HEADER TRANSFERASE 08-JUN-09 3HQN
TITLE APO CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA(LMPYK)PYRUVATE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE;
COMPND 3 CHAIN: D, A;
COMPND 4 SYNONYM: PK;
COMPND 5 EC: 2.7.1.40;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MEXICANA;
SOURCE 3 ORGANISM_TAXID: 5665;
SOURCE 4 STRAIN: NHOM/B2/84/BEL46;
SOURCE 5 GENE: PYK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A_LMPYK
KEYWDS TIM BARREL, T-STATE ENZYME, TRANSFERASE, ALLOSTERIC ENZYME, ATP-
KEYWDS 2 BINDING, GLYCOLYSIS, KINASE, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-
KEYWDS 3 BINDING, PYRUVATE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.MORGAN,M.D.WALKINSHAW
REVDAT 5 01-NOV-23 3HQN 1 REMARK LINK
REVDAT 4 13-JUL-11 3HQN 1 VERSN
REVDAT 3 28-APR-10 3HQN 1 JRNL
REVDAT 2 23-FEB-10 3HQN 1 JRNL REMARK
REVDAT 1 16-FEB-10 3HQN 0
JRNL AUTH H.P.MORGAN,I.W.MCNAE,M.W.NOWICKI,V.HANNAERT,P.A.M.MICHELS,
JRNL AUTH 2 L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW
JRNL TITL THE ALLOSTERIC MECHANISM OF PRYUVATE KINASE FROM LEISHMANIA
JRNL TITL 2 MEXICANA: A ROCK AND LOCK MODEL
JRNL REF J.BIOL.CHEM. V. 285 12892 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20123988
JRNL DOI 10.1074/JBC.M109.079905
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 85394
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4504
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6257
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 325
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7512
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 734
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 30.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : -0.41000
REMARK 3 B33 (A**2) : 0.36000
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): 0.127
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.714
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6895 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9331 ; 2.052 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 891 ; 6.264 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;38.592 ;24.641
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1202 ;15.957 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;22.089 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1084 ; 0.181 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5150 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 4405 ; 1.313 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7116 ; 2.225 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2490 ; 4.036 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2211 ; 6.457 ; 4.500
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 : 7
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 86
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1794 38.3615 34.1589
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.0697
REMARK 3 T33: 0.0726 T12: -0.0517
REMARK 3 T13: -0.0196 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.4241 L22: 1.2101
REMARK 3 L33: 0.2854 L12: -0.1898
REMARK 3 L13: -0.1809 L23: 0.3368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: -0.0170 S13: 0.0971
REMARK 3 S21: 0.1003 S22: -0.0787 S23: 0.0439
REMARK 3 S31: -0.0398 S32: 0.0456 S33: 0.0219
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 : A 188 A 367
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9150 28.5922 42.7427
REMARK 3 T TENSOR
REMARK 3 T11: 0.1626 T22: 0.1002
REMARK 3 T33: 0.0331 T12: -0.0688
REMARK 3 T13: -0.0194 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.5198 L22: 1.4498
REMARK 3 L33: 0.0743 L12: -0.0883
REMARK 3 L13: 0.0208 L23: 0.1010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0596 S12: -0.0660 S13: 0.0654
REMARK 3 S21: 0.2805 S22: -0.0788 S23: -0.0404
REMARK 3 S31: -0.0048 S32: 0.0320 S33: 0.0193
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 : A 368 A 498
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2296 28.2179 31.9736
REMARK 3 T TENSOR
REMARK 3 T11: 0.0602 T22: 0.0604
REMARK 3 T33: 0.0949 T12: -0.0304
REMARK 3 T13: 0.0099 T23: -0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 1.5106 L22: 1.0043
REMARK 3 L33: 0.4662 L12: 0.8440
REMARK 3 L13: 0.0662 L23: 0.0203
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: 0.0209 S13: 0.2764
REMARK 3 S21: 0.0666 S22: -0.0647 S23: 0.2043
REMARK 3 S31: 0.0058 S32: -0.0348 S33: 0.0480
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 87
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8476 3.4505 31.0091
REMARK 3 T TENSOR
REMARK 3 T11: 0.0431 T22: 0.1263
REMARK 3 T33: 0.1741 T12: -0.0490
REMARK 3 T13: -0.0860 T23: 0.0864
REMARK 3 L TENSOR
REMARK 3 L11: 0.6079 L22: 1.5259
REMARK 3 L33: 0.4446 L12: -0.5821
REMARK 3 L13: -0.3211 L23: 0.3159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: -0.0850 S13: 0.0611
REMARK 3 S21: 0.1882 S22: -0.0455 S23: -0.4013
REMARK 3 S31: -0.0429 S32: 0.1340 S33: 0.0744
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 88 D 184
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6540 28.7380 2.4376
REMARK 3 T TENSOR
REMARK 3 T11: 0.5537 T22: 0.2085
REMARK 3 T33: 0.1608 T12: 0.0091
REMARK 3 T13: 0.1342 T23: 0.1429
REMARK 3 L TENSOR
REMARK 3 L11: 2.3466 L22: 8.4182
REMARK 3 L33: 3.6635 L12: 2.9174
REMARK 3 L13: -0.7761 L23: -2.8737
REMARK 3 S TENSOR
REMARK 3 S11: 0.1009 S12: 0.0097 S13: -0.1171
REMARK 3 S21: 0.8583 S22: -0.0754 S23: -0.3259
REMARK 3 S31: -0.7255 S32: 0.0803 S33: -0.0254
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 185 D 464
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7939 0.6830 25.1994
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0840
REMARK 3 T33: 0.0574 T12: -0.0195
REMARK 3 T13: -0.0158 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 0.3410 L22: 0.8994
REMARK 3 L33: 0.4464 L12: -0.1879
REMARK 3 L13: -0.0650 L23: -0.0420
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.0038 S13: -0.0290
REMARK 3 S21: -0.0093 S22: -0.0665 S23: -0.1714
REMARK 3 S31: -0.0136 S32: 0.0322 S33: 0.0487
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 465 D 498
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4910 -16.9321 39.0702
REMARK 3 T TENSOR
REMARK 3 T11: 0.0943 T22: 0.1911
REMARK 3 T33: 0.2882 T12: 0.0348
REMARK 3 T13: 0.0330 T23: 0.1935
REMARK 3 L TENSOR
REMARK 3 L11: 3.6215 L22: 3.5967
REMARK 3 L33: 2.5234 L12: 2.0842
REMARK 3 L13: 2.8293 L23: 1.2369
REMARK 3 S TENSOR
REMARK 3 S11: 0.1673 S12: -0.0470 S13: -0.5449
REMARK 3 S21: 0.2392 S22: 0.0043 S23: -0.4546
REMARK 3 S31: 0.1834 S32: 0.1637 S33: -0.1716
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DNA
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89910
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 52.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.58800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: PDB ENTRY 1PKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-16% PEG8000, 20MM TRIETHANOLAMINE
REMARK 280 -HCL, 50MM MGCL2, 100MM KCL, 10-15% GLYCEROL, PH7.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.28950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.66650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 66.09950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.28950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.66650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.09950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.28950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 83.66650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 66.09950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.28950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 83.66650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 66.09950
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: 12410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 788 LIES ON A SPECIAL POSITION.
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 D 0
REMARK 465 LYS D 484
REMARK 465 VAL D 485
REMARK 465 LYS D 486
REMARK 465 GLY D 487
REMARK 465 TYR D 488
REMARK 465 MET A 0
REMARK 465 ASP A 482
REMARK 465 HIS A 483
REMARK 465 LYS A 484
REMARK 465 VAL A 485
REMARK 465 LYS A 486
REMARK 465 GLY A 487
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 88 CD
REMARK 480 ILE A 89 C
REMARK 480 ARG A 90 C O CG CZ
REMARK 480 GLY A 92 C
REMARK 480 GLN A 93 N CB CD NE2
REMARK 480 PHE A 94 CG CE1 CE2
REMARK 480 VAL A 95 CB
REMARK 480 GLY A 96 N C
REMARK 480 GLY A 97 C
REMARK 480 ASP A 98 C CG
REMARK 480 ALA A 99 O
REMARK 480 VAL A 100 N C CB
REMARK 480 MET A 101 CB CE
REMARK 480 GLU A 102 CA CD OE2
REMARK 480 ARG A 103 C
REMARK 480 GLY A 104 C
REMARK 480 ALA A 105 N C O
REMARK 480 THR A 106 CG2
REMARK 480 CYS A 107 CA SG
REMARK 480 TYR A 108 CG
REMARK 480 VAL A 109 N CA O CG1 CG2
REMARK 480 THR A 110 CB
REMARK 480 THR A 111 N
REMARK 480 ASP A 112 CA O CG
REMARK 480 PRO A 113 CB CD
REMARK 480 ALA A 114 C
REMARK 480 PHE A 115 N C CB
REMARK 480 ALA A 116 CA
REMARK 480 ASP A 117 C CB CG OD2
REMARK 480 GLY A 119 N CA
REMARK 480 LYS A 121 N C CD
REMARK 480 ASP A 122 CA C CG
REMARK 480 LYS A 123 CA
REMARK 480 PHE A 124 N C CG
REMARK 480 TYR A 125 N CA C CD2
REMARK 480 ASP A 127 CA
REMARK 480 GLN A 129 NE2
REMARK 480 ASN A 130 CB OD1
REMARK 480 LEU A 131 CA CD1
REMARK 480 LYS A 133 O NZ
REMARK 480 VAL A 134 N CA O CG1
REMARK 480 VAL A 135 CA
REMARK 480 PRO A 137 N CG
REMARK 480 GLY A 138 C
REMARK 480 ASN A 139 N C
REMARK 480 TYR A 140 N O CG
REMARK 480 ILE A 141 CD1
REMARK 480 TYR A 142 O CB CD1 CE1
REMARK 480 ILE A 143 CA
REMARK 480 ASP A 144 OD1
REMARK 480 ASP A 145 CA CG
REMARK 480 GLY A 146 C O
REMARK 480 LEU A 148 N O CG
REMARK 480 ILE A 149 C
REMARK 480 LEU A 150 C
REMARK 480 GLN A 151 N C O
REMARK 480 VAL A 152 N C
REMARK 480 GLN A 153 N C O CD OE1
REMARK 480 GLU A 158 C
REMARK 480 LEU A 161 CD1
REMARK 480 GLU A 162 CD
REMARK 480 CYS A 163 C SG
REMARK 480 THR A 164 C
REMARK 480 VAL A 165 C
REMARK 480 THR A 166 C
REMARK 480 ASN A 167 C
REMARK 480 SER A 168 CB
REMARK 480 HIS A 169 CG CE1
REMARK 480 THR A 170 CA
REMARK 480 ILE A 171 N C CB
REMARK 480 SER A 172 N CB
REMARK 480 ASP A 173 C
REMARK 480 ARG A 174 C CG
REMARK 480 ARG A 175 CA CZ
REMARK 480 GLY A 176 C
REMARK 480 ASN A 178 CA O CG
REMARK 480 LEU A 179 CB
REMARK 480 GLY A 181 N
REMARK 480 ASP A 183 CG OD2
REMARK 480 PRO A 187 C
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 ALA A 116 O HOH A 693 1.78
REMARK 500 CB SER A 383 O HOH A 811 1.90
REMARK 500 O HOH D 778 O HOH D 862 2.13
REMARK 500 O HOH D 545 O HOH D 822 2.18
REMARK 500 O HOH D 635 O HOH A 535 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS D 446 OE1 GLN A 69 7545 1.83
REMARK 500 CE LYS D 446 O HOH A 825 7545 2.03
REMARK 500 NZ LYS D 446 O HOH A 825 7545 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER D 1 N SER D 1 CA 0.175
REMARK 500 TYR D 18 CE1 TYR D 18 CZ 0.081
REMARK 500 GLU D 378 CB GLU D 378 CG -0.127
REMARK 500 SER A 1 N SER A 1 CA 0.154
REMARK 500 GLY A 86 C PRO A 87 N 0.147
REMARK 500 SER A 383 CB SER A 383 OG -0.078
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 ASP D 185 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG D 223 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU D 281 CB - CG - CD2 ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG D 348 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG D 413 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 VAL A 34 CG1 - CB - CG2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 HIS A 169 CB - CA - C ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 348 NE - CZ - NH2 ANGL. DEV. = 3.5 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 LYS D 118 38.93 -152.30
REMARK 500 ASP D 144 73.09 58.99
REMARK 500 HIS D 169 132.09 -178.64
REMARK 500 LEU D 186 151.99 -47.52
REMARK 500 THR D 296 140.82 74.96
REMARK 500 SER D 330 -105.94 -112.20
REMARK 500 ASN D 415 38.42 -96.17
REMARK 500 LYS D 453 -5.04 77.13
REMARK 500 GLN D 491 136.47 179.18
REMARK 500 ALA A 99 109.62 -162.11
REMARK 500 LYS A 118 53.96 -148.13
REMARK 500 ASP A 144 70.92 57.58
REMARK 500 HIS A 169 156.24 176.99
REMARK 500 THR A 296 147.03 70.15
REMARK 500 SER A 330 -102.20 -112.48
REMARK 500 ASN A 415 37.26 -99.79
REMARK 500 LYS A 453 -7.58 77.72
REMARK 500 GLN A 491 139.32 171.96
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 K D 503 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 51 OD1
REMARK 620 2 SER D 53 OG 67.4
REMARK 620 3 ASP D 83 OD1 111.3 174.7
REMARK 620 4 THR D 84 O 132.1 99.1 77.9
REMARK 620 5 GOL D 499 O3 136.0 70.4 111.9 66.5
REMARK 620 6 HOH D 873 O 92.3 97.0 88.1 135.5 80.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 354 O
REMARK 620 2 LEU D 357 O 84.2
REMARK 620 3 GLU D 359 OE1 84.9 86.6
REMARK 620 4 GLU D 359 OE2 122.1 71.4 43.4
REMARK 620 5 HOH D 872 O 109.5 87.0 163.5 120.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 51 OD1
REMARK 620 2 SER A 53 OG 75.5
REMARK 620 3 ASP A 83 OD1 109.7 168.0
REMARK 620 4 THR A 84 O 132.4 99.1 69.3
REMARK 620 5 HOH A 678 O 145.5 73.7 103.5 68.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 354 O
REMARK 620 2 LEU A 357 O 88.2
REMARK 620 3 GLU A 359 OE1 86.4 83.8
REMARK 620 4 GLU A 359 OE2 129.1 71.1 46.7
REMARK 620 5 HOH A 681 O 155.8 81.8 114.1 67.9
REMARK 620 6 HOH A 797 O 107.1 87.2 163.6 117.2 50.7
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 GOL D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E0V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE KINASE FROM LEISHMANIA MEXICANA:
REMARK 900 SULFATE IONS REMOVED BY BACK-SOAKING
REMARK 900 RELATED ID: 3E0W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE KINASE FROM LEISHMANIA MEXICANA IN
REMARK 900 COMPLEX WITH SULFATE IONS
REMARK 900 RELATED ID: 1PKL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE KINASE FROM LEISHMANIA MEXICANA,
REMARK 900 CRYSTALLIZED UNDER ACIDIC CONDITIONS
REMARK 900 RELATED ID: 3HQO RELATED DB: PDB
REMARK 900 RELATED ID: 3HQP RELATED DB: PDB
REMARK 900 RELATED ID: 3HQQ RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF L. MEXICANA PYRUVATE KINASE HAS BEEN DETERMINED IN
REMARK 999 THE LABORATORY OF PROF. PAUL MICHELS, PUBLISHED AND DEPOSITED IN
REMARK 999 GENBANK. HOWEVER, THE SEQUENCE AS APPEARED IN GENBANK CONTAINED
REMARK 999 ERRORS. THE CORRECTION HAS BEEN INFORMED TO GENBANK WITH THE
REMARK 999 ACCESSION CODE X74944 AND IT WILL BE FILTRATED TO UNIPROT AT A
REMARK 999 LATER TIME.
DBREF 3HQN D 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3HQN A 0 498 UNP Q27686 KPYK_LEIME 1 499
SEQADV 3HQN SER D 382 UNP Q27686 GLY 383 SEE REMARK 999
SEQADV 3HQN TYR D 389 UNP Q27686 SER 390 SEE REMARK 999
SEQADV 3HQN ARG D 404 UNP Q27686 ALA 405 SEE REMARK 999
SEQADV 3HQN SER D 405 UNP Q27686 GLY 406 SEE REMARK 999
SEQADV 3HQN SER A 382 UNP Q27686 GLY 383 SEE REMARK 999
SEQADV 3HQN TYR A 389 UNP Q27686 SER 390 SEE REMARK 999
SEQADV 3HQN ARG A 404 UNP Q27686 ALA 405 SEE REMARK 999
SEQADV 3HQN SER A 405 UNP Q27686 GLY 406 SEE REMARK 999
SEQRES 1 D 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 D 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 D 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 D 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 D 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 D 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 D 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 D 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 D 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 D 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 D 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 D 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 D 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 D 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 D 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 D 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 D 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 D 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 D 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 D 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 D 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 D 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 D 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 D 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 D 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 D 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 D 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 D 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 D 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 D 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 D 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 D 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 D 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 D 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 D 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 D 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 D 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 D 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 D 499 ILE LEU LEU VAL GLU
SEQRES 1 A 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 A 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 A 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 A 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 A 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 A 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 A 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 A 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 A 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 A 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 A 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 A 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 A 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 A 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 A 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 A 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 A 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 A 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 A 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 A 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 A 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 A 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 A 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 A 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 A 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 A 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 A 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 A 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 A 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 A 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 A 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 A 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 A 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 A 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 A 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 A 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 A 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 A 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 A 499 ILE LEU LEU VAL GLU
HET GOL D 499 6
HET GOL D 500 6
HET SO4 D 501 5
HET K D 502 1
HET K D 503 1
HET GOL A 499 6
HET SO4 A 500 5
HET K A 501 1
HET K A 502 1
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM K POTASSIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 K 4(K 1+)
FORMUL 12 HOH *734(H2 O)
HELIX 1 1 SER D 1 THR D 8 1 8
HELIX 2 2 SER D 33 GLY D 44 1 12
HELIX 3 3 SER D 56 GLY D 75 1 20
HELIX 4 4 PHE D 94 GLY D 96 5 3
HELIX 5 5 ASP D 112 ALA D 116 5 5
HELIX 6 6 ASN D 130 VAL D 135 1 6
HELIX 7 7 SER D 190 GLN D 203 1 14
HELIX 8 8 SER D 215 GLY D 227 1 13
HELIX 9 9 PRO D 228 ARG D 231 5 4
HELIX 10 10 ASN D 241 ASN D 247 1 7
HELIX 11 11 ASN D 247 SER D 255 1 9
HELIX 12 12 ARG D 262 ILE D 269 1 8
HELIX 13 13 PRO D 270 GLY D 289 1 20
HELIX 14 14 LEU D 299 TYR D 304 5 6
HELIX 15 15 THR D 309 GLY D 323 1 15
HELIX 16 16 SER D 330 LYS D 335 1 6
HELIX 17 17 TYR D 338 LEU D 357 1 20
HELIX 18 18 ASN D 358 LEU D 369 1 12
HELIX 19 19 SER D 375 LYS D 392 1 18
HELIX 20 20 GLY D 403 TYR D 412 1 10
HELIX 21 21 ARG D 424 LEU D 431 1 8
HELIX 22 22 ASN D 432 THR D 434 5 3
HELIX 23 23 ASP D 443 GLY D 448 1 6
HELIX 24 24 LYS D 453 LYS D 467 1 15
HELIX 25 25 SER A 1 THR A 8 1 8
HELIX 26 26 SER A 33 GLY A 44 1 12
HELIX 27 27 SER A 56 GLY A 75 1 20
HELIX 28 28 PHE A 94 ASP A 98 5 5
HELIX 29 29 ASP A 112 ALA A 116 5 5
HELIX 30 30 ASN A 130 VAL A 135 1 6
HELIX 31 31 SER A 190 GLY A 204 1 15
HELIX 32 32 ALA A 216 GLY A 227 1 12
HELIX 33 33 PRO A 228 ARG A 231 5 4
HELIX 34 34 ASN A 241 ASN A 247 1 7
HELIX 35 35 ASN A 247 SER A 255 1 9
HELIX 36 36 ARG A 262 ILE A 269 1 8
HELIX 37 37 PRO A 270 GLY A 289 1 20
HELIX 38 38 LEU A 299 TYR A 304 5 6
HELIX 39 39 THR A 309 GLY A 323 1 15
HELIX 40 40 SER A 330 LYS A 335 1 6
HELIX 41 41 TYR A 338 LEU A 357 1 20
HELIX 42 42 ASN A 358 LEU A 369 1 12
HELIX 43 43 SER A 375 LYS A 392 1 18
HELIX 44 44 GLY A 403 TYR A 412 1 10
HELIX 45 45 ARG A 424 LEU A 431 1 8
HELIX 46 46 ASN A 432 THR A 434 5 3
HELIX 47 47 ASP A 443 GLY A 448 1 6
HELIX 48 48 LYS A 453 LYS A 467 1 15
SHEET 1 A 9 ARG D 22 ILE D 27 0
SHEET 2 A 9 MET D 45 ASN D 51 1 O VAL D 47 N CYS D 25
SHEET 3 A 9 ALA D 79 ASP D 83 1 O ALA D 79 N ALA D 48
SHEET 4 A 9 MET D 207 ALA D 210 1 O PHE D 209 N LEU D 82
SHEET 5 A 9 MET D 234 ILE D 239 1 O ILE D 236 N ILE D 208
SHEET 6 A 9 GLY D 257 ALA D 261 1 O MET D 259 N CYS D 237
SHEET 7 A 9 VAL D 292 ALA D 295 1 O ILE D 293 N VAL D 260
SHEET 8 A 9 CYS D 326 LEU D 329 1 O CYS D 326 N CYS D 294
SHEET 9 A 9 ARG D 22 ILE D 27 1 N ILE D 24 O VAL D 327
SHEET 1 B 2 ASP D 98 MET D 101 0
SHEET 2 B 2 HIS D 169 SER D 172 -1 O HIS D 169 N MET D 101
SHEET 1 C 6 LYS D 123 TYR D 125 0
SHEET 2 C 6 THR D 106 THR D 110 1 N THR D 110 O PHE D 124
SHEET 3 C 6 THR D 160 VAL D 165 -1 O CYS D 163 N CYS D 107
SHEET 4 C 6 LEU D 148 ASP D 157 -1 N GLN D 151 O THR D 164
SHEET 5 C 6 TYR D 140 ILE D 143 -1 N ILE D 141 O LEU D 150
SHEET 6 C 6 VAL D 177 ASN D 178 -1 O ASN D 178 N TYR D 142
SHEET 1 D 5 VAL D 437 PHE D 441 0
SHEET 2 D 5 ILE D 418 THR D 422 1 N CYS D 420 O GLU D 438
SHEET 3 D 5 ALA D 395 LEU D 399 1 N VAL D 398 O VAL D 419
SHEET 4 D 5 TYR D 475 ALA D 481 1 O ILE D 479 N VAL D 397
SHEET 5 D 5 ASN D 490 LEU D 496 -1 O LEU D 495 N CYS D 476
SHEET 1 E 9 ARG A 22 THR A 26 0
SHEET 2 E 9 MET A 45 ASN A 51 1 O ARG A 49 N CYS A 25
SHEET 3 E 9 ALA A 79 ASP A 83 1 O ALA A 81 N MET A 50
SHEET 4 E 9 MET A 207 ALA A 210 1 O PHE A 209 N LEU A 82
SHEET 5 E 9 MET A 234 ILE A 239 1 O ILE A 236 N ILE A 208
SHEET 6 E 9 GLY A 257 ALA A 261 1 O MET A 259 N CYS A 237
SHEET 7 E 9 VAL A 292 ALA A 295 1 O ILE A 293 N VAL A 260
SHEET 8 E 9 CYS A 326 LEU A 329 1 O CYS A 326 N CYS A 294
SHEET 9 E 9 ARG A 22 THR A 26 1 N ILE A 24 O LEU A 329
SHEET 1 F 2 VAL A 100 MET A 101 0
SHEET 2 F 2 HIS A 169 THR A 170 -1 O HIS A 169 N MET A 101
SHEET 1 G 6 LYS A 123 TYR A 125 0
SHEET 2 G 6 THR A 106 THR A 110 1 N THR A 110 O PHE A 124
SHEET 3 G 6 THR A 160 VAL A 165 -1 O CYS A 163 N CYS A 107
SHEET 4 G 6 LEU A 148 ASP A 157 -1 N SER A 154 O GLU A 162
SHEET 5 G 6 TYR A 140 ILE A 143 -1 N ILE A 141 O LEU A 150
SHEET 6 G 6 VAL A 177 ASN A 178 -1 O ASN A 178 N TYR A 142
SHEET 1 H 5 VAL A 437 PHE A 441 0
SHEET 2 H 5 ILE A 418 THR A 422 1 N CYS A 420 O VAL A 440
SHEET 3 H 5 ALA A 395 LEU A 399 1 N MET A 396 O VAL A 419
SHEET 4 H 5 TYR A 475 HIS A 480 1 O VAL A 477 N VAL A 397
SHEET 5 H 5 GLN A 491 LEU A 496 -1 O ARG A 493 N VAL A 478
LINK OD1 ASN D 51 K K D 503 1555 1555 2.80
LINK OG SER D 53 K K D 503 1555 1555 2.87
LINK OD1 ASP D 83 K K D 503 1555 1555 2.77
LINK O THR D 84 K K D 503 1555 1555 2.82
LINK O GLN D 354 K K D 502 1555 1555 2.68
LINK O LEU D 357 K K D 502 1555 1555 2.68
LINK OE1 GLU D 359 K K D 502 1555 1555 2.93
LINK OE2 GLU D 359 K K D 502 1555 1555 3.08
LINK O3 GOL D 499 K K D 503 1555 1555 3.00
LINK K K D 502 O HOH D 872 1555 1555 2.73
LINK K K D 503 O HOH D 873 1555 1555 3.07
LINK OD1 ASN A 51 K K A 502 1555 1555 2.72
LINK OG SER A 53 K K A 502 1555 1555 2.89
LINK OD1 ASP A 83 K K A 502 1555 1555 2.82
LINK O THR A 84 K K A 502 1555 1555 2.88
LINK O GLN A 354 K K A 501 1555 1555 2.66
LINK O LEU A 357 K K A 501 1555 1555 2.80
LINK OE1AGLU A 359 K K A 501 1555 1555 2.70
LINK OE2AGLU A 359 K K A 501 1555 1555 2.95
LINK K K A 501 O HOH A 681 1555 1555 2.84
LINK K K A 501 O HOH A 797 1555 1555 2.94
LINK K K A 502 O HOH A 678 1555 1555 2.78
CISPEP 1 ILE D 372 PRO D 373 0 4.39
CISPEP 2 ILE A 372 PRO A 373 0 3.03
SITE 1 AC1 9 SER D 53 THR D 84 LYS D 85 SER D 211
SITE 2 AC1 9 LYS D 238 GLU D 240 K D 503 HOH D 782
SITE 3 AC1 9 HOH D 873
SITE 1 AC2 5 ASP D 232 ARG D 424 GLN D 426 THR D 427
SITE 2 AC2 5 GLN D 430
SITE 1 AC3 11 SER D 400 ASN D 401 THR D 402 ARG D 404
SITE 2 AC3 11 SER D 405 ASP D 482 HIS D 483 HOH D 619
SITE 3 AC3 11 HOH D 724 HOH D 801 HOH D 883
SITE 1 AC4 4 GLN D 354 LEU D 357 GLU D 359 HOH D 872
SITE 1 AC5 7 ASN D 51 SER D 53 ASP D 83 THR D 84
SITE 2 AC5 7 LYS D 238 GOL D 499 HOH D 873
SITE 1 AC6 8 GLU A 438 SER A 439 PHE A 463 HOH A 667
SITE 2 AC6 8 HOH A 724 HOH A 732 HOH A 734 HOH A 746
SITE 1 AC7 7 SER A 400 ASN A 401 THR A 402 ARG A 404
SITE 2 AC7 7 SER A 405 HOH A 815 HOH A 830
SITE 1 AC8 5 GLN A 354 LEU A 357 GLU A 359 HOH A 681
SITE 2 AC8 5 HOH A 797
SITE 1 AC9 5 ASN A 51 SER A 53 ASP A 83 THR A 84
SITE 2 AC9 5 HOH A 678
CRYST1 120.579 167.333 132.199 90.00 90.00 90.00 I 2 2 2 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 0.008293 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007564 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
