HEADER OXIDOREDUCTASE 13-MAY-02 1LQT
TITLE A COVALENT MODIFICATION OF NADP+ REVEALED BY THE ATOMIC RESOLUTION
TITLE 2 STRUCTURE OF FPRA, A MYCOBACTERIUM TUBERCULOSIS OXIDOREDUCTASE
CAVEAT 1LQT CHIRALITY ERROR AT THE CA CENTER OF ASP A 31.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FPRA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FERREDOXIN NADP REDUCTASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NADP+ DERIVATIVE, TUBERCULOSIS, OXIDOREDUCTASE, STRUCTURAL GENOMICS,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.BOSSI,A.ALIVERTI,D.RAIMONDI,F.FISCHER,G.ZANETTI,D.FERRARI,
AUTHOR 2 N.TAHALLAH,C.S.MAIER,A.J.R.HECK,M.RIZZI,A.MATTEVI,TB STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (TBSGC)
REVDAT 7 25-OCT-23 1LQT 1 REMARK LINK
REVDAT 6 11-OCT-17 1LQT 1 REMARK
REVDAT 5 13-JUL-11 1LQT 1 VERSN
REVDAT 4 24-FEB-09 1LQT 1 VERSN
REVDAT 3 01-FEB-05 1LQT 1 JRNL AUTHOR KEYWDS REMARK
REVDAT 2 16-OCT-02 1LQT 3 HETATM
REVDAT 1 31-JUL-02 1LQT 0
JRNL AUTH R.T.BOSSI,A.ALIVERTI,D.RAIMONDI,F.FISCHER,G.ZANETTI,
JRNL AUTH 2 D.FERRARI,N.TAHALLAH,C.S.MAIER,A.J.R.HECK,M.RIZZI,A.MATTEVI
JRNL TITL A COVALENT MODIFICATION OF NADP+ REVEALED BY THE ATOMIC
JRNL TITL 2 RESOLUTION STRUCTURE OF FPRA, A MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 3 OXIDOREDUCTASE.
JRNL REF BIOCHEMISTRY V. 41 8807 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12102623
JRNL DOI 10.1021/BI025858A
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 440131
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) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.153
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2200
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) : 1.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 31536
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 184
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6908
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 248
REMARK 3 SOLVENT ATOMS : 1864
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 0.01000
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): 0.023
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.019
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.756
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7499 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6929 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10336 ; 1.747 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16156 ; 0.918 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 967 ; 5.086 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1304 ;15.938 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1209 ; 0.157 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8385 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1447 ; 0.012 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1853 ; 0.395 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7460 ; 0.213 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 6 ; 0.987 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1497 ; 0.241 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 9 ; 0.307 ; 0.500
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): 22 ; 0.426 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 95 ; 0.239 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 129 ; 0.302 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.094 ; 0.500
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): 4661 ; 1.468 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7594 ; 2.172 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2838 ; 3.000 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2737 ; 4.498 ; 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): 7499 ; 1.382 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 1881 ;10.895 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 7344 ; 4.947 ; 5.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1LQT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016195.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 440216
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BEAST
REMARK 200 STARTING MODEL: 1E1L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, PH 5.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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 34.66750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.43650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.60750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.43650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.66750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.60750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 260
REMARK 465 PRO A 399
REMARK 465 GLU A 400
REMARK 465 MET B 1
REMARK 465 GLU B 400
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 OD1 ASN A 349 O HOH A 3154 0.50
REMARK 500 ND2 ASN A 349 O HOH A 3234 0.61
REMARK 500 HD21 ASN A 349 O HOH A 3234 0.79
REMARK 500 HD22 ASN A 349 O HOH A 3234 1.02
REMARK 500 HH21 ARG A 199 HOP3 ODP A 2458 1.13
REMARK 500 OE2 GLU A 449 O HOH A 2682 1.18
REMARK 500 H ARG A 2 O HOH A 3386 1.22
REMARK 500 CH3 ACT A 1870 O HOH A 2636 1.23
REMARK 500 HH11 ARG A 286 OE1 GLU A 312 1.23
REMARK 500 HH21 ARG B 199 HOP3 ODP B 3458 1.24
REMARK 500 H3 ACT A 1870 O HOH A 2636 1.24
REMARK 500 H ARG B 282 O HOH B 4313 1.25
REMARK 500 HH21 ARG A 200 HOP2 ODP A 2458 1.28
REMARK 500 H VAL B 83 HD1 HIS B 87 1.29
REMARK 500 H VAL A 83 HD1 HIS A 87 1.30
REMARK 500 HH21 ARG A 286 O HOH A 3139 1.31
REMARK 500 H2 ACT B 1876 H3D ODP B 3458 1.34
REMARK 500 HH21 ARG B 200 HOP2 ODP B 3458 1.35
REMARK 500 H1 ACT B 1876 O1A ODP B 3458 1.36
REMARK 500 HH12 ARG B 261 O HOH B 4298 1.37
REMARK 500 H1 ACT A 1870 O HOH A 2636 1.37
REMARK 500 HZ1 LYS A 281 O HOH A 3357 1.42
REMARK 500 CG ASN A 349 O HOH A 3154 1.44
REMARK 500 H2 ACT A 1870 O HOH A 2636 1.44
REMARK 500 HH22 ARG B 189 O HOH B 3972 1.46
REMARK 500 HG13 ILE A 60 O HOH A 2865 1.46
REMARK 500 OD1 ASP B 31 H1 ACT B 1873 1.47
REMARK 500 HG1 THR A 381 O HOH A 3379 1.49
REMARK 500 HD2 LYS B 361 O HOH B 4329 1.50
REMARK 500 HG3 GLN B 192 O HOH B 4269 1.53
REMARK 500 HH22 ARG A 189 O HOH A 3388 1.55
REMARK 500 H2 ACT B 1876 O1A ODP B 3458 1.57
REMARK 500 OD1 ASP B 31 H2 ACT B 1873 1.59
REMARK 500 OD1 ASP B 127 O HOH B 3885 1.69
REMARK 500 OD1 ASP A 127 O HOH A 2848 1.77
REMARK 500 CG ASN A 349 O HOH A 3234 1.81
REMARK 500 O HOH A 2749 O HOH A 3412 1.83
REMARK 500 N ARG A 2 O HOH A 3386 1.87
REMARK 500 OD1 ASP B 118 O HOH B 4330 1.89
REMARK 500 O HOH B 3932 O HOH B 4339 1.90
REMARK 500 O HOH A 3387 O HOH A 3404 1.90
REMARK 500 O HOH A 2668 O HOH A 3296 1.91
REMARK 500 O HOH A 2691 O HOH A 3179 1.92
REMARK 500 NH1 ARG A 286 OE1 GLU A 312 1.93
REMARK 500 O HOH A 3291 O HOH A 3314 1.93
REMARK 500 NH2 ARG A 286 O HOH A 3139 1.94
REMARK 500 CD LYS B 361 O HOH B 4329 1.95
REMARK 500 NE2 HIS A 264 O HOH A 3408 1.99
REMARK 500 O HOH B 4314 O HOH B 4319 2.02
REMARK 500 NE ARG B 265 O HOH B 4299 2.03
REMARK 500
REMARK 500 THIS ENTRY HAS 95 CLOSE CONTACTS
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 OXT ACT B 1868 O HOH A 3320 1565 0.65
REMARK 500 C ACT B 1868 O HOH A 3320 1565 1.82
REMARK 500 O HOH A 3325 O HOH B 3803 3545 1.84
REMARK 500 O HOH A 2970 O HOH A 3396 4445 1.99
REMARK 500 O HOH A 2684 O HOH B 4333 1545 2.01
REMARK 500 O HOH A 3425 O HOH B 3695 4455 2.02
REMARK 500 O HOH A 3383 O HOH B 4315 1545 2.07
REMARK 500 O HOH A 3363 O HOH B 4202 3545 2.10
REMARK 500 O HOH B 4173 O HOH B 4183 1455 2.12
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 A 33 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 164 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 441 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 31 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 MET B 34 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 401 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 441 NE - CZ - NH1 ANGL. DEV. = 5.2 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 SER A 11 26.19 -141.28
REMARK 500 TRP A 46 -5.58 98.24
REMARK 500 SER A 108 -166.19 -125.06
REMARK 500 ARG A 282 -4.74 69.02
REMARK 500 SER A 321 64.47 -114.77
REMARK 500 ASN A 353 16.00 -147.83
REMARK 500 SER B 11 24.55 -141.72
REMARK 500 TRP B 46 -4.06 97.24
REMARK 500 HIS B 57 51.93 -117.80
REMARK 500 GLU B 86 -65.07 -122.75
REMARK 500 SER B 108 -165.57 -126.73
REMARK 500 PRO B 262 -29.94 -34.77
REMARK 500 ARG B 282 -24.82 79.14
REMARK 500 SER B 321 64.83 -117.64
REMARK 500 ASN B 353 18.27 -150.03
REMARK 500 LYS B 416 44.10 -106.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1866
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1867
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1868
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1869
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1870
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1871
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1872
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1873
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1874
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1875
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1876
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 2457
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ODP A 2458
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 3457
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ODP B 3458
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LQU RELATED DB: PDB
REMARK 900 1LQU CONTAINS THE SAME PROTEIN COMPLEXED WITH NADPH
REMARK 900 RELATED ID: RV3106 RELATED DB: TARGETDB
DBREF 1LQT A 1 456 UNP O05783 FPRA_MYCTU 1 456
DBREF 1LQT B 1 456 UNP O05783 FPRA_MYCTU 1 456
SEQRES 1 A 456 MET ARG PRO TYR TYR ILE ALA ILE VAL GLY SER GLY PRO
SEQRES 2 A 456 SER ALA PHE PHE ALA ALA ALA SER LEU LEU LYS ALA ALA
SEQRES 3 A 456 ASP THR THR GLU ASP LEU ASP MET ALA VAL ASP MET LEU
SEQRES 4 A 456 GLU MET LEU PRO THR PRO TRP GLY LEU VAL ARG SER GLY
SEQRES 5 A 456 VAL ALA PRO ASP HIS PRO LYS ILE LYS SER ILE SER LYS
SEQRES 6 A 456 GLN PHE GLU LYS THR ALA GLU ASP PRO ARG PHE ARG PHE
SEQRES 7 A 456 PHE GLY ASN VAL VAL VAL GLY GLU HIS VAL GLN PRO GLY
SEQRES 8 A 456 GLU LEU SER GLU ARG TYR ASP ALA VAL ILE TYR ALA VAL
SEQRES 9 A 456 GLY ALA GLN SER ASP ARG MET LEU ASN ILE PRO GLY GLU
SEQRES 10 A 456 ASP LEU PRO GLY SER ILE ALA ALA VAL ASP PHE VAL GLY
SEQRES 11 A 456 TRP TYR ASN ALA HIS PRO HIS PHE GLU GLN VAL SER PRO
SEQRES 12 A 456 ASP LEU SER GLY ALA ARG ALA VAL VAL ILE GLY ASN GLY
SEQRES 13 A 456 ASN VAL ALA LEU ASP VAL ALA ARG ILE LEU LEU THR ASP
SEQRES 14 A 456 PRO ASP VAL LEU ALA ARG THR ASP ILE ALA ASP HIS ALA
SEQRES 15 A 456 LEU GLU SER LEU ARG PRO ARG GLY ILE GLN GLU VAL VAL
SEQRES 16 A 456 ILE VAL GLY ARG ARG GLY PRO LEU GLN ALA ALA PHE THR
SEQRES 17 A 456 THR LEU GLU LEU ARG GLU LEU ALA ASP LEU ASP GLY VAL
SEQRES 18 A 456 ASP VAL VAL ILE ASP PRO ALA GLU LEU ASP GLY ILE THR
SEQRES 19 A 456 ASP GLU ASP ALA ALA ALA VAL GLY LYS VAL CYS LYS GLN
SEQRES 20 A 456 ASN ILE LYS VAL LEU ARG GLY TYR ALA ASP ARG GLU PRO
SEQRES 21 A 456 ARG PRO GLY HIS ARG ARG MET VAL PHE ARG PHE LEU THR
SEQRES 22 A 456 SER PRO ILE GLU ILE LYS GLY LYS ARG LYS VAL GLU ARG
SEQRES 23 A 456 ILE VAL LEU GLY ARG ASN GLU LEU VAL SER ASP GLY SER
SEQRES 24 A 456 GLY ARG VAL ALA ALA LYS ASP THR GLY GLU ARG GLU GLU
SEQRES 25 A 456 LEU PRO ALA GLN LEU VAL VAL ARG SER VAL GLY TYR ARG
SEQRES 26 A 456 GLY VAL PRO THR PRO GLY LEU PRO PHE ASP ASP GLN SER
SEQRES 27 A 456 GLY THR ILE PRO ASN VAL GLY GLY ARG ILE ASN GLY SER
SEQRES 28 A 456 PRO ASN GLU TYR VAL VAL GLY TRP ILE LYS ARG GLY PRO
SEQRES 29 A 456 THR GLY VAL ILE GLY THR ASN LYS LYS ASP ALA GLN ASP
SEQRES 30 A 456 THR VAL ASP THR LEU ILE LYS ASN LEU GLY ASN ALA LYS
SEQRES 31 A 456 GLU GLY ALA GLU CYS LYS SER PHE PRO GLU ASP HIS ALA
SEQRES 32 A 456 ASP GLN VAL ALA ASP TRP LEU ALA ALA ARG GLN PRO LYS
SEQRES 33 A 456 LEU VAL THR SER ALA HIS TRP GLN VAL ILE ASP ALA PHE
SEQRES 34 A 456 GLU ARG ALA ALA GLY GLU PRO HIS GLY ARG PRO ARG VAL
SEQRES 35 A 456 LYS LEU ALA SER LEU ALA GLU LEU LEU ARG ILE GLY LEU
SEQRES 36 A 456 GLY
SEQRES 1 B 456 MET ARG PRO TYR TYR ILE ALA ILE VAL GLY SER GLY PRO
SEQRES 2 B 456 SER ALA PHE PHE ALA ALA ALA SER LEU LEU LYS ALA ALA
SEQRES 3 B 456 ASP THR THR GLU ASP LEU ASP MET ALA VAL ASP MET LEU
SEQRES 4 B 456 GLU MET LEU PRO THR PRO TRP GLY LEU VAL ARG SER GLY
SEQRES 5 B 456 VAL ALA PRO ASP HIS PRO LYS ILE LYS SER ILE SER LYS
SEQRES 6 B 456 GLN PHE GLU LYS THR ALA GLU ASP PRO ARG PHE ARG PHE
SEQRES 7 B 456 PHE GLY ASN VAL VAL VAL GLY GLU HIS VAL GLN PRO GLY
SEQRES 8 B 456 GLU LEU SER GLU ARG TYR ASP ALA VAL ILE TYR ALA VAL
SEQRES 9 B 456 GLY ALA GLN SER ASP ARG MET LEU ASN ILE PRO GLY GLU
SEQRES 10 B 456 ASP LEU PRO GLY SER ILE ALA ALA VAL ASP PHE VAL GLY
SEQRES 11 B 456 TRP TYR ASN ALA HIS PRO HIS PHE GLU GLN VAL SER PRO
SEQRES 12 B 456 ASP LEU SER GLY ALA ARG ALA VAL VAL ILE GLY ASN GLY
SEQRES 13 B 456 ASN VAL ALA LEU ASP VAL ALA ARG ILE LEU LEU THR ASP
SEQRES 14 B 456 PRO ASP VAL LEU ALA ARG THR ASP ILE ALA ASP HIS ALA
SEQRES 15 B 456 LEU GLU SER LEU ARG PRO ARG GLY ILE GLN GLU VAL VAL
SEQRES 16 B 456 ILE VAL GLY ARG ARG GLY PRO LEU GLN ALA ALA PHE THR
SEQRES 17 B 456 THR LEU GLU LEU ARG GLU LEU ALA ASP LEU ASP GLY VAL
SEQRES 18 B 456 ASP VAL VAL ILE ASP PRO ALA GLU LEU ASP GLY ILE THR
SEQRES 19 B 456 ASP GLU ASP ALA ALA ALA VAL GLY LYS VAL CYS LYS GLN
SEQRES 20 B 456 ASN ILE LYS VAL LEU ARG GLY TYR ALA ASP ARG GLU PRO
SEQRES 21 B 456 ARG PRO GLY HIS ARG ARG MET VAL PHE ARG PHE LEU THR
SEQRES 22 B 456 SER PRO ILE GLU ILE LYS GLY LYS ARG LYS VAL GLU ARG
SEQRES 23 B 456 ILE VAL LEU GLY ARG ASN GLU LEU VAL SER ASP GLY SER
SEQRES 24 B 456 GLY ARG VAL ALA ALA LYS ASP THR GLY GLU ARG GLU GLU
SEQRES 25 B 456 LEU PRO ALA GLN LEU VAL VAL ARG SER VAL GLY TYR ARG
SEQRES 26 B 456 GLY VAL PRO THR PRO GLY LEU PRO PHE ASP ASP GLN SER
SEQRES 27 B 456 GLY THR ILE PRO ASN VAL GLY GLY ARG ILE ASN GLY SER
SEQRES 28 B 456 PRO ASN GLU TYR VAL VAL GLY TRP ILE LYS ARG GLY PRO
SEQRES 29 B 456 THR GLY VAL ILE GLY THR ASN LYS LYS ASP ALA GLN ASP
SEQRES 30 B 456 THR VAL ASP THR LEU ILE LYS ASN LEU GLY ASN ALA LYS
SEQRES 31 B 456 GLU GLY ALA GLU CYS LYS SER PHE PRO GLU ASP HIS ALA
SEQRES 32 B 456 ASP GLN VAL ALA ASP TRP LEU ALA ALA ARG GLN PRO LYS
SEQRES 33 B 456 LEU VAL THR SER ALA HIS TRP GLN VAL ILE ASP ALA PHE
SEQRES 34 B 456 GLU ARG ALA ALA GLY GLU PRO HIS GLY ARG PRO ARG VAL
SEQRES 35 B 456 LYS LEU ALA SER LEU ALA GLU LEU LEU ARG ILE GLY LEU
SEQRES 36 B 456 GLY
HET ACT A1866 7
HET ACT A1869 7
HET ACT A1870 7
HET ACT A1871 7
HET ACT A1872 7
HET FAD A2457 86
HET ODP A2458 76
HET ACT B1867 7
HET ACT B1868 7
HET ACT B1873 7
HET ACT B1874 7
HET ACT B1875 7
HET ACT B1876 7
HET FAD B3457 86
HET ODP B3458 76
HETNAM ACT ACETATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM ODP 4-OXO-NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE
FORMUL 3 ACT 11(C2 H3 O2 1-)
FORMUL 8 FAD 2(C27 H33 N9 O15 P2)
FORMUL 9 ODP 2(C21 H29 N7 O18 P3 1+)
FORMUL 18 HOH *1864(H2 O)
HELIX 1 1 GLY A 12 THR A 29 1 18
HELIX 2 2 GLY A 47 GLY A 52 1 6
HELIX 3 3 PRO A 58 SER A 62 5 5
HELIX 4 4 ILE A 63 GLU A 72 1 10
HELIX 5 5 GLN A 89 TYR A 97 1 9
HELIX 6 6 ALA A 125 ASN A 133 1 9
HELIX 7 7 HIS A 135 GLU A 139 5 5
HELIX 8 8 GLY A 156 THR A 168 1 13
HELIX 9 9 ASP A 169 ALA A 174 1 6
HELIX 10 10 ALA A 179 ARG A 187 1 9
HELIX 11 11 GLY A 201 ALA A 205 5 5
HELIX 12 12 THR A 208 LEU A 215 1 8
HELIX 13 13 ALA A 216 LEU A 218 5 3
HELIX 14 14 ASP A 226 ASP A 231 5 6
HELIX 15 15 THR A 234 GLY A 242 1 9
HELIX 16 16 GLY A 242 ASP A 257 1 16
HELIX 17 17 GLY A 358 GLY A 363 1 6
HELIX 18 18 VAL A 367 GLY A 369 5 3
HELIX 19 19 THR A 370 GLY A 392 1 23
HELIX 20 20 ASP A 401 GLN A 414 1 14
HELIX 21 21 SER A 420 GLU A 435 1 16
HELIX 22 22 PRO A 436 GLY A 438 5 3
HELIX 23 23 SER A 446 LEU A 455 1 10
HELIX 24 24 GLY B 12 THR B 29 1 18
HELIX 25 25 GLY B 47 GLY B 52 1 6
HELIX 26 26 LYS B 59 SER B 62 5 4
HELIX 27 27 ILE B 63 GLU B 72 1 10
HELIX 28 28 GLN B 89 TYR B 97 1 9
HELIX 29 29 ALA B 125 ASN B 133 1 9
HELIX 30 30 HIS B 135 GLU B 139 5 5
HELIX 31 31 GLY B 156 THR B 168 1 13
HELIX 32 32 ASP B 169 ALA B 174 1 6
HELIX 33 33 ALA B 179 ARG B 187 1 9
HELIX 34 34 GLY B 201 ALA B 205 5 5
HELIX 35 35 THR B 208 GLU B 214 1 7
HELIX 36 36 LEU B 215 LEU B 218 5 4
HELIX 37 37 ASP B 226 ASP B 231 5 6
HELIX 38 38 THR B 234 GLY B 242 1 9
HELIX 39 39 GLY B 242 ASP B 257 1 16
HELIX 40 40 GLY B 358 GLY B 363 1 6
HELIX 41 41 VAL B 367 GLY B 369 5 3
HELIX 42 42 THR B 370 GLY B 392 1 23
HELIX 43 43 ASP B 401 GLN B 414 1 14
HELIX 44 44 SER B 420 GLU B 435 1 16
HELIX 45 45 PRO B 436 GLY B 438 5 3
HELIX 46 46 SER B 446 LEU B 455 1 10
SHEET 1 A 6 GLU A 354 VAL A 356 0
SHEET 2 A 6 ALA A 99 TYR A 102 1 N TYR A 102 O TYR A 355
SHEET 3 A 6 TYR A 4 VAL A 9 1 N VAL A 9 O ILE A 101
SHEET 4 A 6 MET A 34 GLU A 40 1 O LEU A 39 N ILE A 8
SHEET 5 A 6 PHE A 76 GLY A 80 1 O ARG A 77 N MET A 38
SHEET 6 A 6 VAL A 418 THR A 419 -1 O VAL A 418 N GLY A 80
SHEET 1 B 2 SER A 108 ASP A 109 0
SHEET 2 B 2 TYR A 324 ARG A 325 -1 O ARG A 325 N SER A 108
SHEET 1 C 6 SER A 122 ALA A 124 0
SHEET 2 C 6 LEU A 317 ARG A 320 1 O ARG A 320 N ILE A 123
SHEET 3 C 6 ARG A 149 ILE A 153 1 N VAL A 151 O VAL A 319
SHEET 4 C 6 GLU A 193 VAL A 197 1 O VAL A 197 N VAL A 152
SHEET 5 C 6 ARG A 265 ARG A 270 1 O VAL A 268 N ILE A 196
SHEET 6 C 6 VAL A 221 VAL A 224 1 N VAL A 224 O MET A 267
SHEET 1 D 3 THR A 273 LYS A 279 0
SHEET 2 D 3 ARG A 286 SER A 296 -1 O VAL A 288 N GLU A 277
SHEET 3 D 3 VAL A 302 PRO A 314 -1 O GLU A 311 N LEU A 289
SHEET 1 E 2 ASN A 343 VAL A 344 0
SHEET 2 E 2 ARG A 347 ILE A 348 -1 O ARG A 347 N VAL A 344
SHEET 1 F 6 GLU B 354 VAL B 356 0
SHEET 2 F 6 ALA B 99 TYR B 102 1 N TYR B 102 O TYR B 355
SHEET 3 F 6 TYR B 4 VAL B 9 1 N VAL B 9 O ILE B 101
SHEET 4 F 6 MET B 34 GLU B 40 1 O LEU B 39 N ILE B 8
SHEET 5 F 6 PHE B 76 GLY B 80 1 O ARG B 77 N MET B 38
SHEET 6 F 6 VAL B 418 THR B 419 -1 O VAL B 418 N GLY B 80
SHEET 1 G 2 SER B 108 ASP B 109 0
SHEET 2 G 2 TYR B 324 ARG B 325 -1 O ARG B 325 N SER B 108
SHEET 1 H 6 SER B 122 ALA B 124 0
SHEET 2 H 6 LEU B 317 ARG B 320 1 O VAL B 318 N ILE B 123
SHEET 3 H 6 ARG B 149 ILE B 153 1 N VAL B 151 O VAL B 319
SHEET 4 H 6 GLU B 193 VAL B 197 1 O VAL B 197 N VAL B 152
SHEET 5 H 6 ARG B 265 ARG B 270 1 O VAL B 268 N ILE B 196
SHEET 6 H 6 VAL B 221 VAL B 224 1 N VAL B 224 O MET B 267
SHEET 1 I 3 THR B 273 LYS B 279 0
SHEET 2 I 3 ARG B 286 SER B 296 -1 O VAL B 288 N GLU B 277
SHEET 3 I 3 VAL B 302 PRO B 314 -1 O GLU B 311 N LEU B 289
SHEET 1 J 2 ASN B 343 VAL B 344 0
SHEET 2 J 2 ARG B 347 ILE B 348 -1 O ARG B 347 N VAL B 344
LINK OD1BASP B 31 CH3 ACT B1873 1555 1555 1.55
LINK CH3 ACT B1876 O1A ODP B3458 1555 1555 1.74
SITE 1 AC1 8 ARG A 110 MET A 111 LEU A 112 ASN A 113
SITE 2 AC1 8 VAL A 322 ODP A2458 HOH A2833 HOH A3054
SITE 1 AC2 3 ALA B 148 GLN B 192 HOH B4269
SITE 1 AC3 10 ARG A 452 HOH A3223 HOH A3309 HOH A3320
SITE 2 AC3 10 HOH A3373 HIS B 422 GLY B 454 HOH B3674
SITE 3 AC3 10 HOH B3985 HOH B4097
SITE 1 AC4 5 ASP A 56 GLU A 214 ACT A1870 HOH A2842
SITE 2 AC4 5 HOH A3052
SITE 1 AC5 9 HIS A 57 PRO A 58 LYS A 59 ILE A 60
SITE 2 AC5 9 ACT A1869 HOH A2636 HOH A3023 HOH A3186
SITE 3 AC5 9 HOH A3427
SITE 1 AC6 6 ALA A 71 PHE A 78 SER A 420 HOH A2546
SITE 2 AC6 6 HOH A2572 HOH A2672
SITE 1 AC7 5 ASN A 292 ALA A 304 HOH A2531 HOH A2562
SITE 2 AC7 5 GLU B 391
SITE 1 AC8 5 ARG B 2 ASP B 31 ASP B 33 HOH B3658
SITE 2 AC8 5 HOH B4281
SITE 1 AC9 5 ALA B 71 PHE B 78 SER B 420 HOH B3536
SITE 2 AC9 5 HOH B3849
SITE 1 BC1 8 ARG B 110 MET B 111 LEU B 112 ASN B 113
SITE 2 BC1 8 VAL B 322 ODP B3458 HOH B3971 HOH B3976
SITE 1 BC2 4 ODP B3458 HOH B3470 HOH B3759 HOH B4079
SITE 1 BC3 37 GLY A 10 GLY A 12 PRO A 13 SER A 14
SITE 2 BC3 37 GLU A 40 MET A 41 GLY A 47 LEU A 48
SITE 3 BC3 37 GLY A 52 VAL A 53 ILE A 60 VAL A 82
SITE 4 BC3 37 VAL A 84 ALA A 103 VAL A 104 GLY A 105
SITE 5 BC3 37 VAL A 158 TYR A 324 GLY A 358 TRP A 359
SITE 6 BC3 37 GLY A 366 VAL A 367 ILE A 368 ASN A 371
SITE 7 BC3 37 ODP A2458 HOH A2460 HOH A2461 HOH A2463
SITE 8 BC3 37 HOH A2465 HOH A2468 HOH A2469 HOH A2470
SITE 9 BC3 37 HOH A2505 HOH A2510 HOH A2606 HOH A2691
SITE 10 BC3 37 HOH A2826
SITE 1 BC4 42 ARG A 110 ILE A 153 ASN A 155 GLY A 156
SITE 2 BC4 42 ASN A 157 VAL A 158 ASP A 161 ARG A 199
SITE 3 BC4 42 ARG A 200 ALA A 206 GLU A 211 SER A 321
SITE 4 BC4 42 VAL A 322 TRP A 359 PRO A 364 THR A 365
SITE 5 BC4 42 GLY A 366 VAL A 367 ACT A1866 FAD A2457
SITE 6 BC4 42 HOH A2459 HOH A2460 HOH A2471 HOH A2474
SITE 7 BC4 42 HOH A2476 HOH A2478 HOH A2482 HOH A2484
SITE 8 BC4 42 HOH A2496 HOH A2497 HOH A2533 HOH A2542
SITE 9 BC4 42 HOH A2614 HOH A2617 HOH A2715 HOH A2738
SITE 10 BC4 42 HOH A2753 HOH A2854 HOH A2870 HOH A3179
SITE 11 BC4 42 HOH A3322 HOH A3360
SITE 1 BC5 38 VAL B 9 GLY B 10 GLY B 12 PRO B 13
SITE 2 BC5 38 SER B 14 GLU B 40 MET B 41 GLY B 47
SITE 3 BC5 38 LEU B 48 GLY B 52 VAL B 53 VAL B 82
SITE 4 BC5 38 VAL B 84 ALA B 103 VAL B 104 GLY B 105
SITE 5 BC5 38 VAL B 158 ASP B 161 TYR B 324 GLY B 358
SITE 6 BC5 38 TRP B 359 GLY B 366 VAL B 367 ILE B 368
SITE 7 BC5 38 ASN B 371 ODP B3458 HOH B3461 HOH B3464
SITE 8 BC5 38 HOH B3466 HOH B3468 HOH B3479 HOH B3483
SITE 9 BC5 38 HOH B3525 HOH B3559 HOH B3586 HOH B3636
SITE 10 BC5 38 HOH B3845 HOH B4227
SITE 1 BC6 40 HIS B 57 ARG B 110 ILE B 153 ASN B 155
SITE 2 BC6 40 GLY B 156 ASN B 157 VAL B 158 ASP B 161
SITE 3 BC6 40 ARG B 199 ARG B 200 ALA B 206 GLU B 211
SITE 4 BC6 40 SER B 321 VAL B 322 PRO B 364 GLY B 366
SITE 5 BC6 40 VAL B 367 ACT B1875 ACT B1876 FAD B3457
SITE 6 BC6 40 HOH B3463 HOH B3468 HOH B3470 HOH B3474
SITE 7 BC6 40 HOH B3488 HOH B3491 HOH B3501 HOH B3513
SITE 8 BC6 40 HOH B3527 HOH B3542 HOH B3546 HOH B3554
SITE 9 BC6 40 HOH B3574 HOH B3586 HOH B3620 HOH B3767
SITE 10 BC6 40 HOH B3839 HOH B3852 HOH B3872 HOH B3964
CRYST1 69.335 89.215 160.873 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014423 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
