HEADER TRANSFERASE 31-AUG-15 5DHR
TITLE CRYSTAL STRUCTURE OF NAD KINASE 1 FROM LISTERIA MONOCYTOGENES IN
TITLE 2 COMPLEX WITH A NOVEL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD KINASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ATP-DEPENDENT NAD KINASE;
COMPND 5 EC: 2.7.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES SEROVAR 1/2A (STRAIN
SOURCE 3 ATCC BAA-679 / EGD-E);
SOURCE 4 ORGANISM_TAXID: 169963;
SOURCE 5 STRAIN: ATCC BAA-679 / EGD-E;
SOURCE 6 GENE: NADK1, LMO0968;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TETRAMERIC NAD KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GELIN,J.PAOLETTI,L.ASSAIRI,V.HUTEAU,S.POCHET,G.LABESSE
REVDAT 3 06-SEP-17 5DHR 1 REMARK
REVDAT 2 09-NOV-16 5DHR 1 JRNL
REVDAT 1 14-SEP-16 5DHR 0
JRNL AUTH J.PAOLETTI,L.ASSAIRI,M.GELIN,V.HUTEAU,M.A.NAHORI,
JRNL AUTH 2 O.DUSSURGET,G.LABESSE,S.POCHET
JRNL TITL 8-THIOALKYL-ADENOSINE DERIVATIVES INHIBIT LISTERIA
JRNL TITL 2 MONOCYTOGENES NAD KINASE THROUGH A NOVEL BINDING MODE.
JRNL REF EUR.J.MED.CHEM. V. 124 1041 2016
JRNL REFN ISSN 0223-5234
JRNL PMID 27783975
JRNL DOI 10.1016/J.EJMECH.2016.10.033
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 87321
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2719
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 57.3204 - 6.1617 1.00 4483 133 0.2021 0.2409
REMARK 3 2 6.1617 - 4.8915 1.00 4474 142 0.1825 0.2451
REMARK 3 3 4.8915 - 4.2734 0.99 4461 146 0.1469 0.1983
REMARK 3 4 4.2734 - 3.8828 1.00 4413 156 0.1603 0.1724
REMARK 3 5 3.8828 - 3.6046 1.00 4533 128 0.1749 0.2017
REMARK 3 6 3.6046 - 3.3921 1.00 4454 167 0.1837 0.2078
REMARK 3 7 3.3921 - 3.2222 1.00 4446 166 0.2200 0.2693
REMARK 3 8 3.2222 - 3.0819 1.00 4471 142 0.2437 0.2630
REMARK 3 9 3.0819 - 2.9633 1.00 4455 152 0.2719 0.4080
REMARK 3 10 2.9633 - 2.8611 1.00 4490 144 0.2890 0.3445
REMARK 3 11 2.8611 - 2.7716 1.00 4410 137 0.2993 0.3952
REMARK 3 12 2.7716 - 2.6924 1.00 4520 126 0.2933 0.3500
REMARK 3 13 2.6924 - 2.6215 1.00 4432 149 0.3118 0.3883
REMARK 3 14 2.6215 - 2.5575 1.00 4488 119 0.3178 0.3678
REMARK 3 15 2.5575 - 2.4994 0.99 4510 117 0.3259 0.3140
REMARK 3 16 2.4994 - 2.4462 0.99 4441 152 0.3586 0.3813
REMARK 3 17 2.4462 - 2.3973 0.99 4441 164 0.3850 0.4661
REMARK 3 18 2.3973 - 2.3520 0.98 4356 145 0.3861 0.4031
REMARK 3 19 2.3520 - 2.3100 0.98 4324 134 0.3730 0.4089
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.33
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 : 0.004 8594
REMARK 3 ANGLE : 0.508 11641
REMARK 3 CHIRALITY : 0.022 1261
REMARK 3 PLANARITY : 0.002 1482
REMARK 3 DIHEDRAL : 10.203 3072
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0235 24.9918 0.8301
REMARK 3 T TENSOR
REMARK 3 T11: 0.4038 T22: 0.2766
REMARK 3 T33: 0.7130 T12: -0.0512
REMARK 3 T13: -0.0107 T23: 0.0832
REMARK 3 L TENSOR
REMARK 3 L11: 2.4855 L22: 6.0324
REMARK 3 L33: 4.5843 L12: 2.5390
REMARK 3 L13: -0.6348 L23: -1.4801
REMARK 3 S TENSOR
REMARK 3 S11: 0.1280 S12: -0.1775 S13: 0.2972
REMARK 3 S21: 0.4862 S22: -0.4108 S23: -0.4167
REMARK 3 S31: -0.4213 S32: 0.3240 S33: 0.2336
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 101:264)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1383 1.1841 2.9079
REMARK 3 T TENSOR
REMARK 3 T11: 0.2861 T22: 0.1826
REMARK 3 T33: 0.3050 T12: 0.0479
REMARK 3 T13: 0.0213 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 4.0325 L22: 2.5457
REMARK 3 L33: 2.2855 L12: 0.8674
REMARK 3 L13: -0.2784 L23: -1.3144
REMARK 3 S TENSOR
REMARK 3 S11: 0.0920 S12: 0.1785 S13: 0.1148
REMARK 3 S21: -0.0300 S22: -0.2791 S23: -0.3188
REMARK 3 S31: -0.0987 S32: 0.1183 S33: 0.1399
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 1:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5688 -23.7550 30.2491
REMARK 3 T TENSOR
REMARK 3 T11: 0.7329 T22: 1.3090
REMARK 3 T33: 0.8819 T12: 0.1901
REMARK 3 T13: -0.1382 T23: 0.9855
REMARK 3 L TENSOR
REMARK 3 L11: 1.2923 L22: 1.3308
REMARK 3 L33: 2.6934 L12: -0.2901
REMARK 3 L13: 0.4112 L23: -1.4408
REMARK 3 S TENSOR
REMARK 3 S11: -0.4225 S12: -0.7513 S13: -0.7338
REMARK 3 S21: 0.0657 S22: -0.3311 S23: -0.5906
REMARK 3 S31: 0.7283 S32: 0.7934 S33: -0.4488
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 101:264)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8709 1.0835 28.0090
REMARK 3 T TENSOR
REMARK 3 T11: 0.7506 T22: 0.6804
REMARK 3 T33: 0.3490 T12: -0.1901
REMARK 3 T13: -0.1046 T23: 0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 2.7238 L22: 1.3426
REMARK 3 L33: 2.6931 L12: 0.0354
REMARK 3 L13: 0.1495 L23: -0.2575
REMARK 3 S TENSOR
REMARK 3 S11: 0.1103 S12: -1.0776 S13: 0.0768
REMARK 3 S21: 0.7621 S22: -0.3162 S23: -0.2063
REMARK 3 S31: -0.5030 S32: 0.3547 S33: 0.1247
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN C AND RESID 1:100)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4909 -13.8349 -7.9468
REMARK 3 T TENSOR
REMARK 3 T11: 0.7619 T22: 0.9697
REMARK 3 T33: 0.8504 T12: -0.1732
REMARK 3 T13: -0.0474 T23: -0.4537
REMARK 3 L TENSOR
REMARK 3 L11: 3.2623 L22: 2.4177
REMARK 3 L33: 3.1216 L12: 2.0777
REMARK 3 L13: 2.4464 L23: 0.3911
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: 0.7211 S13: -0.8589
REMARK 3 S21: -0.5491 S22: -0.2067 S23: 0.6126
REMARK 3 S31: 0.9304 S32: -0.6679 S33: 0.0110
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN C AND RESID 101:264)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.7080 7.6756 3.8979
REMARK 3 T TENSOR
REMARK 3 T11: 0.2957 T22: 0.4346
REMARK 3 T33: 0.3272 T12: 0.1337
REMARK 3 T13: -0.0128 T23: -0.1016
REMARK 3 L TENSOR
REMARK 3 L11: 2.6701 L22: 2.6598
REMARK 3 L33: 3.2947 L12: -0.4531
REMARK 3 L13: -0.4380 L23: -0.4804
REMARK 3 S TENSOR
REMARK 3 S11: 0.0994 S12: 0.2173 S13: 0.1675
REMARK 3 S21: -0.1316 S22: -0.1346 S23: 0.2377
REMARK 3 S31: -0.3506 S32: -0.7363 S33: 0.0313
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN D AND RESID 1:100)
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5505 19.2195 38.5920
REMARK 3 T TENSOR
REMARK 3 T11: 0.9334 T22: 1.4092
REMARK 3 T33: 0.6168 T12: 0.3134
REMARK 3 T13: 0.0844 T23: -0.3692
REMARK 3 L TENSOR
REMARK 3 L11: 4.7130 L22: 2.9983
REMARK 3 L33: 1.7599 L12: -2.4458
REMARK 3 L13: -2.8548 L23: 1.3240
REMARK 3 S TENSOR
REMARK 3 S11: 0.1812 S12: -0.3831 S13: 0.6944
REMARK 3 S21: 0.1120 S22: -0.4447 S23: 0.2258
REMARK 3 S31: -0.7853 S32: -1.3664 S33: 0.0321
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN D AND RESID 101:264)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1751 -2.4156 26.8429
REMARK 3 T TENSOR
REMARK 3 T11: 0.5137 T22: 0.6895
REMARK 3 T33: 0.3421 T12: -0.0552
REMARK 3 T13: 0.1332 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 3.0339 L22: 1.8459
REMARK 3 L33: 2.4132 L12: -0.5548
REMARK 3 L13: -0.8074 L23: 0.4825
REMARK 3 S TENSOR
REMARK 3 S11: -0.1164 S12: -0.7365 S13: -0.2086
REMARK 3 S21: 0.6690 S22: -0.0949 S23: 0.3432
REMARK 3 S31: 0.1466 S32: -0.4990 S33: 0.1795
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 5DHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000213152.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978002
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44486
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
REMARK 200 RESOLUTION RANGE LOW (A) : 65.499
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : 0.39200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 MM SODIUM BROMIDE, 220 MM POTASSIUM
REMARK 280 CITRATE, PH 4.8-5.1, GLYCEROL 6%, 15-16% W/V POLYETHYLENE GLYCOL
REMARK 280 400, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 59.35500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 112
REMARK 465 LEU A 265
REMARK 465 GLU A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 GLY B 110
REMARK 465 ILE B 111
REMARK 465 GLY B 112
REMARK 465 LYS B 113
REMARK 465 GLY B 130
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 GLU C 26
REMARK 465 LYS C 92
REMARK 465 ILE C 111
REMARK 465 GLY C 112
REMARK 465 ASP C 264
REMARK 465 LEU C 265
REMARK 465 GLU C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 GLY D 110
REMARK 465 ILE D 111
REMARK 465 GLY D 112
REMARK 465 LYS D 113
REMARK 465 ASP D 264
REMARK 465 LEU D 265
REMARK 465 GLU D 266
REMARK 465 HIS D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 HIS D 272
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 GLU A 11 CG CD OE1 OE2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 ASP A 60 CG OD1 OD2
REMARK 470 LYS A 85 CG CD CE NZ
REMARK 470 ILE A 111 CG1 CG2 CD1
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 ARG A 247 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 96 CG CD OE1 NE2
REMARK 470 LYS B 108 CG CD CE NZ
REMARK 470 ARG B 190 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 193 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 216 CG OD1 OD2
REMARK 470 LYS C 12 CG CD CE NZ
REMARK 470 LEU C 15 CG CD1 CD2
REMARK 470 ASP C 28 CB CG OD1 OD2
REMARK 470 ARG C 58 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 61 CG CD OE1 OE2
REMARK 470 GLU C 82 CG CD OE1 OE2
REMARK 470 LYS C 85 CG CD CE NZ
REMARK 470 LEU C 89 CG CD1 CD2
REMARK 470 ALA C 91 CB
REMARK 470 GLU C 94 CG CD OE1 OE2
REMARK 470 GLN C 96 CG CD OE1 NE2
REMARK 470 LYS C 97 CG CD CE NZ
REMARK 470 LYS C 113 CG CD CE NZ
REMARK 470 LYS C 114 CG CD CE NZ
REMARK 470 GLN C 232 CG CD OE1 NE2
REMARK 470 ARG C 249 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 2 CG CD CE NZ
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 LYS D 12 CG CD CE NZ
REMARK 470 ASP D 33 CG OD1 OD2
REMARK 470 VAL D 34 CG1 CG2
REMARK 470 ASP D 60 CG OD1 OD2
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 GLU D 94 CG CD OE1 OE2
REMARK 470 LYS D 108 CG CD CE NZ
REMARK 470 LYS D 114 CB CG CD CE NZ
REMARK 470 GLU D 115 CG CD OE1 OE2
REMARK 470 LEU D 227 CG CD1 CD2
REMARK 470 GLN D 232 CG CD OE1 NE2
REMARK 470 ARG D 249 CG CD NE CZ NH1 NH2
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 OG1 THR A 125 OG SER A 220 2.18
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 ASN A 122 -74.13 -96.05
REMARK 500 ALA A 162 -122.62 -107.77
REMARK 500 ASN A 189 -161.71 -114.28
REMARK 500 TYR A 192 72.12 -117.29
REMARK 500 ASN A 213 -67.33 -126.27
REMARK 500 ASP A 222 -111.70 56.74
REMARK 500 PHE A 248 -64.21 -120.28
REMARK 500 ARG A 249 -159.92 -80.16
REMARK 500 ILE A 262 -77.56 -95.85
REMARK 500 ASN B 122 -72.44 -102.20
REMARK 500 ALA B 162 -122.81 -95.67
REMARK 500 ASN B 213 -23.62 -141.34
REMARK 500 ASP B 222 -110.64 55.92
REMARK 500 ASP B 222 -108.59 55.92
REMARK 500 ILE B 262 -81.66 -83.15
REMARK 500 ASP C 28 45.13 -92.11
REMARK 500 LYS C 114 -166.33 57.60
REMARK 500 ASN C 122 -71.72 -94.89
REMARK 500 ALA C 162 -117.61 -108.83
REMARK 500 PRO C 174 6.84 -67.33
REMARK 500 TYR C 192 74.09 -114.84
REMARK 500 PRO C 202 -169.83 -78.51
REMARK 500 ASN C 213 -60.10 -127.65
REMARK 500 ASP C 222 -111.78 57.51
REMARK 500 PHE C 248 -77.48 -105.39
REMARK 500 ASN D 122 -70.60 -96.67
REMARK 500 SER D 129 48.81 -96.84
REMARK 500 ALA D 162 -118.29 -104.78
REMARK 500 ASN D 188 74.06 41.40
REMARK 500 ASN D 189 -152.41 -124.30
REMARK 500 PRO D 202 -168.32 -78.77
REMARK 500 ASN D 213 -69.19 -129.65
REMARK 500 ASP D 222 -112.54 56.89
REMARK 500 PHE D 248 -61.30 -105.64
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 C 451 DISTANCE = 6.36 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5AJ A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5AJ B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5AJ C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5AJ D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DHU RELATED DB: PDB
REMARK 900 RELATED ID: 5DHT RELATED DB: PDB
REMARK 900 RELATED ID: 5DHS RELATED DB: PDB
REMARK 900 RELATED ID: 5DHQ RELATED DB: PDB
REMARK 900 RELATED ID: 5DHP RELATED DB: PDB
DBREF 5DHR A 1 264 UNP Q8Y8D7 NADK1_LISMO 1 264
DBREF 5DHR B 1 264 UNP Q8Y8D7 NADK1_LISMO 1 264
DBREF 5DHR C 1 264 UNP Q8Y8D7 NADK1_LISMO 1 264
DBREF 5DHR D 1 264 UNP Q8Y8D7 NADK1_LISMO 1 264
SEQADV 5DHR LEU A 265 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR GLU A 266 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS A 267 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS A 268 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS A 269 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS A 270 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS A 271 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS A 272 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR LEU B 265 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR GLU B 266 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS B 267 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS B 268 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS B 269 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS B 270 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS B 271 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS B 272 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR LEU C 265 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR GLU C 266 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS C 267 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS C 268 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS C 269 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS C 270 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS C 271 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS C 272 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR LEU D 265 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR GLU D 266 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS D 267 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS D 268 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS D 269 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS D 270 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS D 271 UNP Q8Y8D7 EXPRESSION TAG
SEQADV 5DHR HIS D 272 UNP Q8Y8D7 EXPRESSION TAG
SEQRES 1 A 272 MET LYS TYR MET ILE THR SER LYS GLY ASP GLU LYS SER
SEQRES 2 A 272 ASP LEU LEU ARG LEU ASN MET ILE ALA GLY PHE GLY GLU
SEQRES 3 A 272 TYR ASP MET GLU TYR ASP ASP VAL GLU PRO GLU ILE VAL
SEQRES 4 A 272 ILE SER ILE GLY GLY ASP GLY THR PHE LEU SER ALA PHE
SEQRES 5 A 272 HIS GLN TYR GLU GLU ARG LEU ASP GLU ILE ALA PHE ILE
SEQRES 6 A 272 GLY ILE HIS THR GLY HIS LEU GLY PHE TYR ALA ASP TRP
SEQRES 7 A 272 ARG PRO ALA GLU ALA ASP LYS LEU VAL LYS LEU LEU ALA
SEQRES 8 A 272 LYS GLY GLU TYR GLN LYS VAL SER TYR PRO LEU LEU LYS
SEQRES 9 A 272 THR THR VAL LYS TYR GLY ILE GLY LYS LYS GLU ALA THR
SEQRES 10 A 272 TYR LEU ALA LEU ASN GLU SER THR VAL LYS SER SER GLY
SEQRES 11 A 272 GLY PRO PHE VAL VAL ASP VAL VAL ILE ASN ASP ILE HIS
SEQRES 12 A 272 PHE GLU ARG PHE ARG GLY ASP GLY LEU CYS MET SER THR
SEQRES 13 A 272 PRO SER GLY THR THR ALA TYR ASN LYS SER LEU GLY GLY
SEQRES 14 A 272 ALA LEU MET HIS PRO SER ILE GLU ALA MET GLN LEU THR
SEQRES 15 A 272 GLU MET ALA SER ILE ASN ASN ARG VAL TYR ARG THR ILE
SEQRES 16 A 272 GLY SER PRO LEU VAL PHE PRO LYS HIS HIS VAL VAL SER
SEQRES 17 A 272 LEU GLN PRO VAL ASN ASP LYS ASP PHE GLN ILE SER VAL
SEQRES 18 A 272 ASP HIS LEU SER ILE LEU HIS ARG ASP VAL GLN GLU ILE
SEQRES 19 A 272 ARG TYR GLU VAL SER ALA LYS LYS ILE HIS PHE ALA ARG
SEQRES 20 A 272 PHE ARG SER PHE PRO PHE TRP ARG ARG VAL HIS ASP SER
SEQRES 21 A 272 PHE ILE GLU ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 272 MET LYS TYR MET ILE THR SER LYS GLY ASP GLU LYS SER
SEQRES 2 B 272 ASP LEU LEU ARG LEU ASN MET ILE ALA GLY PHE GLY GLU
SEQRES 3 B 272 TYR ASP MET GLU TYR ASP ASP VAL GLU PRO GLU ILE VAL
SEQRES 4 B 272 ILE SER ILE GLY GLY ASP GLY THR PHE LEU SER ALA PHE
SEQRES 5 B 272 HIS GLN TYR GLU GLU ARG LEU ASP GLU ILE ALA PHE ILE
SEQRES 6 B 272 GLY ILE HIS THR GLY HIS LEU GLY PHE TYR ALA ASP TRP
SEQRES 7 B 272 ARG PRO ALA GLU ALA ASP LYS LEU VAL LYS LEU LEU ALA
SEQRES 8 B 272 LYS GLY GLU TYR GLN LYS VAL SER TYR PRO LEU LEU LYS
SEQRES 9 B 272 THR THR VAL LYS TYR GLY ILE GLY LYS LYS GLU ALA THR
SEQRES 10 B 272 TYR LEU ALA LEU ASN GLU SER THR VAL LYS SER SER GLY
SEQRES 11 B 272 GLY PRO PHE VAL VAL ASP VAL VAL ILE ASN ASP ILE HIS
SEQRES 12 B 272 PHE GLU ARG PHE ARG GLY ASP GLY LEU CYS MET SER THR
SEQRES 13 B 272 PRO SER GLY THR THR ALA TYR ASN LYS SER LEU GLY GLY
SEQRES 14 B 272 ALA LEU MET HIS PRO SER ILE GLU ALA MET GLN LEU THR
SEQRES 15 B 272 GLU MET ALA SER ILE ASN ASN ARG VAL TYR ARG THR ILE
SEQRES 16 B 272 GLY SER PRO LEU VAL PHE PRO LYS HIS HIS VAL VAL SER
SEQRES 17 B 272 LEU GLN PRO VAL ASN ASP LYS ASP PHE GLN ILE SER VAL
SEQRES 18 B 272 ASP HIS LEU SER ILE LEU HIS ARG ASP VAL GLN GLU ILE
SEQRES 19 B 272 ARG TYR GLU VAL SER ALA LYS LYS ILE HIS PHE ALA ARG
SEQRES 20 B 272 PHE ARG SER PHE PRO PHE TRP ARG ARG VAL HIS ASP SER
SEQRES 21 B 272 PHE ILE GLU ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 272 MET LYS TYR MET ILE THR SER LYS GLY ASP GLU LYS SER
SEQRES 2 C 272 ASP LEU LEU ARG LEU ASN MET ILE ALA GLY PHE GLY GLU
SEQRES 3 C 272 TYR ASP MET GLU TYR ASP ASP VAL GLU PRO GLU ILE VAL
SEQRES 4 C 272 ILE SER ILE GLY GLY ASP GLY THR PHE LEU SER ALA PHE
SEQRES 5 C 272 HIS GLN TYR GLU GLU ARG LEU ASP GLU ILE ALA PHE ILE
SEQRES 6 C 272 GLY ILE HIS THR GLY HIS LEU GLY PHE TYR ALA ASP TRP
SEQRES 7 C 272 ARG PRO ALA GLU ALA ASP LYS LEU VAL LYS LEU LEU ALA
SEQRES 8 C 272 LYS GLY GLU TYR GLN LYS VAL SER TYR PRO LEU LEU LYS
SEQRES 9 C 272 THR THR VAL LYS TYR GLY ILE GLY LYS LYS GLU ALA THR
SEQRES 10 C 272 TYR LEU ALA LEU ASN GLU SER THR VAL LYS SER SER GLY
SEQRES 11 C 272 GLY PRO PHE VAL VAL ASP VAL VAL ILE ASN ASP ILE HIS
SEQRES 12 C 272 PHE GLU ARG PHE ARG GLY ASP GLY LEU CYS MET SER THR
SEQRES 13 C 272 PRO SER GLY THR THR ALA TYR ASN LYS SER LEU GLY GLY
SEQRES 14 C 272 ALA LEU MET HIS PRO SER ILE GLU ALA MET GLN LEU THR
SEQRES 15 C 272 GLU MET ALA SER ILE ASN ASN ARG VAL TYR ARG THR ILE
SEQRES 16 C 272 GLY SER PRO LEU VAL PHE PRO LYS HIS HIS VAL VAL SER
SEQRES 17 C 272 LEU GLN PRO VAL ASN ASP LYS ASP PHE GLN ILE SER VAL
SEQRES 18 C 272 ASP HIS LEU SER ILE LEU HIS ARG ASP VAL GLN GLU ILE
SEQRES 19 C 272 ARG TYR GLU VAL SER ALA LYS LYS ILE HIS PHE ALA ARG
SEQRES 20 C 272 PHE ARG SER PHE PRO PHE TRP ARG ARG VAL HIS ASP SER
SEQRES 21 C 272 PHE ILE GLU ASP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 272 MET LYS TYR MET ILE THR SER LYS GLY ASP GLU LYS SER
SEQRES 2 D 272 ASP LEU LEU ARG LEU ASN MET ILE ALA GLY PHE GLY GLU
SEQRES 3 D 272 TYR ASP MET GLU TYR ASP ASP VAL GLU PRO GLU ILE VAL
SEQRES 4 D 272 ILE SER ILE GLY GLY ASP GLY THR PHE LEU SER ALA PHE
SEQRES 5 D 272 HIS GLN TYR GLU GLU ARG LEU ASP GLU ILE ALA PHE ILE
SEQRES 6 D 272 GLY ILE HIS THR GLY HIS LEU GLY PHE TYR ALA ASP TRP
SEQRES 7 D 272 ARG PRO ALA GLU ALA ASP LYS LEU VAL LYS LEU LEU ALA
SEQRES 8 D 272 LYS GLY GLU TYR GLN LYS VAL SER TYR PRO LEU LEU LYS
SEQRES 9 D 272 THR THR VAL LYS TYR GLY ILE GLY LYS LYS GLU ALA THR
SEQRES 10 D 272 TYR LEU ALA LEU ASN GLU SER THR VAL LYS SER SER GLY
SEQRES 11 D 272 GLY PRO PHE VAL VAL ASP VAL VAL ILE ASN ASP ILE HIS
SEQRES 12 D 272 PHE GLU ARG PHE ARG GLY ASP GLY LEU CYS MET SER THR
SEQRES 13 D 272 PRO SER GLY THR THR ALA TYR ASN LYS SER LEU GLY GLY
SEQRES 14 D 272 ALA LEU MET HIS PRO SER ILE GLU ALA MET GLN LEU THR
SEQRES 15 D 272 GLU MET ALA SER ILE ASN ASN ARG VAL TYR ARG THR ILE
SEQRES 16 D 272 GLY SER PRO LEU VAL PHE PRO LYS HIS HIS VAL VAL SER
SEQRES 17 D 272 LEU GLN PRO VAL ASN ASP LYS ASP PHE GLN ILE SER VAL
SEQRES 18 D 272 ASP HIS LEU SER ILE LEU HIS ARG ASP VAL GLN GLU ILE
SEQRES 19 D 272 ARG TYR GLU VAL SER ALA LYS LYS ILE HIS PHE ALA ARG
SEQRES 20 D 272 PHE ARG SER PHE PRO PHE TRP ARG ARG VAL HIS ASP SER
SEQRES 21 D 272 PHE ILE GLU ASP LEU GLU HIS HIS HIS HIS HIS HIS
HET CIT A 301 13
HET 5AJ A 302 37
HET CIT B 301 13
HET 5AJ B 302 37
HET GOL C 301 6
HET 5AJ C 302 37
HET 5AJ D 301 37
HETNAM CIT CITRIC ACID
HETNAM 5AJ 5'-AZIDO-8-[(2-{[2-(1H-BENZIMIDAZOL-2-YL)ETHYL]AMINO}-
HETNAM 2 5AJ 2-OXOETHYL)SULFANYL]-5'-DEOXYADENOSINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 CIT 2(C6 H8 O7)
FORMUL 6 5AJ 4(C21 H23 N11 O4 S)
FORMUL 9 GOL C3 H8 O3
FORMUL 12 HOH *206(H2 O)
HELIX 1 AA1 ASP A 10 GLY A 25 1 16
HELIX 2 AA2 GLY A 44 TYR A 55 1 12
HELIX 3 AA3 ARG A 58 GLU A 61 5 4
HELIX 4 AA4 ARG A 79 ALA A 81 5 3
HELIX 5 AA5 GLU A 82 GLY A 93 1 12
HELIX 6 AA6 PRO A 157 THR A 161 5 5
HELIX 7 AA7 ALA A 162 LEU A 167 1 6
HELIX 8 AA8 PRO A 252 ILE A 262 1 11
HELIX 9 AA9 ASP B 10 PHE B 24 1 15
HELIX 10 AB1 GLY B 25 TYR B 27 5 3
HELIX 11 AB2 GLY B 44 TYR B 55 1 12
HELIX 12 AB3 ARG B 79 ALA B 81 5 3
HELIX 13 AB4 GLU B 82 LYS B 92 1 11
HELIX 14 AB5 ALA B 162 LEU B 167 1 6
HELIX 15 AB6 PRO B 252 ILE B 262 1 11
HELIX 16 AB7 ASP C 10 ALA C 22 1 13
HELIX 17 AB8 GLY C 23 GLY C 25 5 3
HELIX 18 AB9 GLY C 44 TYR C 55 1 12
HELIX 19 AC1 ARG C 58 GLU C 61 5 4
HELIX 20 AC2 ARG C 79 ALA C 81 5 3
HELIX 21 AC3 GLU C 82 ALA C 91 1 10
HELIX 22 AC4 PRO C 157 THR C 161 5 5
HELIX 23 AC5 ALA C 162 LEU C 167 1 6
HELIX 24 AC6 PRO C 252 ILE C 262 1 11
HELIX 25 AC7 ASP D 10 GLY D 25 1 16
HELIX 26 AC8 GLY D 44 GLN D 54 1 11
HELIX 27 AC9 ARG D 58 GLU D 61 5 4
HELIX 28 AD1 GLU D 82 GLY D 93 1 12
HELIX 29 AD2 ALA D 162 LEU D 167 1 6
HELIX 30 AD3 PRO D 252 ILE D 262 1 11
SHEET 1 AA1 7 GLU A 30 TYR A 31 0
SHEET 2 AA1 7 LYS A 2 SER A 7 1 N TYR A 3 O GLU A 30
SHEET 3 AA1 7 ILE A 38 GLY A 43 1 O ILE A 40 N THR A 6
SHEET 4 AA1 7 ALA A 63 HIS A 68 1 O ILE A 65 N SER A 41
SHEET 5 AA1 7 VAL A 231 ARG A 247 1 O HIS A 244 N PHE A 64
SHEET 6 AA1 7 GLN A 96 TYR A 109 -1 N GLN A 96 O ARG A 247
SHEET 7 AA1 7 ALA A 116 ALA A 120 -1 O TYR A 118 N THR A 105
SHEET 1 AA2 8 GLU A 30 TYR A 31 0
SHEET 2 AA2 8 LYS A 2 SER A 7 1 N TYR A 3 O GLU A 30
SHEET 3 AA2 8 ILE A 38 GLY A 43 1 O ILE A 40 N THR A 6
SHEET 4 AA2 8 ALA A 63 HIS A 68 1 O ILE A 65 N SER A 41
SHEET 5 AA2 8 VAL A 231 ARG A 247 1 O HIS A 244 N PHE A 64
SHEET 6 AA2 8 VAL A 207 PRO A 211 -1 N LEU A 209 O ILE A 234
SHEET 7 AA2 8 PHE A 133 ILE A 139 -1 N ASP A 136 O GLN A 210
SHEET 8 AA2 8 ILE A 142 GLY A 149 -1 O PHE A 144 N VAL A 137
SHEET 1 AA3 7 LEU A 224 HIS A 228 0
SHEET 2 AA3 7 PHE A 217 VAL A 221 -1 N VAL A 221 O LEU A 224
SHEET 3 AA3 7 GLU A 123 SER A 128 -1 N THR A 125 O SER A 220
SHEET 4 AA3 7 GLY A 151 SER A 155 -1 O MET A 154 N SER A 124
SHEET 5 AA3 7 ALA A 178 MET A 184 -1 O GLN A 180 N SER A 155
SHEET 6 AA3 7 LEU A 199 PRO A 202 -1 O LEU A 199 N LEU A 181
SHEET 7 AA3 7 LEU B 171 MET B 172 1 O LEU B 171 N VAL A 200
SHEET 1 AA4 9 LEU A 171 MET A 172 0
SHEET 2 AA4 9 LEU B 199 PHE B 201 1 O VAL B 200 N LEU A 171
SHEET 3 AA4 9 MET B 179 MET B 184 -1 N LEU B 181 O LEU B 199
SHEET 4 AA4 9 HIS B 143 SER B 155 -1 N SER B 155 O GLN B 180
SHEET 5 AA4 9 PRO B 132 ILE B 139 -1 N VAL B 137 O PHE B 144
SHEET 6 AA4 9 VAL B 207 PRO B 211 -1 O SER B 208 N VAL B 138
SHEET 7 AA4 9 GLU B 233 ARG B 247 -1 O ILE B 234 N LEU B 209
SHEET 8 AA4 9 GLN B 96 LYS B 108 -1 N LYS B 108 O GLU B 233
SHEET 9 AA4 9 ALA B 116 ALA B 120 -1 O TYR B 118 N THR B 105
SHEET 1 AA510 TYR B 3 SER B 7 0
SHEET 2 AA510 ILE B 38 GLY B 43 1 O ILE B 40 N THR B 6
SHEET 3 AA510 ALA B 63 HIS B 68 1 O ILE B 65 N SER B 41
SHEET 4 AA510 GLU B 233 ARG B 247 1 O HIS B 244 N PHE B 64
SHEET 5 AA510 VAL B 207 PRO B 211 -1 N LEU B 209 O ILE B 234
SHEET 6 AA510 PRO B 132 ILE B 139 -1 N VAL B 138 O SER B 208
SHEET 7 AA510 HIS B 143 SER B 155 -1 O PHE B 144 N VAL B 137
SHEET 8 AA510 GLU B 123 SER B 129 -1 N VAL B 126 O LEU B 152
SHEET 9 AA510 PHE B 217 VAL B 221 -1 O SER B 220 N THR B 125
SHEET 10 AA510 LEU B 224 SER B 225 -1 O LEU B 224 N VAL B 221
SHEET 1 AA6 7 GLU C 30 TYR C 31 0
SHEET 2 AA6 7 LYS C 2 SER C 7 1 N TYR C 3 O GLU C 30
SHEET 3 AA6 7 ILE C 38 GLY C 43 1 O ILE C 40 N MET C 4
SHEET 4 AA6 7 ALA C 63 HIS C 68 1 O ILE C 65 N SER C 41
SHEET 5 AA6 7 VAL C 231 ARG C 247 1 O HIS C 244 N PHE C 64
SHEET 6 AA6 7 GLN C 96 TYR C 109 -1 N VAL C 98 O PHE C 245
SHEET 7 AA6 7 GLU C 115 ALA C 120 -1 O ALA C 116 N VAL C 107
SHEET 1 AA7 8 GLU C 30 TYR C 31 0
SHEET 2 AA7 8 LYS C 2 SER C 7 1 N TYR C 3 O GLU C 30
SHEET 3 AA7 8 ILE C 38 GLY C 43 1 O ILE C 40 N MET C 4
SHEET 4 AA7 8 ALA C 63 HIS C 68 1 O ILE C 65 N SER C 41
SHEET 5 AA7 8 VAL C 231 ARG C 247 1 O HIS C 244 N PHE C 64
SHEET 6 AA7 8 VAL C 207 PRO C 211 -1 N LEU C 209 O ILE C 234
SHEET 7 AA7 8 PHE C 133 ILE C 139 -1 N VAL C 138 O SER C 208
SHEET 8 AA7 8 ILE C 142 GLY C 149 -1 O GLU C 145 N VAL C 137
SHEET 1 AA8 7 LEU C 224 HIS C 228 0
SHEET 2 AA8 7 PHE C 217 VAL C 221 -1 N PHE C 217 O HIS C 228
SHEET 3 AA8 7 GLU C 123 LYS C 127 -1 N THR C 125 O SER C 220
SHEET 4 AA8 7 GLY C 151 SER C 155 -1 O MET C 154 N SER C 124
SHEET 5 AA8 7 MET C 179 MET C 184 -1 O GLN C 180 N SER C 155
SHEET 6 AA8 7 LEU C 199 PHE C 201 -1 O LEU C 199 N LEU C 181
SHEET 7 AA8 7 LEU D 171 MET D 172 1 O LEU D 171 N VAL C 200
SHEET 1 AA9 7 LEU C 171 MET C 172 0
SHEET 2 AA9 7 LEU D 199 PHE D 201 1 O VAL D 200 N LEU C 171
SHEET 3 AA9 7 MET D 179 MET D 184 -1 N MET D 179 O PHE D 201
SHEET 4 AA9 7 GLY D 151 SER D 155 -1 N SER D 155 O GLN D 180
SHEET 5 AA9 7 GLU D 123 SER D 128 -1 N SER D 124 O MET D 154
SHEET 6 AA9 7 PHE D 217 VAL D 221 -1 O GLN D 218 N LYS D 127
SHEET 7 AA9 7 LEU D 224 HIS D 228 -1 O ILE D 226 N ILE D 219
SHEET 1 AB1 6 TYR D 3 SER D 7 0
SHEET 2 AB1 6 ILE D 38 GLY D 43 1 O ILE D 40 N THR D 6
SHEET 3 AB1 6 ALA D 63 HIS D 68 1 O ILE D 67 N SER D 41
SHEET 4 AB1 6 GLU D 233 ARG D 247 1 O HIS D 244 N PHE D 64
SHEET 5 AB1 6 GLN D 96 LYS D 108 -1 N GLN D 96 O ARG D 247
SHEET 6 AB1 6 ALA D 116 ALA D 120 -1 O TYR D 118 N THR D 105
SHEET 1 AB2 6 ALA D 76 TRP D 78 0
SHEET 2 AB2 6 ALA D 63 HIS D 68 1 N GLY D 66 O TRP D 78
SHEET 3 AB2 6 GLU D 233 ARG D 247 1 O HIS D 244 N PHE D 64
SHEET 4 AB2 6 VAL D 207 PRO D 211 -1 N LEU D 209 O ILE D 234
SHEET 5 AB2 6 PHE D 133 ILE D 139 -1 N VAL D 138 O SER D 208
SHEET 6 AB2 6 ILE D 142 GLY D 149 -1 O PHE D 144 N VAL D 137
SITE 1 AC1 8 VAL A 98 TYR A 100 HIS A 173 PHE A 251
SITE 2 AC1 8 PRO A 252 PHE A 253 ARG A 256 HOH A 406
SITE 1 AC2 13 ASN A 122 GLU A 123 ALA A 162 TYR A 163
SITE 2 AC2 13 SER A 166 HIS A 223 HOH A 413 GLY C 131
SITE 3 AC2 13 PRO C 132 ARG C 148 GLY C 149 ASP C 150
SITE 4 AC2 13 ALA C 185
SITE 1 AC3 7 VAL B 98 TYR B 100 HIS B 173 PRO B 252
SITE 2 AC3 7 PHE B 253 ARG B 256 HOH B 411
SITE 1 AC4 14 ASN B 122 GLU B 123 LYS B 127 ALA B 162
SITE 2 AC4 14 TYR B 163 SER B 166 ASP B 222 HIS B 223
SITE 3 AC4 14 GLY D 131 PRO D 132 ARG D 148 GLY D 149
SITE 4 AC4 14 ASP D 150 ALA D 185
SITE 1 AC5 4 ASP A 150 LYS C 127 ASP C 150 LEU C 167
SITE 1 AC6 14 GLY A 131 PRO A 132 ARG A 148 GLY A 149
SITE 2 AC6 14 ASP A 150 ALA A 185 GLY C 46 LEU C 49
SITE 3 AC6 14 ASN C 122 GLU C 123 ALA C 162 TYR C 163
SITE 4 AC6 14 SER C 166 ASP C 222
SITE 1 AC7 12 GLY B 131 ARG B 148 GLY B 149 ASP B 150
SITE 2 AC7 12 ALA B 185 GLY D 46 ASN D 122 GLU D 123
SITE 3 AC7 12 ALA D 162 TYR D 163 SER D 166 HIS D 223
CRYST1 66.530 118.710 66.600 90.00 100.43 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015031 0.000000 0.002767 0.00000
SCALE2 0.000000 0.008424 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015267 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
