HEADER TRANSFERASE 29-OCT-09 3KGF
TITLE THE STRUCTURE OF 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE
TITLE 2 FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH PHENYLALANINE AND
TITLE 3 TRYPTOPHAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE
COMPND 3 SYNTHASE AROG;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: DAHP SYNTHETASE, PHENYLALANINE-REPRESSIBLE;
COMPND 6 EC: 2.5.1.54;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV2178C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEXHTA
KEYWDS MYCOBACTERIUM TUBERCULOSIS, DAH7P SYNTHASE, SHIKIMATE PATHWAY,
KEYWDS 2 AROMATIC BIOSYNTHESIS, EVOLUTIONARY RELATIONSHIPS, TRANSFERASE,
KEYWDS 3 PHE+TRP-BOUND, AUGMENTED TIM-BARREL STRUCTURE, STRUCTURAL GENOMICS,
KEYWDS 4 MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT, XMTB
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.PARKER,G.B.JAMESON,W.JIAO,C.J.WEBBY,E.N.BAKER,H.M.BAKER,
AUTHOR 2 MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT (XMTB)
REVDAT 3 01-NOV-23 3KGF 1 REMARK SEQADV LINK
REVDAT 2 22-FEB-12 3KGF 1 JRNL VERSN
REVDAT 1 28-JUL-10 3KGF 0
JRNL AUTH C.J.WEBBY,W.JIAO,R.D.HUTTON,N.J.BLACKMORE,H.M.BAKER,
JRNL AUTH 2 E.N.BAKER,G.B.JAMESON,E.J.PARKER
JRNL TITL SYNERGISTIC ALLOSTERY, A SOPHISTICATED REGULATORY NETWORK
JRNL TITL 2 FOR THE CONTROL OF AROMATIC AMINO ACID BIOSYNTHESIS IN
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS
JRNL REF J.BIOL.CHEM. V. 285 30567 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20667835
JRNL DOI 10.1074/JBC.M110.111856
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.WEBBY,H.M.BAKER,J.S.LOTT,E.N.BAKER,E.J.PARKER
REMARK 1 TITL THE STRUCTURE OF 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE
REMARK 1 TITL 2 SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS REVEALS A COMMON
REMARK 1 TITL 3 CATALYTIC SCAFFOLD AND ANCESTRY FOR TYPE I AND TYPE II
REMARK 1 TITL 4 ENZYMES
REMARK 1 REF J.MOL.BIOL. V. 354 927 2005
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 16288916
REMARK 1 DOI 10.1016/J.JMB.2005.09.093
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.R.SCHOFIELD,B.F.ANDERSON,M.L.PATCHETT,G.E.NORRIS,
REMARK 1 AUTH 2 G.B.JAMESON,E.J.PARKER
REMARK 1 TITL SUBSTRATE AMBIGUITY AND CRYSTAL STRUCTURE OF PYROCOCCUS
REMARK 1 TITL 2 FURIOSUS 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE
REMARK 1 TITL 3 SYNTHASE: AN ANCESTRAL 3-DEOXYALD-2-ULOSONATE-PHOSPHATE
REMARK 1 TITL 4 SYNTHASE?
REMARK 1 REF BIOCHEMISTRY V. 44 11950 2005
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 16142893
REMARK 1 DOI 10.1021/BI050577Z
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 32.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 105110
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5245
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) : 6339
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 336
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6976
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 191
REMARK 3 SOLVENT ATOMS : 771
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.23000
REMARK 3 B12 (A**2) : -0.08000
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): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.535
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7699 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5214 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10484 ; 1.318 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12647 ; 0.976 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 977 ; 6.187 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 368 ;34.003 ;23.261
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1225 ;12.893 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 79 ;15.749 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1155 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8748 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1568 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1536 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5733 ; 0.203 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3665 ; 0.164 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3753 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 620 ; 0.163 ; 0.200
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): 11 ; 0.101 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 71 ; 0.269 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.163 ; 0.200
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): 4950 ; 0.696 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1917 ; 0.161 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7751 ; 1.090 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3072 ; 2.796 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2731 ; 4.212 ; 7.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 462 5
REMARK 3 1 B 1 B 462 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2573 ; 0.790 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 3018 ; 0.900 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2573 ; 0.620 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 3018 ; 1.370 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 2 A 462
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2740 115.7270 14.9750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0185 T22: 0.0021
REMARK 3 T33: -0.1340 T12: 0.0236
REMARK 3 T13: -0.0041 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 0.7881 L22: 0.7647
REMARK 3 L33: 0.6505 L12: -0.2637
REMARK 3 L13: -0.3004 L23: 0.2349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: -0.1247 S13: 0.1457
REMARK 3 S21: 0.0944 S22: 0.0291 S23: -0.1371
REMARK 3 S31: -0.0795 S32: 0.0881 S33: -0.0782
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 462
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7980 89.9440 -6.4380
REMARK 3 T TENSOR
REMARK 3 T11: -0.0568 T22: -0.0033
REMARK 3 T33: -0.1566 T12: 0.0271
REMARK 3 T13: -0.0154 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.8803 L22: 0.8191
REMARK 3 L33: 0.5050 L12: -0.3974
REMARK 3 L13: 0.1687 L23: -0.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0480 S12: -0.0098 S13: -0.1695
REMARK 3 S21: -0.0264 S22: -0.0096 S23: 0.1540
REMARK 3 S31: 0.0192 S32: -0.0853 S33: -0.0385
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 ADDED IN THE RIDING POSITIONS.
REMARK 3 MN IS CHAIN A IS PRESENT IN 75% OCCUPANCY,
REMARK 3 WHILE IN CHAIN B ITS OCCUPANCY IS 50%.
REMARK 3 THE WATER THAT IS OBSERVED COORDINATED TO THE MN ION IN CHAIN A IS
REMARK 3 DISPLACED
REMARK 3 TO MORE THAN 4 ANGSTROMS AWAY FROM THE MN IN CHAIN B.
REMARK 3 ATOM OE1 OF GLU411 IS WEAKLY COORDINATED AT DISTANCES GREATER THAN
REMARK 3 2.6 ANGSTROMS FOR BOTH MN SITES.
REMARK 3 BECAUSE THE OCCUPANCY OF MN IN CHAIN B IS ONLY TWO-THIRDS THAT OF
REMARK 3 THE MN IN CHAIN A,
REMARK 3 MN-LIGAND DISTANCES IN CHAIN B ARE ~0.2 A LONGER THAN THE
REMARK 3 CORRESPONDING DISTANCES IN CHAIN A.
REMARK 4
REMARK 4 3KGF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000055960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : OSMIC BLUE MIRRORS
REMARK 200 OPTICS : OSMIC BLUE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105425
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 2.070
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.38
REMARK 200 R MERGE FOR SHELL (I) : 0.38100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 2B7O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM BTP, 150MM NACL, 0.5MM TCEP,
REMARK 280 0.005%(V/V) THESIT, 0.2MM PEP, 0.1MM MNCL2, 0.1M NA HEPES, 0.8M
REMARK 280 NAK PHOSPHATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.30800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.15400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.15400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.30800
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: 12290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 GLN A 11
REMARK 465 LEU A 12
REMARK 465 PRO A 13
REMARK 465 SER A 14
REMARK 465 LEU A 15
REMARK 465 ASP A 265
REMARK 465 ASP A 266
REMARK 465 GLY A 267
REMARK 465 GLU A 268
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 ASP B 10
REMARK 465 GLN B 11
REMARK 465 LEU B 12
REMARK 465 PRO B 13
REMARK 465 SER B 14
REMARK 465 SER B 376
REMARK 465 THR B 377
REMARK 465 GLY B 378
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 TRP A 3 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 3 CZ3 CH2
REMARK 470 LEU B 15 CG CD1 CD2
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 ASP A 138 O HOH A 629 2.01
REMARK 500 ND1 HIS B 198 O HOH B 586 2.11
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 VAL A 233 -159.15 -103.18
REMARK 500 ALA A 234 54.53 81.17
REMARK 500 ASP A 235 -135.58 -119.65
REMARK 500 LEU A 250 -50.47 -122.30
REMARK 500 CYS A 440 -118.19 -146.60
REMARK 500 CYS A 440 -114.57 -150.33
REMARK 500 ASP B 263 119.86 141.61
REMARK 500 ASP B 265 -68.03 -94.11
REMARK 500 ASP B 265 -79.93 -50.07
REMARK 500 CYS B 440 -111.88 -146.95
REMARK 500 CYS B 440 -105.68 -146.70
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 MN A 465 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 87 SG
REMARK 620 2 HIS A 369 NE2 173.4
REMARK 620 3 GLU A 411 OE2 96.3 87.6
REMARK 620 4 GLU A 411 OE1 100.3 86.3 55.4
REMARK 620 5 ASP A 441 OD2 95.8 83.2 150.6 96.1
REMARK 620 6 HOH A 586 O 95.3 79.0 94.4 147.1 111.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 466 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 87 SG
REMARK 620 2 HIS B 369 NE2 174.6
REMARK 620 3 GLU B 411 OE2 98.9 83.0
REMARK 620 4 GLU B 411 OE1 93.2 84.2 50.0
REMARK 620 5 ASP B 441 OD2 89.3 86.6 150.5 101.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE A 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2647
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 463
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 465
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE B 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP B 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 463
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 465
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2647
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE B 4188
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 472
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B7O RELATED DB: PDB
REMARK 900 THE SELENOMETHIONINE LIGAND- AND INHIBITOR-FREE MN2+-BOUND
REMARK 900 FORM(PSEUDO-WILD-TYPE)
REMARK 900 RELATED ID: RV2178C RELATED DB: TARGETDB
DBREF 3KGF A 1 462 UNP O53512 O53512_MYCTU 1 462
DBREF 3KGF B 1 462 UNP O53512 O53512_MYCTU 1 462
SEQADV 3KGF GLY A -1 UNP O53512 EXPRESSION TAG
SEQADV 3KGF ALA A 0 UNP O53512 EXPRESSION TAG
SEQADV 3KGF GLY B -1 UNP O53512 EXPRESSION TAG
SEQADV 3KGF ALA B 0 UNP O53512 EXPRESSION TAG
SEQRES 1 A 464 GLY ALA MET ASN TRP THR VAL ASP ILE PRO ILE ASP GLN
SEQRES 2 A 464 LEU PRO SER LEU PRO PRO LEU PRO THR ASP LEU ARG THR
SEQRES 3 A 464 ARG LEU ASP ALA ALA LEU ALA LYS PRO ALA ALA GLN GLN
SEQRES 4 A 464 PRO THR TRP PRO ALA ASP GLN ALA LEU ALA MET ARG THR
SEQRES 5 A 464 VAL LEU GLU SER VAL PRO PRO VAL THR VAL PRO SER GLU
SEQRES 6 A 464 ILE VAL ARG LEU GLN GLU GLN LEU ALA GLN VAL ALA LYS
SEQRES 7 A 464 GLY GLU ALA PHE LEU LEU GLN GLY GLY ASP CYS ALA GLU
SEQRES 8 A 464 THR PHE MET ASP ASN THR GLU PRO HIS ILE ARG GLY ASN
SEQRES 9 A 464 VAL ARG ALA LEU LEU GLN MET ALA VAL VAL LEU THR TYR
SEQRES 10 A 464 GLY ALA SER MET PRO VAL VAL LYS VAL ALA ARG ILE ALA
SEQRES 11 A 464 GLY GLN TYR ALA LYS PRO ARG SER ALA ASP ILE ASP ALA
SEQRES 12 A 464 LEU GLY LEU ARG SER TYR ARG GLY ASP MET ILE ASN GLY
SEQRES 13 A 464 PHE ALA PRO ASP ALA ALA ALA ARG GLU HIS ASP PRO SER
SEQRES 14 A 464 ARG LEU VAL ARG ALA TYR ALA ASN ALA SER ALA ALA MET
SEQRES 15 A 464 ASN LEU VAL ARG ALA LEU THR SER SER GLY LEU ALA SER
SEQRES 16 A 464 LEU HIS LEU VAL HIS ASP TRP ASN ARG GLU PHE VAL ARG
SEQRES 17 A 464 THR SER PRO ALA GLY ALA ARG TYR GLU ALA LEU ALA THR
SEQRES 18 A 464 GLU ILE ASP ARG GLY LEU ARG PHE MET SER ALA CYS GLY
SEQRES 19 A 464 VAL ALA ASP ARG ASN LEU GLN THR ALA GLU ILE TYR ALA
SEQRES 20 A 464 SER HIS GLU ALA LEU VAL LEU ASP TYR GLU ARG ALA MET
SEQRES 21 A 464 LEU ARG LEU SER ASP GLY ASP ASP GLY GLU PRO GLN LEU
SEQRES 22 A 464 PHE ASP LEU SER ALA HIS THR VAL TRP ILE GLY GLU ARG
SEQRES 23 A 464 THR ARG GLN ILE ASP GLY ALA HIS ILE ALA PHE ALA GLN
SEQRES 24 A 464 VAL ILE ALA ASN PRO VAL GLY VAL LYS LEU GLY PRO ASN
SEQRES 25 A 464 MET THR PRO GLU LEU ALA VAL GLU TYR VAL GLU ARG LEU
SEQRES 26 A 464 ASP PRO HIS ASN LYS PRO GLY ARG LEU THR LEU VAL SER
SEQRES 27 A 464 ARG MET GLY ASN HIS LYS VAL ARG ASP LEU LEU PRO PRO
SEQRES 28 A 464 ILE VAL GLU LYS VAL GLN ALA THR GLY HIS GLN VAL ILE
SEQRES 29 A 464 TRP GLN CYS ASP PRO MET HIS GLY ASN THR HIS GLU SER
SEQRES 30 A 464 SER THR GLY PHE LYS THR ARG HIS PHE ASP ARG ILE VAL
SEQRES 31 A 464 ASP GLU VAL GLN GLY PHE PHE GLU VAL HIS ARG ALA LEU
SEQRES 32 A 464 GLY THR HIS PRO GLY GLY ILE HIS VAL GLU ILE THR GLY
SEQRES 33 A 464 GLU ASN VAL THR GLU CYS LEU GLY GLY ALA GLN ASP ILE
SEQRES 34 A 464 SER GLU THR ASP LEU ALA GLY ARG TYR GLU THR ALA CYS
SEQRES 35 A 464 ASP PRO ARG LEU ASN THR GLN GLN SER LEU GLU LEU ALA
SEQRES 36 A 464 PHE LEU VAL ALA GLU MET LEU ARG ASP
SEQRES 1 B 464 GLY ALA MET ASN TRP THR VAL ASP ILE PRO ILE ASP GLN
SEQRES 2 B 464 LEU PRO SER LEU PRO PRO LEU PRO THR ASP LEU ARG THR
SEQRES 3 B 464 ARG LEU ASP ALA ALA LEU ALA LYS PRO ALA ALA GLN GLN
SEQRES 4 B 464 PRO THR TRP PRO ALA ASP GLN ALA LEU ALA MET ARG THR
SEQRES 5 B 464 VAL LEU GLU SER VAL PRO PRO VAL THR VAL PRO SER GLU
SEQRES 6 B 464 ILE VAL ARG LEU GLN GLU GLN LEU ALA GLN VAL ALA LYS
SEQRES 7 B 464 GLY GLU ALA PHE LEU LEU GLN GLY GLY ASP CYS ALA GLU
SEQRES 8 B 464 THR PHE MET ASP ASN THR GLU PRO HIS ILE ARG GLY ASN
SEQRES 9 B 464 VAL ARG ALA LEU LEU GLN MET ALA VAL VAL LEU THR TYR
SEQRES 10 B 464 GLY ALA SER MET PRO VAL VAL LYS VAL ALA ARG ILE ALA
SEQRES 11 B 464 GLY GLN TYR ALA LYS PRO ARG SER ALA ASP ILE ASP ALA
SEQRES 12 B 464 LEU GLY LEU ARG SER TYR ARG GLY ASP MET ILE ASN GLY
SEQRES 13 B 464 PHE ALA PRO ASP ALA ALA ALA ARG GLU HIS ASP PRO SER
SEQRES 14 B 464 ARG LEU VAL ARG ALA TYR ALA ASN ALA SER ALA ALA MET
SEQRES 15 B 464 ASN LEU VAL ARG ALA LEU THR SER SER GLY LEU ALA SER
SEQRES 16 B 464 LEU HIS LEU VAL HIS ASP TRP ASN ARG GLU PHE VAL ARG
SEQRES 17 B 464 THR SER PRO ALA GLY ALA ARG TYR GLU ALA LEU ALA THR
SEQRES 18 B 464 GLU ILE ASP ARG GLY LEU ARG PHE MET SER ALA CYS GLY
SEQRES 19 B 464 VAL ALA ASP ARG ASN LEU GLN THR ALA GLU ILE TYR ALA
SEQRES 20 B 464 SER HIS GLU ALA LEU VAL LEU ASP TYR GLU ARG ALA MET
SEQRES 21 B 464 LEU ARG LEU SER ASP GLY ASP ASP GLY GLU PRO GLN LEU
SEQRES 22 B 464 PHE ASP LEU SER ALA HIS THR VAL TRP ILE GLY GLU ARG
SEQRES 23 B 464 THR ARG GLN ILE ASP GLY ALA HIS ILE ALA PHE ALA GLN
SEQRES 24 B 464 VAL ILE ALA ASN PRO VAL GLY VAL LYS LEU GLY PRO ASN
SEQRES 25 B 464 MET THR PRO GLU LEU ALA VAL GLU TYR VAL GLU ARG LEU
SEQRES 26 B 464 ASP PRO HIS ASN LYS PRO GLY ARG LEU THR LEU VAL SER
SEQRES 27 B 464 ARG MET GLY ASN HIS LYS VAL ARG ASP LEU LEU PRO PRO
SEQRES 28 B 464 ILE VAL GLU LYS VAL GLN ALA THR GLY HIS GLN VAL ILE
SEQRES 29 B 464 TRP GLN CYS ASP PRO MET HIS GLY ASN THR HIS GLU SER
SEQRES 30 B 464 SER THR GLY PHE LYS THR ARG HIS PHE ASP ARG ILE VAL
SEQRES 31 B 464 ASP GLU VAL GLN GLY PHE PHE GLU VAL HIS ARG ALA LEU
SEQRES 32 B 464 GLY THR HIS PRO GLY GLY ILE HIS VAL GLU ILE THR GLY
SEQRES 33 B 464 GLU ASN VAL THR GLU CYS LEU GLY GLY ALA GLN ASP ILE
SEQRES 34 B 464 SER GLU THR ASP LEU ALA GLY ARG TYR GLU THR ALA CYS
SEQRES 35 B 464 ASP PRO ARG LEU ASN THR GLN GLN SER LEU GLU LEU ALA
SEQRES 36 B 464 PHE LEU VAL ALA GLU MET LEU ARG ASP
HET PHE A9003 12
HET TRP A9004 15
HET GOL A2647 6
HET GOL A 466 6
HET PO4 A 463 5
HET PO4 A 464 5
HET MN A 465 1
HET CL A 467 1
HET GOL A 468 6
HET GOL A 469 6
HET GOL A 470 6
HET CL A 471 1
HET GOL A 472 6
HET GOL A 473 6
HET GOL A 474 6
HET GOL A 475 6
HET PHE B9001 12
HET TRP B9004 15
HET PO4 B 463 5
HET SO4 B 464 5
HET SO4 B 465 5
HET MN B 466 1
HET GOL B2647 6
HET GOL B 467 6
HET PHE B4188 12
HET GOL B 468 6
HET GOL B 469 6
HET GOL B 470 6
HET GOL B 471 6
HET GOL B 472 6
HETNAM PHE PHENYLALANINE
HETNAM TRP TRYPTOPHAN
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 PHE 3(C9 H11 N O2)
FORMUL 4 TRP 2(C11 H12 N2 O2)
FORMUL 5 GOL 16(C3 H8 O3)
FORMUL 7 PO4 3(O4 P 3-)
FORMUL 9 MN 2(MN 2+)
FORMUL 10 CL 2(CL 1-)
FORMUL 22 SO4 2(O4 S 2-)
FORMUL 33 HOH *771(H2 O)
HELIX 1 1 PRO A 19 ALA A 31 1 13
HELIX 2 2 PRO A 41 GLU A 53 1 13
HELIX 3 3 VAL A 60 LYS A 76 1 17
HELIX 4 4 THR A 90 ASN A 94 5 5
HELIX 5 5 THR A 95 SER A 118 1 24
HELIX 6 6 ASP A 158 GLU A 163 1 6
HELIX 7 7 SER A 167 SER A 189 1 23
HELIX 8 8 SER A 193 SER A 208 1 16
HELIX 9 9 ALA A 210 CYS A 231 1 22
HELIX 10 10 ASP A 235 GLN A 239 5 5
HELIX 11 11 VAL A 251 MET A 258 1 8
HELIX 12 12 GLY A 290 ILE A 299 1 10
HELIX 13 13 THR A 312 ASP A 324 1 13
HELIX 14 14 LYS A 342 ALA A 356 1 15
HELIX 15 15 HIS A 383 GLY A 402 1 20
HELIX 16 16 THR A 430 GLY A 434 5 5
HELIX 17 17 ASN A 445 ASP A 462 1 18
HELIX 18 18 PRO B 19 LYS B 32 1 14
HELIX 19 19 PRO B 41 GLU B 53 1 13
HELIX 20 20 VAL B 60 LYS B 76 1 17
HELIX 21 21 THR B 95 SER B 118 1 24
HELIX 22 22 SER B 167 SER B 189 1 23
HELIX 23 23 SER B 193 SER B 208 1 16
HELIX 24 24 ALA B 210 CYS B 231 1 22
HELIX 25 25 ASP B 235 GLN B 239 5 5
HELIX 26 26 VAL B 251 MET B 258 1 8
HELIX 27 27 GLY B 290 ILE B 299 1 10
HELIX 28 28 THR B 312 ASP B 324 1 13
HELIX 29 29 LYS B 342 ALA B 356 1 15
HELIX 30 30 HIS B 383 GLY B 402 1 20
HELIX 31 31 THR B 430 GLY B 434 5 5
HELIX 32 32 ASN B 445 ASP B 462 1 18
SHEET 1 A 2 THR A 4 PRO A 8 0
SHEET 2 A 2 ASN B 2 ASP B 6 -1 O TRP B 3 N ILE A 7
SHEET 1 B 9 PHE A 80 GLY A 85 0
SHEET 2 B 9 VAL A 121 ARG A 126 1 O VAL A 124 N LEU A 82
SHEET 3 B 9 ILE A 243 GLU A 248 1 O TYR A 244 N ALA A 125
SHEET 4 B 9 THR A 278 ILE A 281 1 N THR A 278 O ALA A 245
SHEET 5 B 9 VAL A 303 LEU A 307 1 O GLY A 304 N ILE A 281
SHEET 6 B 9 LEU A 332 SER A 336 1 O VAL A 335 N LEU A 307
SHEET 7 B 9 ILE A 362 CYS A 365 1 O ILE A 362 N LEU A 334
SHEET 8 B 9 GLY A 407 GLU A 411 1 O HIS A 409 N CYS A 365
SHEET 9 B 9 PHE A 80 GLY A 85 1 N GLN A 83 O VAL A 410
SHEET 1 C 2 LEU A 259 LEU A 261 0
SHEET 2 C 2 LEU A 271 ASP A 273 -1 O PHE A 272 N ARG A 260
SHEET 1 D 2 THR A 372 GLU A 374 0
SHEET 2 D 2 LYS A 380 ARG A 382 -1 O THR A 381 N HIS A 373
SHEET 1 E 9 PHE B 80 GLY B 85 0
SHEET 2 E 9 VAL B 121 ARG B 126 1 O VAL B 124 N LEU B 82
SHEET 3 E 9 ILE B 243 GLU B 248 1 O TYR B 244 N ALA B 125
SHEET 4 E 9 THR B 278 ILE B 281 1 N THR B 278 O ALA B 245
SHEET 5 E 9 VAL B 303 LEU B 307 1 O LYS B 306 N ILE B 281
SHEET 6 E 9 LEU B 332 SER B 336 1 O VAL B 335 N LEU B 307
SHEET 7 E 9 ILE B 362 CYS B 365 1 O ILE B 362 N LEU B 334
SHEET 8 E 9 GLY B 407 GLU B 411 1 O GLY B 407 N CYS B 365
SHEET 9 E 9 PHE B 80 GLY B 85 1 N GLN B 83 O VAL B 410
SHEET 1 F 2 LEU B 259 SER B 262 0
SHEET 2 F 2 GLN B 270 ASP B 273 -1 O GLN B 270 N SER B 262
LINK SG CYS A 87 MN MN A 465 1555 1555 2.50
LINK NE2 HIS A 369 MN MN A 465 1555 1555 2.45
LINK OE2 GLU A 411 MN MN A 465 1555 1555 1.99
LINK OE1 GLU A 411 MN MN A 465 1555 1555 2.60
LINK OD2 ASP A 441 MN MN A 465 1555 1555 2.33
LINK MN MN A 465 O HOH A 586 1555 1555 2.23
LINK SG CYS B 87 MN MN B 466 1555 1555 2.65
LINK NE2 HIS B 369 MN MN B 466 1555 1555 2.47
LINK OE2 GLU B 411 MN MN B 466 1555 1555 2.13
LINK OE1 GLU B 411 MN MN B 466 1555 1555 2.82
LINK OD2 ASP B 441 MN MN B 466 1555 1555 2.54
SITE 1 AC1 8 PHE A 91 MET A 92 ARG A 171 ALA A 174
SITE 2 AC1 8 ASN A 175 HOH A2666 VAL B 5 HOH B4224
SITE 1 AC2 11 VAL A 111 LYS A 123 ALA A 192 CYS A 231
SITE 2 AC2 11 ASN A 237 LEU A 238 THR A 240 HOH A 540
SITE 3 AC2 11 HOH A2683 HOH A2831 HOH A4195
SITE 1 AC3 9 THR A 24 ASP A 27 ALA A 28 GOL A 470
SITE 2 AC3 9 HOH A2888 ARG B 25 VAL B 298 HOH B2747
SITE 3 AC3 9 HOH B4222
SITE 1 AC4 6 LEU A 30 ALA A 34 ASP A 253 ARG A 256
SITE 2 AC4 6 HOH A 522 HOH A2964
SITE 1 AC5 10 GLY A 282 GLU A 283 LYS A 306 ARG A 337
SITE 2 AC5 10 HIS A 369 HOH A 520 HOH A 521 HOH A2698
SITE 3 AC5 10 HOH A2959 HOH A3031
SITE 1 AC6 12 THR A 39 ARG A 135 ASP A 138 ARG A 145
SITE 2 AC6 12 ARG A 148 HIS A 164 GOL A 475 HOH A 567
SITE 3 AC6 12 HOH A 569 HOH A 629 HOH A2792 HOH A4245
SITE 1 AC7 5 CYS A 87 HIS A 369 GLU A 411 ASP A 441
SITE 2 AC7 5 HOH A 586
SITE 1 AC8 3 GLN A 36 ARG A 135 GOL A 475
SITE 1 AC9 7 GLN A 44 MET A 48 ASP A 165 HOH A 552
SITE 2 AC9 7 HOH A 556 MET B 1 ASN B 2
SITE 1 BC1 7 MET A 180 THR A 187 ALA A 241 GLU A 242
SITE 2 BC1 7 ILE A 243 HIS A 277 HOH A 503
SITE 1 BC2 6 ARG A 23 THR A 24 ASP A 27 GOL A2647
SITE 2 BC2 6 GLN B 297 ARG B 322
SITE 1 BC3 3 HOH A 499 ARG B 25 HOH B 590
SITE 1 BC4 3 SER A 188 GLY A 190 GLN A 239
SITE 1 BC5 5 LEU A 46 ALA A 47 THR A 50 HOH A 587
SITE 2 BC5 5 HOH A4229
SITE 1 BC6 5 ARG A 135 SER A 136 ALA A 137 ARG A 284
SITE 2 BC6 5 HOH A2688
SITE 1 BC7 9 GLN A 36 ARG A 135 SER A 136 ALA A 137
SITE 2 BC7 9 ASP A 138 ARG A 148 PO4 A 464 CL A 467
SITE 3 BC7 9 HOH A 624
SITE 1 BC8 7 TYR A 173 HOH A 538 HOH A2884 PHE B 91
SITE 2 BC8 7 ARG B 171 ASN B 175 HOH B2735
SITE 1 BC9 14 LEU B 107 VAL B 111 LYS B 123 ALA B 192
SITE 2 BC9 14 LEU B 194 CYS B 231 ASN B 237 LEU B 238
SITE 3 BC9 14 THR B 240 ALA B 241 HOH B 474 HOH B 475
SITE 4 BC9 14 HOH B 495 HOH B2670
SITE 1 CC1 8 GLY B 282 GLU B 283 LYS B 306 ARG B 337
SITE 2 CC1 8 HOH B 546 HOH B2720 HOH B2935 HOH B2992
SITE 1 CC2 4 ARG B 135 SER B 136 ALA B 137 ARG B 284
SITE 1 CC3 9 PRO B 17 LEU B 18 ARG B 23 LEU B 144
SITE 2 CC3 9 ASP B 158 ALA B 159 HOH B 605 HOH B2677
SITE 3 CC3 9 HOH B2894
SITE 1 CC4 4 CYS B 87 HIS B 369 GLU B 411 ASP B 441
SITE 1 CC5 8 GLN B 70 VAL B 121 GLU B 242 HOH B 473
SITE 2 CC5 8 HOH B 474 HOH B 495 HOH B2710 HOH B4244
SITE 1 CC6 7 GLU B 63 ARG B 66 MET B 180 THR B 187
SITE 2 CC6 7 GLU B 242 ILE B 243 HIS B 277
SITE 1 CC7 8 LEU B 18 ARG B 23 LEU B 26 GLU B 53
SITE 2 CC7 8 ARG B 256 LEU B 259 HOH B2878 HOH B4288
SITE 1 CC8 5 LEU B 30 ASP B 253 ARG B 256 HOH B 553
SITE 2 CC8 5 HOH B2934
SITE 1 CC9 6 THR B 90 MET B 92 ASP B 93 PHE B 155
SITE 2 CC9 6 GLU B 437 HOH B 493
SITE 1 DC1 4 ASP B 43 LEU B 46 ALA B 47 THR B 50
SITE 1 DC2 6 SER A 62 ASP A 263 ARG B 100 SER B 189
SITE 2 DC2 6 GLY B 190 LEU B 191
SITE 1 DC3 6 ARG A 145 HOH A4245 PRO B 33 ALA B 34
SITE 2 DC3 6 ALA B 35 HOH B2665
CRYST1 204.537 204.537 66.462 90.00 90.00 120.00 P 32 2 1 12
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 0.004889 0.002823 0.000000 0.00000
SCALE2 0.000000 0.005645 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
