HEADER TRANSFERASE 09-JUL-11 3STC
TITLE CRYSTAL STRUCTURE OF LOOP 7 TRUNCATED MUTANT OF 3-DEOXY-D-MANNO-
TITLE 2 OCTULOSONATE 8-PHOSPHATE SYNTHASE (KDO8PS) FROM NEISSERIA
TITLE 3 MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 3-DEOXY-D-MANNO-OCTULOSONIC ACID 8-PHOSPHATE SYNTHASE, KDO-
COMPND 5 8-PHOSPHATE SYNTHASE, KDO 8-P SYNTHASE, KDOPS, PHOSPHO-2-DEHYDRO-3-
COMPND 6 DEOXYOCTONATE ALDOLASE;
COMPND 7 EC: 2.5.1.55;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 122586;
SOURCE 4 STRAIN: MC58;
SOURCE 5 GENE: KDSA, NMB1283;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS MANNO-OCTULOSONATE, SYNTHASE, LIPOPOLYSACCHARIDE, KDOP, KDO8 KDOPS,
KEYWDS 2 KDO8PS, TIM BARREL, BIOSYNTHESIS, TRANSFERASE, LYASE,
KEYWDS 3 LIPOPOLYSACCHARIDE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.ALLISON,G.B.JAMESON,E.J.PARKER
REVDAT 2 01-NOV-23 3STC 1 REMARK SEQADV LINK
REVDAT 1 23-NOV-11 3STC 0
JRNL AUTH T.M.ALLISON,R.D.HUTTON,W.JIAO,B.J.GLOYNE,E.B.NIMMO,
JRNL AUTH 2 G.B.JAMESON,E.J.PARKER
JRNL TITL AN EXTENDED (BETA)7(ALPHA)7 SUBSTRATE-BINDING LOOP IS
JRNL TITL 2 ESSENTIAL FOR EFFICIENT CATALYSIS BY
JRNL TITL 3 3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE SYNTHASE
JRNL REF BIOCHEMISTRY V. 50 9318 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21942786
JRNL DOI 10.1021/BI201231E
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 88211
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4415
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5676
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.4780
REMARK 3 BIN FREE R VALUE SET COUNT : 326
REMARK 3 BIN FREE R VALUE : 0.4950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7843
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.87000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : -0.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.827
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8059 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5390 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10881 ; 1.158 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13308 ; 0.864 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1038 ; 5.107 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1295 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8709 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1509 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5360 20.9650 48.0700
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.1558
REMARK 3 T33: 0.0299 T12: 0.0228
REMARK 3 T13: -0.0098 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.6192 L22: 0.3513
REMARK 3 L33: 0.4773 L12: 0.1683
REMARK 3 L13: -0.3899 L23: 0.0932
REMARK 3 S TENSOR
REMARK 3 S11: -0.1016 S12: 0.1020 S13: -0.0103
REMARK 3 S21: -0.1139 S22: 0.0484 S23: 0.0032
REMARK 3 S31: -0.0482 S32: -0.1332 S33: 0.0532
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9670 13.3730 84.1750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0827 T22: 0.1510
REMARK 3 T33: 0.0334 T12: -0.0028
REMARK 3 T13: 0.0138 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.3428 L22: 0.6436
REMARK 3 L33: 0.7841 L12: -0.4328
REMARK 3 L13: 0.1819 L23: 0.0131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0265 S12: -0.0188 S13: 0.0353
REMARK 3 S21: 0.0258 S22: 0.0064 S23: -0.0284
REMARK 3 S31: 0.0138 S32: -0.0143 S33: 0.0202
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 268
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4690 -1.4790 37.9110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.0983
REMARK 3 T33: 0.0090 T12: 0.0090
REMARK 3 T13: 0.0176 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.1474 L22: 0.2307
REMARK 3 L33: 0.5683 L12: -0.0536
REMARK 3 L13: 0.0501 L23: -0.0697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0405 S12: -0.0573 S13: 0.0072
REMARK 3 S21: -0.0795 S22: -0.0033 S23: -0.0316
REMARK 3 S31: 0.0180 S32: -0.0453 S33: 0.0438
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 268
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0760 -11.5370 73.1780
REMARK 3 T TENSOR
REMARK 3 T11: 0.2430 T22: 0.0762
REMARK 3 T33: 0.0163 T12: 0.0643
REMARK 3 T13: -0.0011 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.1932 L22: 1.2488
REMARK 3 L33: 0.7581 L12: -0.4717
REMARK 3 L13: -0.2625 L23: 0.5210
REMARK 3 S TENSOR
REMARK 3 S11: -0.1080 S12: -0.0000 S13: 0.0153
REMARK 3 S21: 0.3105 S22: 0.0698 S23: -0.0427
REMARK 3 S31: 0.2475 S32: 0.0235 S33: 0.0382
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 3 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3STC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95368
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88598
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 36.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.31300
REMARK 200 R SYM FOR SHELL (I) : 0.31300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2QKF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML PROTEIN (IN 10 MM BTP PH 7.5)
REMARK 280 MIXED 1:1 WITH RESERVOIR LIQUOR CONTAINING 100 MM NAOAC (PH 4.6)
REMARK 280 AND 0.6-3.0 M NACL. IMMEDIATELY PRIOR TO DATA COLLECTION,
REMARK 280 CRYSTALS WERE HARVESTED AND SOAKED BRIEFLY IN CRYOPROTECTANT
REMARK 280 SOLUTION, COMPRISING 20% GLYCEROL AND THE RESERVOIR SOLUTION,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
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 40.89000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.61000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.61000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.89000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.88000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 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 SER A 226
REMARK 465 HIS A 227
REMARK 465 PRO A 228
REMARK 465 ASP A 229
REMARK 465 PRO A 230
REMARK 465 LYS A 231
REMARK 465 LEU A 232
REMARK 465 ALA A 233
REMARK 465 LYS A 234
REMARK 465 CYS A 235
REMARK 465 ASP A 236
REMARK 465 GLY A 237
REMARK 465 PRO A 238
REMARK 465 SER A 239
REMARK 465 ALA A 240
REMARK 465 LEU A 241
REMARK 465 PRO A 242
REMARK 465 THR A 267
REMARK 465 ILE A 268
REMARK 465 GLU A 269
REMARK 465 HIS B 227
REMARK 465 PRO B 228
REMARK 465 ASP B 229
REMARK 465 PRO B 230
REMARK 465 LYS B 231
REMARK 465 LEU B 232
REMARK 465 ALA B 233
REMARK 465 LYS B 234
REMARK 465 CYS B 235
REMARK 465 ASP B 236
REMARK 465 GLY B 237
REMARK 465 PRO B 238
REMARK 465 THR B 267
REMARK 465 ILE B 268
REMARK 465 GLU B 269
REMARK 465 PRO C 230
REMARK 465 LYS C 231
REMARK 465 LEU C 232
REMARK 465 ALA C 233
REMARK 465 LYS C 234
REMARK 465 CYS C 235
REMARK 465 ASP C 236
REMARK 465 GLY C 237
REMARK 465 GLU C 269
REMARK 465 ASP D 229
REMARK 465 PRO D 230
REMARK 465 LYS D 231
REMARK 465 LEU D 232
REMARK 465 ALA D 233
REMARK 465 LYS D 234
REMARK 465 CYS D 235
REMARK 465 ASP D 236
REMARK 465 GLY D 237
REMARK 465 GLU D 269
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 ARG A 67 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 203 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 203 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 204 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 243 CG CD1 CD2
REMARK 470 ARG D 203 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 O HOH D 296 O HOH D 669 2.12
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 6 -122.79 51.98
REMARK 500 ARG A 165 19.64 -142.01
REMARK 500 ARG A 218 83.73 78.20
REMARK 500 ASN B 6 -119.80 53.20
REMARK 500 GLU B 26 -54.20 -122.97
REMARK 500 ASN B 59 62.71 -111.43
REMARK 500 ARG B 218 88.01 78.20
REMARK 500 ASN C 6 -119.89 50.00
REMARK 500 ARG C 218 82.47 82.05
REMARK 500 ASN D 6 -114.93 50.04
REMARK 500 ARG D 165 23.77 -140.61
REMARK 500 ARG D 218 86.97 82.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 272 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 103 O
REMARK 620 2 CYS C 106 O 88.4
REMARK 620 3 ASN C 130 OD1 81.8 75.5
REMARK 620 4 ASN C 130 OD1 85.6 85.0 10.2
REMARK 620 5 HOH C 630 O 150.6 120.6 100.2 92.2
REMARK 620 6 HOH C 631 O 96.5 90.6 166.0 175.1 88.1
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 CL A 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 271
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3STE RELATED DB: PDB
REMARK 900 RELATED ID: 3STF RELATED DB: PDB
REMARK 900 RELATED ID: 3STG RELATED DB: PDB
DBREF 3STC A 1 269 UNP Q9JZ55 KDSA_NEIMB 1 280
DBREF 3STC B 1 269 UNP Q9JZ55 KDSA_NEIMB 1 280
DBREF 3STC C 1 269 UNP Q9JZ55 KDSA_NEIMB 1 280
DBREF 3STC D 1 269 UNP Q9JZ55 KDSA_NEIMB 1 280
SEQADV 3STC A UNP Q9JZ55 GLN 202 DELETION
SEQADV 3STC A UNP Q9JZ55 THR 203 DELETION
SEQADV 3STC A UNP Q9JZ55 ARG 204 DELETION
SEQADV 3STC A UNP Q9JZ55 ASP 205 DELETION
SEQADV 3STC A UNP Q9JZ55 ALA 206 DELETION
SEQADV 3STC A UNP Q9JZ55 GLY 207 DELETION
SEQADV 3STC A UNP Q9JZ55 SER 208 DELETION
SEQADV 3STC A UNP Q9JZ55 ALA 209 DELETION
SEQADV 3STC A UNP Q9JZ55 ALA 210 DELETION
SEQADV 3STC A UNP Q9JZ55 SER 211 DELETION
SEQADV 3STC A UNP Q9JZ55 GLY 212 DELETION
SEQADV 3STC B UNP Q9JZ55 GLN 202 DELETION
SEQADV 3STC B UNP Q9JZ55 THR 203 DELETION
SEQADV 3STC B UNP Q9JZ55 ARG 204 DELETION
SEQADV 3STC B UNP Q9JZ55 ASP 205 DELETION
SEQADV 3STC B UNP Q9JZ55 ALA 206 DELETION
SEQADV 3STC B UNP Q9JZ55 GLY 207 DELETION
SEQADV 3STC B UNP Q9JZ55 SER 208 DELETION
SEQADV 3STC B UNP Q9JZ55 ALA 209 DELETION
SEQADV 3STC B UNP Q9JZ55 ALA 210 DELETION
SEQADV 3STC B UNP Q9JZ55 SER 211 DELETION
SEQADV 3STC B UNP Q9JZ55 GLY 212 DELETION
SEQADV 3STC C UNP Q9JZ55 GLN 202 DELETION
SEQADV 3STC C UNP Q9JZ55 THR 203 DELETION
SEQADV 3STC C UNP Q9JZ55 ARG 204 DELETION
SEQADV 3STC C UNP Q9JZ55 ASP 205 DELETION
SEQADV 3STC C UNP Q9JZ55 ALA 206 DELETION
SEQADV 3STC C UNP Q9JZ55 GLY 207 DELETION
SEQADV 3STC C UNP Q9JZ55 SER 208 DELETION
SEQADV 3STC C UNP Q9JZ55 ALA 209 DELETION
SEQADV 3STC C UNP Q9JZ55 ALA 210 DELETION
SEQADV 3STC C UNP Q9JZ55 SER 211 DELETION
SEQADV 3STC C UNP Q9JZ55 GLY 212 DELETION
SEQADV 3STC D UNP Q9JZ55 GLN 202 DELETION
SEQADV 3STC D UNP Q9JZ55 THR 203 DELETION
SEQADV 3STC D UNP Q9JZ55 ARG 204 DELETION
SEQADV 3STC D UNP Q9JZ55 ASP 205 DELETION
SEQADV 3STC D UNP Q9JZ55 ALA 206 DELETION
SEQADV 3STC D UNP Q9JZ55 GLY 207 DELETION
SEQADV 3STC D UNP Q9JZ55 SER 208 DELETION
SEQADV 3STC D UNP Q9JZ55 ALA 209 DELETION
SEQADV 3STC D UNP Q9JZ55 ALA 210 DELETION
SEQADV 3STC D UNP Q9JZ55 SER 211 DELETION
SEQADV 3STC D UNP Q9JZ55 GLY 212 DELETION
SEQRES 1 A 269 MET ASP ILE LYS ILE ASN ASP ILE THR LEU GLY ASN ASN
SEQRES 2 A 269 SER PRO PHE VAL LEU PHE GLY GLY ILE ASN VAL LEU GLU
SEQRES 3 A 269 SER LEU ASP SER THR LEU GLN THR CYS ALA HIS TYR VAL
SEQRES 4 A 269 GLU VAL THR ARG LYS LEU GLY ILE PRO TYR ILE PHE LYS
SEQRES 5 A 269 ALA SER PHE ASP LYS ALA ASN ARG SER SER ILE HIS SER
SEQRES 6 A 269 TYR ARG GLY VAL GLY LEU GLU GLU GLY LEU LYS ILE PHE
SEQRES 7 A 269 GLU LYS VAL LYS ALA GLU PHE GLY ILE PRO VAL ILE THR
SEQRES 8 A 269 ASP VAL HIS GLU PRO HIS GLN CYS GLN PRO VAL ALA GLU
SEQRES 9 A 269 VAL CYS ASP VAL ILE GLN LEU PRO ALA PHE LEU ALA ARG
SEQRES 10 A 269 GLN THR ASP LEU VAL VAL ALA MET ALA LYS THR GLY ASN
SEQRES 11 A 269 VAL VAL ASN ILE LYS LYS PRO GLN PHE LEU SER PRO SER
SEQRES 12 A 269 GLN MET LYS ASN ILE VAL GLU LYS PHE HIS GLU ALA GLY
SEQRES 13 A 269 ASN GLY LYS LEU ILE LEU CYS GLU ARG GLY SER SER PHE
SEQRES 14 A 269 GLY TYR ASP ASN LEU VAL VAL ASP MET LEU GLY PHE GLY
SEQRES 15 A 269 VAL MET LYS GLN THR CYS GLY ASN LEU PRO VAL ILE PHE
SEQRES 16 A 269 ASP VAL THR HIS SER LEU GLY ARG ARG ALA GLN ALA LEU
SEQRES 17 A 269 ASP LEU ALA LEU ALA GLY MET ALA THR ARG LEU ALA GLY
SEQRES 18 A 269 LEU PHE LEU GLU SER HIS PRO ASP PRO LYS LEU ALA LYS
SEQRES 19 A 269 CYS ASP GLY PRO SER ALA LEU PRO LEU HIS LEU LEU GLU
SEQRES 20 A 269 ASP PHE LEU ILE ARG ILE LYS ALA LEU ASP ASP LEU ILE
SEQRES 21 A 269 LYS SER GLN PRO ILE LEU THR ILE GLU
SEQRES 1 B 269 MET ASP ILE LYS ILE ASN ASP ILE THR LEU GLY ASN ASN
SEQRES 2 B 269 SER PRO PHE VAL LEU PHE GLY GLY ILE ASN VAL LEU GLU
SEQRES 3 B 269 SER LEU ASP SER THR LEU GLN THR CYS ALA HIS TYR VAL
SEQRES 4 B 269 GLU VAL THR ARG LYS LEU GLY ILE PRO TYR ILE PHE LYS
SEQRES 5 B 269 ALA SER PHE ASP LYS ALA ASN ARG SER SER ILE HIS SER
SEQRES 6 B 269 TYR ARG GLY VAL GLY LEU GLU GLU GLY LEU LYS ILE PHE
SEQRES 7 B 269 GLU LYS VAL LYS ALA GLU PHE GLY ILE PRO VAL ILE THR
SEQRES 8 B 269 ASP VAL HIS GLU PRO HIS GLN CYS GLN PRO VAL ALA GLU
SEQRES 9 B 269 VAL CYS ASP VAL ILE GLN LEU PRO ALA PHE LEU ALA ARG
SEQRES 10 B 269 GLN THR ASP LEU VAL VAL ALA MET ALA LYS THR GLY ASN
SEQRES 11 B 269 VAL VAL ASN ILE LYS LYS PRO GLN PHE LEU SER PRO SER
SEQRES 12 B 269 GLN MET LYS ASN ILE VAL GLU LYS PHE HIS GLU ALA GLY
SEQRES 13 B 269 ASN GLY LYS LEU ILE LEU CYS GLU ARG GLY SER SER PHE
SEQRES 14 B 269 GLY TYR ASP ASN LEU VAL VAL ASP MET LEU GLY PHE GLY
SEQRES 15 B 269 VAL MET LYS GLN THR CYS GLY ASN LEU PRO VAL ILE PHE
SEQRES 16 B 269 ASP VAL THR HIS SER LEU GLY ARG ARG ALA GLN ALA LEU
SEQRES 17 B 269 ASP LEU ALA LEU ALA GLY MET ALA THR ARG LEU ALA GLY
SEQRES 18 B 269 LEU PHE LEU GLU SER HIS PRO ASP PRO LYS LEU ALA LYS
SEQRES 19 B 269 CYS ASP GLY PRO SER ALA LEU PRO LEU HIS LEU LEU GLU
SEQRES 20 B 269 ASP PHE LEU ILE ARG ILE LYS ALA LEU ASP ASP LEU ILE
SEQRES 21 B 269 LYS SER GLN PRO ILE LEU THR ILE GLU
SEQRES 1 C 269 MET ASP ILE LYS ILE ASN ASP ILE THR LEU GLY ASN ASN
SEQRES 2 C 269 SER PRO PHE VAL LEU PHE GLY GLY ILE ASN VAL LEU GLU
SEQRES 3 C 269 SER LEU ASP SER THR LEU GLN THR CYS ALA HIS TYR VAL
SEQRES 4 C 269 GLU VAL THR ARG LYS LEU GLY ILE PRO TYR ILE PHE LYS
SEQRES 5 C 269 ALA SER PHE ASP LYS ALA ASN ARG SER SER ILE HIS SER
SEQRES 6 C 269 TYR ARG GLY VAL GLY LEU GLU GLU GLY LEU LYS ILE PHE
SEQRES 7 C 269 GLU LYS VAL LYS ALA GLU PHE GLY ILE PRO VAL ILE THR
SEQRES 8 C 269 ASP VAL HIS GLU PRO HIS GLN CYS GLN PRO VAL ALA GLU
SEQRES 9 C 269 VAL CYS ASP VAL ILE GLN LEU PRO ALA PHE LEU ALA ARG
SEQRES 10 C 269 GLN THR ASP LEU VAL VAL ALA MET ALA LYS THR GLY ASN
SEQRES 11 C 269 VAL VAL ASN ILE LYS LYS PRO GLN PHE LEU SER PRO SER
SEQRES 12 C 269 GLN MET LYS ASN ILE VAL GLU LYS PHE HIS GLU ALA GLY
SEQRES 13 C 269 ASN GLY LYS LEU ILE LEU CYS GLU ARG GLY SER SER PHE
SEQRES 14 C 269 GLY TYR ASP ASN LEU VAL VAL ASP MET LEU GLY PHE GLY
SEQRES 15 C 269 VAL MET LYS GLN THR CYS GLY ASN LEU PRO VAL ILE PHE
SEQRES 16 C 269 ASP VAL THR HIS SER LEU GLY ARG ARG ALA GLN ALA LEU
SEQRES 17 C 269 ASP LEU ALA LEU ALA GLY MET ALA THR ARG LEU ALA GLY
SEQRES 18 C 269 LEU PHE LEU GLU SER HIS PRO ASP PRO LYS LEU ALA LYS
SEQRES 19 C 269 CYS ASP GLY PRO SER ALA LEU PRO LEU HIS LEU LEU GLU
SEQRES 20 C 269 ASP PHE LEU ILE ARG ILE LYS ALA LEU ASP ASP LEU ILE
SEQRES 21 C 269 LYS SER GLN PRO ILE LEU THR ILE GLU
SEQRES 1 D 269 MET ASP ILE LYS ILE ASN ASP ILE THR LEU GLY ASN ASN
SEQRES 2 D 269 SER PRO PHE VAL LEU PHE GLY GLY ILE ASN VAL LEU GLU
SEQRES 3 D 269 SER LEU ASP SER THR LEU GLN THR CYS ALA HIS TYR VAL
SEQRES 4 D 269 GLU VAL THR ARG LYS LEU GLY ILE PRO TYR ILE PHE LYS
SEQRES 5 D 269 ALA SER PHE ASP LYS ALA ASN ARG SER SER ILE HIS SER
SEQRES 6 D 269 TYR ARG GLY VAL GLY LEU GLU GLU GLY LEU LYS ILE PHE
SEQRES 7 D 269 GLU LYS VAL LYS ALA GLU PHE GLY ILE PRO VAL ILE THR
SEQRES 8 D 269 ASP VAL HIS GLU PRO HIS GLN CYS GLN PRO VAL ALA GLU
SEQRES 9 D 269 VAL CYS ASP VAL ILE GLN LEU PRO ALA PHE LEU ALA ARG
SEQRES 10 D 269 GLN THR ASP LEU VAL VAL ALA MET ALA LYS THR GLY ASN
SEQRES 11 D 269 VAL VAL ASN ILE LYS LYS PRO GLN PHE LEU SER PRO SER
SEQRES 12 D 269 GLN MET LYS ASN ILE VAL GLU LYS PHE HIS GLU ALA GLY
SEQRES 13 D 269 ASN GLY LYS LEU ILE LEU CYS GLU ARG GLY SER SER PHE
SEQRES 14 D 269 GLY TYR ASP ASN LEU VAL VAL ASP MET LEU GLY PHE GLY
SEQRES 15 D 269 VAL MET LYS GLN THR CYS GLY ASN LEU PRO VAL ILE PHE
SEQRES 16 D 269 ASP VAL THR HIS SER LEU GLY ARG ARG ALA GLN ALA LEU
SEQRES 17 D 269 ASP LEU ALA LEU ALA GLY MET ALA THR ARG LEU ALA GLY
SEQRES 18 D 269 LEU PHE LEU GLU SER HIS PRO ASP PRO LYS LEU ALA LYS
SEQRES 19 D 269 CYS ASP GLY PRO SER ALA LEU PRO LEU HIS LEU LEU GLU
SEQRES 20 D 269 ASP PHE LEU ILE ARG ILE LYS ALA LEU ASP ASP LEU ILE
SEQRES 21 D 269 LYS SER GLN PRO ILE LEU THR ILE GLU
HET CL A 270 1
HET CL B 270 1
HET CL B 271 1
HET CL C 270 1
HET CL C 271 1
HET NA C 272 1
HET CL D 270 1
HET CL D 271 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 5 CL 7(CL 1-)
FORMUL 10 NA NA 1+
FORMUL 13 HOH *699(H2 O)
HELIX 1 1 SER A 27 GLY A 46 1 20
HELIX 2 2 VAL A 69 GLY A 86 1 18
HELIX 3 3 GLU A 95 HIS A 97 5 3
HELIX 4 4 GLN A 98 CYS A 106 1 9
HELIX 5 5 PRO A 112 ALA A 116 5 5
HELIX 6 6 GLN A 118 GLY A 129 1 12
HELIX 7 7 SER A 141 SER A 143 5 3
HELIX 8 8 GLN A 144 ALA A 155 1 12
HELIX 9 9 MET A 178 CYS A 188 1 11
HELIX 10 10 THR A 198 LEU A 201 5 4
HELIX 11 11 ARG A 203 ALA A 205 5 3
HELIX 12 12 GLN A 206 ALA A 216 1 11
HELIX 13 13 HIS A 244 SER A 262 1 19
HELIX 14 14 SER B 27 GLY B 46 1 20
HELIX 15 15 GLY B 70 GLY B 86 1 17
HELIX 16 16 GLU B 95 HIS B 97 5 3
HELIX 17 17 GLN B 98 CYS B 106 1 9
HELIX 18 18 PRO B 112 ALA B 116 5 5
HELIX 19 19 GLN B 118 THR B 128 1 11
HELIX 20 20 SER B 141 SER B 143 5 3
HELIX 21 21 GLN B 144 ALA B 155 1 12
HELIX 22 22 ASP B 177 CYS B 188 1 12
HELIX 23 23 ARG B 203 ALA B 205 5 3
HELIX 24 24 GLN B 206 ALA B 216 1 11
HELIX 25 25 PRO B 242 HIS B 244 5 3
HELIX 26 26 LEU B 245 GLN B 263 1 19
HELIX 27 27 LEU C 28 GLY C 46 1 19
HELIX 28 28 GLY C 70 GLY C 86 1 17
HELIX 29 29 GLU C 95 HIS C 97 5 3
HELIX 30 30 GLN C 98 CYS C 106 1 9
HELIX 31 31 PRO C 112 ALA C 116 5 5
HELIX 32 32 GLN C 118 GLY C 129 1 12
HELIX 33 33 SER C 141 SER C 143 5 3
HELIX 34 34 GLN C 144 ALA C 155 1 12
HELIX 35 35 MET C 178 CYS C 188 1 11
HELIX 36 36 ARG C 203 ALA C 205 5 3
HELIX 37 37 GLN C 206 ALA C 216 1 11
HELIX 38 38 LEU C 245 GLN C 263 1 19
HELIX 39 39 SER D 27 GLY D 46 1 20
HELIX 40 40 GLY D 70 GLY D 86 1 17
HELIX 41 41 GLU D 95 HIS D 97 5 3
HELIX 42 42 GLN D 98 CYS D 106 1 9
HELIX 43 43 PRO D 112 ALA D 116 5 5
HELIX 44 44 GLN D 118 THR D 128 1 11
HELIX 45 45 SER D 141 SER D 143 5 3
HELIX 46 46 GLN D 144 ALA D 155 1 12
HELIX 47 47 MET D 178 CYS D 188 1 11
HELIX 48 48 THR D 198 LEU D 201 5 4
HELIX 49 49 ARG D 203 ALA D 205 5 3
HELIX 50 50 GLN D 206 ALA D 216 1 11
HELIX 51 51 LEU D 245 SER D 262 1 18
SHEET 1 A 2 ILE A 3 ILE A 5 0
SHEET 2 A 2 ILE A 8 LEU A 10 -1 O LEU A 10 N ILE A 3
SHEET 1 B 9 VAL A 17 VAL A 24 0
SHEET 2 B 9 TYR A 49 SER A 54 1 O ILE A 50 N LEU A 18
SHEET 3 B 9 VAL A 89 ASP A 92 1 O ILE A 90 N PHE A 51
SHEET 4 B 9 VAL A 108 LEU A 111 1 O GLN A 110 N THR A 91
SHEET 5 B 9 VAL A 131 LYS A 135 1 O ASN A 133 N LEU A 111
SHEET 6 B 9 LEU A 160 GLU A 164 1 O ILE A 161 N ILE A 134
SHEET 7 B 9 VAL A 193 ASP A 196 1 O ASP A 196 N GLU A 164
SHEET 8 B 9 GLY A 221 PHE A 223 1 O PHE A 223 N PHE A 195
SHEET 9 B 9 VAL A 17 VAL A 24 1 N PHE A 19 O LEU A 222
SHEET 1 C 2 SER A 167 SER A 168 0
SHEET 2 C 2 LEU A 174 VAL A 175 -1 O VAL A 175 N SER A 167
SHEET 1 D 2 ILE B 3 ILE B 5 0
SHEET 2 D 2 ILE B 8 LEU B 10 -1 O LEU B 10 N ILE B 3
SHEET 1 E 9 VAL B 17 VAL B 24 0
SHEET 2 E 9 TYR B 49 SER B 54 1 O ILE B 50 N LEU B 18
SHEET 3 E 9 VAL B 89 ASP B 92 1 O ILE B 90 N PHE B 51
SHEET 4 E 9 VAL B 108 LEU B 111 1 O GLN B 110 N THR B 91
SHEET 5 E 9 VAL B 131 LYS B 135 1 O ASN B 133 N LEU B 111
SHEET 6 E 9 LEU B 160 GLU B 164 1 O ILE B 161 N ILE B 134
SHEET 7 E 9 VAL B 193 ASP B 196 1 O ILE B 194 N LEU B 162
SHEET 8 E 9 GLY B 221 PHE B 223 1 O PHE B 223 N PHE B 195
SHEET 9 E 9 VAL B 17 VAL B 24 1 N PHE B 19 O LEU B 222
SHEET 1 F 2 SER B 167 SER B 168 0
SHEET 2 F 2 LEU B 174 VAL B 175 -1 O VAL B 175 N SER B 167
SHEET 1 G 2 ILE C 3 ILE C 5 0
SHEET 2 G 2 ILE C 8 LEU C 10 -1 O LEU C 10 N ILE C 3
SHEET 1 H10 LEU C 241 PRO C 242 0
SHEET 2 H10 GLY C 221 HIS C 227 1 N GLU C 225 O LEU C 241
SHEET 3 H10 VAL C 193 ASP C 196 1 N PHE C 195 O PHE C 223
SHEET 4 H10 LEU C 160 GLU C 164 1 N GLU C 164 O ASP C 196
SHEET 5 H10 VAL C 131 LYS C 135 1 N ILE C 134 O ILE C 161
SHEET 6 H10 VAL C 108 LEU C 111 1 N LEU C 111 O ASN C 133
SHEET 7 H10 VAL C 89 ASP C 92 1 N THR C 91 O GLN C 110
SHEET 8 H10 TYR C 49 SER C 54 1 N PHE C 51 O ILE C 90
SHEET 9 H10 VAL C 17 VAL C 24 1 N LEU C 18 O ILE C 50
SHEET 10 H10 GLY C 221 HIS C 227 1 O LEU C 222 N PHE C 19
SHEET 1 I 2 SER C 167 SER C 168 0
SHEET 2 I 2 LEU C 174 VAL C 175 -1 O VAL C 175 N SER C 167
SHEET 1 J 2 ILE D 3 ILE D 5 0
SHEET 2 J 2 ILE D 8 LEU D 10 -1 O LEU D 10 N ILE D 3
SHEET 1 K10 LEU D 241 PRO D 242 0
SHEET 2 K10 GLY D 221 HIS D 227 1 N GLU D 225 O LEU D 241
SHEET 3 K10 VAL D 193 ASP D 196 1 N PHE D 195 O PHE D 223
SHEET 4 K10 LEU D 160 GLU D 164 1 N GLU D 164 O ASP D 196
SHEET 5 K10 VAL D 131 LYS D 135 1 N ILE D 134 O ILE D 161
SHEET 6 K10 VAL D 108 LEU D 111 1 N LEU D 111 O ASN D 133
SHEET 7 K10 VAL D 89 ASP D 92 1 N THR D 91 O GLN D 110
SHEET 8 K10 TYR D 49 SER D 54 1 N PHE D 51 O ILE D 90
SHEET 9 K10 VAL D 17 VAL D 24 1 N LEU D 18 O ILE D 50
SHEET 10 K10 GLY D 221 HIS D 227 1 O LEU D 222 N PHE D 19
SHEET 1 L 2 SER D 167 SER D 168 0
SHEET 2 L 2 LEU D 174 VAL D 175 -1 O VAL D 175 N SER D 167
LINK O ALA C 103 NA NA C 272 1555 1555 2.29
LINK O CYS C 106 NA NA C 272 1555 1555 2.51
LINK OD1BASN C 130 NA NA C 272 1555 1555 2.41
LINK OD1AASN C 130 NA NA C 272 1555 1555 2.49
LINK NA NA C 272 O HOH C 630 1555 1555 2.26
LINK NA NA C 272 O HOH C 631 1555 1555 2.12
SITE 1 AC1 2 PHE A 114 GLN A 138
SITE 1 AC2 3 PRO B 137 GLN B 138 ARG B 165
SITE 1 AC3 5 LYS B 52 GLN B 110 LYS B 135 PHE B 223
SITE 2 AC3 5 HOH B 674
SITE 1 AC4 3 ALA C 113 GLN C 138 ARG C 165
SITE 1 AC5 4 GLN C 110 LYS C 135 HIS C 199 PHE C 223
SITE 1 AC6 6 GLU B 104 ALA C 103 CYS C 106 ASN C 130
SITE 2 AC6 6 HOH C 630 HOH C 631
SITE 1 AC7 3 ALA D 113 GLN D 138 ARG D 165
SITE 1 AC8 5 LYS D 52 GLN D 110 LYS D 135 HIS D 199
SITE 2 AC8 5 PHE D 223
CRYST1 81.780 85.760 163.220 90.00 90.00 90.00 P 21 21 21 16
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 0.012228 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011660 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006127 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
