB7 THR A 461 ARG A 473 1 13
HELIX 17 AB8 TYR A 488 THR A 506 1 19
HELIX 18 AB9 THR A 521 PHE A 534 1 14
HELIX 19 AC1 PRO A 546 ASP A 558 1 13
HELIX 20 AC2 ASP A 567 ILE A 572 5 6
HELIX 21 AC3 ALA A 584 ALA A 593 1 10
HELIX 22 AC4 PRO A 598 GLY A 603 5 6
HELIX 23 AC5 HIS A 631 HIS A 646 1 16
HELIX 24 AC6 ASP A 662 LEU A 673 1 12
HELIX 25 AC7 PRO A 682 ARG A 687 1 6
HELIX 26 AC8 ALA A 688 GLU A 699 1 12
HELIX 27 AC9 ILE A 707 HIS A 721 1 15
HELIX 28 AD1 HIS A 721 GLN A 726 1 6
HELIX 29 AD2 ASP A 741 ARG A 744 5 4
HELIX 30 AD3 LEU A 745 ARG A 753 1 9
HELIX 31 AD4 ILE A 765 THR A 769 5 5
HELIX 32 AD5 ARG A 780 GLY A 785 1 6
HELIX 33 AD6 ARG A 831 ARG A 838 1 8
HELIX 34 AD7 ASP A 873 GLN A 875 5 3
HELIX 35 AD8 GLU A 884 LEU A 892 1 9
HELIX 36 AD9 GLU A 930 GLU A 938 1 9
HELIX 37 AE1 ASP A 984 GLY A 999 1 16
HELIX 38 AE2 ILE A 1017 LEU A 1026 1 10
HELIX 39 AE3 PRO A 1029 ALA A 1036 1 8
HELIX 40 AE4 THR A 1038 ASP A 1048 1 11
HELIX 41 AE5 SER A 1084 SER A 1087 5 4
HELIX 42 AE6 TYR A 1088 ARG A 1093 1 6
HELIX 43 AE7 ASP A 1120 ALA A 1136 1 17
HELIX 44 AE8 ALA A 1147 GLY A 1161 1 15
HELIX 45 AE9 ASP A 1179 GLY A 1188 1 10
HELIX 46 AF1 SER A 1191 ILE A 1202 1 12
HELIX 47 AF2 ASP A 1210 GLU A 1235 1 26
HELIX 48 AF3 ASP A 1259 TYR A 1264 1 6
HELIX 49 AF4 LEU A 1265 SER A 1271 5 7
HELIX 50 AF5 TYR A 1285 HIS A 1290 1 6
HELIX 51 AF6 HIS A 1290 LEU A 1303 1 14
HELIX 52 AF7 ASN A 1321 ASP A 1325 5 5
HELIX 53 AF8 SER A 1361 GLY A 1367 1 7
SHEET 1 AA1 3 VAL A 9 PRO A 11 0
SHEET 2 AA1 3 VAL A 78 PHE A 82 -1 O GLN A 80 N LEU A 10
SHEET 3 AA1 3 MET A 65 GLU A 69 -1 N VAL A 68 O ARG A 79
SHEET 1 AA2 6 ALA A 89 ASP A 94 0
SHEET 2 AA2 6 HIS A 126 ARG A 131 1 O ALA A 127 N ALA A 89
SHEET 3 AA2 6 ASP A 136 HIS A 143 -1 O TYR A 137 N LEU A 130
SHEET 4 AA2 6 ASN A 33 VAL A 40 -1 N VAL A 34 O SER A 142
SHEET 5 AA2 6 ALA A 368 SER A 376 -1 O ARG A 373 N HIS A 37
SHEET 6 AA2 6 ILE A 363 PHE A 365 -1 N ILE A 363 O GLY A 370
SHEET 1 AA3 4 VAL A 228 PRO A 233 0
SHEET 2 AA3 4 LEU A 396 ALA A 402 -1 O ILE A 398 N ALA A 232
SHEET 3 AA3 4 VAL A 383 ARG A 389 -1 N GLN A 388 O THR A 397
SHEET 4 AA3 4 GLN A 353 ILE A 354 1 N GLN A 353 O VAL A 383
SHEET 1 AA4 2 ASP A 273 MET A 280 0
SHEET 2 AA4 2 ASN A 297 ASP A 304 -1 O ASN A 297 N MET A 280
SHEET 1 AA5 4 THR A 484 ASP A 487 0
SHEET 2 AA5 4 SER A 477 LEU A 481 -1 N ALA A 478 O TRP A 486
SHEET 3 AA5 4 ARG A 677 VAL A 680 1 O LEU A 678 N ALA A 478
SHEET 4 AA5 4 VAL A 652 MET A 655 1 N MET A 655 O VAL A 679
SHEET 1 AA6 4 ALA A 537 ILE A 541 0
SHEET 2 AA6 4 ARG A 513 LEU A 517 1 N VAL A 514 O ALA A 537
SHEET 3 AA6 4 LEU A 561 THR A 564 1 O VAL A 563 N ALA A 515
SHEET 4 AA6 4 LEU A 579 VAL A 581 1 O VAL A 580 N THR A 564
SHEET 1 AA7 3 LEU A 611 PHE A 616 0
SHEET 2 AA7 3 GLY A 626 THR A 630 -1 O ILE A 629 N ALA A 612
SHEET 3 AA7 3 GLY A 827 TYR A 828 -1 O GLY A 827 N LYS A 628
SHEET 1 AA8 9 VAL A 703 GLN A 706 0
SHEET 2 AA8 9 TYR A 732 PHE A 735 1 O CYS A 734 N PHE A 704
SHEET 3 AA8 9 LEU A 760 ASN A 761 1 O LEU A 760 N GLN A 733
SHEET 4 AA8 9 THR A 773 PHE A 776 -1 O ARG A 775 N ASN A 761
SHEET 5 AA8 9 LEU A 789 VAL A 793 -1 O GLU A 792 N TYR A 774
SHEET 6 AA8 9 LEU A 866 ARG A 871 -1 O LEU A 866 N ILE A 790
SHEET 7 AA8 9 ARG A 850 LEU A 860 -1 N VAL A 857 O GLY A 870
SHEET 8 AA8 9 TYR A 814 GLY A 821 -1 N GLY A 815 O ALA A 858
SHEET 9 AA8 9 LEU A 797 LEU A 802 -1 N VAL A 800 O TYR A 818
SHEET 1 AA9 8 VAL A 703 GLN A 706 0
SHEET 2 AA9 8 TYR A 732 PHE A 735 1 O CYS A 734 N PHE A 704
SHEET 3 AA9 8 LEU A 760 ASN A 761 1 O LEU A 760 N GLN A 733
SHEET 4 AA9 8 THR A 773 PHE A 776 -1 O ARG A 775 N ASN A 761
SHEET 5 AA9 8 LEU A 789 VAL A 793 -1 O GLU A 792 N TYR A 774
SHEET 6 AA9 8 LEU A 866 ARG A 871 -1 O LEU A 866 N ILE A 790
SHEET 7 AA9 8 ARG A 850 LEU A 860 -1 N VAL A 857 O GLY A 870
SHEET 8 AA9 8 PHE A 839 ALA A 841 -1 N VAL A 840 O MET A 851
SHEET 1 AB1 2 VAL A 876 LYS A 877 0
SHEET 2 AB1 2 ARG A 882 ILE A 883 -1 O ILE A 883 N VAL A 876
SHEET 1 AB2 3 ASP A 900 ARG A 906 0
SHEET 2 AB2 3 GLN A 914 VAL A 920 -1 O VAL A 916 N SER A 904
SHEET 3 AB2 3 ALA A 948 THR A 951 1 O GLY A 950 N VAL A 919
SHEET 1 AB3 7 LEU A1062 LYS A1066 0
SHEET 2 AB3 7 PHE A1099 LEU A1104 -1 O ALA A1103 N HIS A1063
SHEET 3 AB3 7 VAL A1073 VAL A1078 1 N MET A1075 O ALA A1100
SHEET 4 AB3 7 ILE A1140 HIS A1145 1 O TYR A1143 N VAL A1076
SHEET 5 AB3 7 GLY A1168 GLY A1172 1 O GLY A1172 N GLY A1144
SHEET 6 AB3 7 LEU A1246 GLY A1251 1 O HIS A1247 N ILE A1171
SHEET 7 AB3 7 VAL A1274 ILE A1279 1 O ASP A1277 N VAL A1248
SHEET 1 AB4 3 HIS A1340 PRO A1344 0
SHEET 2 AB4 3 HIS A1330 ALA A1334 -1 N LEU A1333 O SER A1341
SHEET 3 AB4 3 ARG A1354 ALA A1360 -1 O ALA A1360 N HIS A1330
LINK OG SER A1016 P24 PNS A1401 1555 1555 1.61
SITE 1 AC1 8 ALA A 18 LEU A 25 ALA A 296 GLU A 334
SITE 2 AC1 8 ARG A 337 ARG A 338 ILE A 343 SER A1016
SITE 1 AC2 4 GLY A 821 LEU A 824 THR A 849 ARG A 850
SITE 1 AC3 12 PHE A 661 ASP A 662 ALA A 663 TRP A 666
SITE 2 AC3 12 GLN A 706 GLY A 736 GLY A 737 GLY A 764
SITE 3 AC3 12 ILE A 765 THR A 766 ILE A 770 ASN A 771
SITE 1 AC4 1 ARG A1362
SITE 1 AC5 5 HIS A 23 GLN A 24 ARG A 116 ASP A 118
SITE 2 AC5 5 LEU A 119
SITE 1 AC6 4 GLU A 240 HIS A 243 ASP A 394 ARG A 571
CRYST1 81.325 154.345 183.905 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012296 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005438 0.00000
TER 19416 PRO A1370
MASTER 614 0 6 53 58 0 10 610004 1 93 109
END |