HEADER OXIDOREDUCTASE 23-DEC-13 4CJX
TITLE THE CRYSTAL STRUCTURE OF TRYPANOSOMA BRUCEI N5, N10-
TITLE 2 METHYLENETETRAHYDROFOLATE DEHYDROGENASE-CYCLOHYDROLASE (FOLD)
TITLE 3 COMPLEXED WITH NADP COFACTOR AND INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.5.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI STRAIN 927/4
SOURCE 3 GUTAT10.1;
SOURCE 4 ORGANISM_TAXID: 999953;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.C.EADSFORTH,W.N.HUNTER
REVDAT 3 20-DEC-23 4CJX 1 REMARK
REVDAT 2 10-FEB-16 4CJX 1 SOURCE JRNL
REVDAT 1 04-FEB-15 4CJX 0
JRNL AUTH T.C.EADSFORTH,A.PINTO,R.LUCIANI,L.TAMBORINI,G.CULLIA,
JRNL AUTH 2 C.DE MICHELI,L.MARINELLI,S.COSCONATI,E.NOVELLINO,
JRNL AUTH 3 L.LO PRESTI,A.CORDEIRO DA SILVA,P.CONTI,W.N.HUNTER,M.P.COSTI
JRNL TITL CHARACTERIZATION OF
JRNL TITL 2 2,4-DIAMINO-6-OXO-1,6-DIHYDROPYRIMIDIN-5-YL UREIDO BASED
JRNL TITL 3 INHIBITORS OF TRYPANOSOMA BRUCEI FOLD AND TESTING FOR
JRNL TITL 4 ANTIPARASITIC ACTIVITY.
JRNL REF J.MED.CHEM. V. 58 7938 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26322631
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00687
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 35419
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1862
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2562
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4450
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 123
REMARK 3 SOLVENT ATOMS : 322
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.03000
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): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.598
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4625 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4669 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6311 ; 1.470 ; 2.019
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10718 ; 0.893 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 609 ; 5.478 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;32.040 ;22.774
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 772 ;14.085 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;15.802 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 768 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5139 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 933 ; 0.009 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2396 ; 0.635 ; 1.161
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2394 ; 0.634 ; 1.160
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2992 ; 1.095 ; 1.733
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2229 ; 1.163 ; 1.406
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2215 -5.0124 -14.1644
REMARK 3 T TENSOR
REMARK 3 T11: 0.0031 T22: 0.1266
REMARK 3 T33: 0.0158 T12: -0.0016
REMARK 3 T13: -0.0009 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.1165 L22: 1.8116
REMARK 3 L33: 0.8042 L12: -0.1867
REMARK 3 L13: -0.0042 L23: 0.3193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: -0.1198 S13: -0.0646
REMARK 3 S21: 0.0126 S22: -0.0144 S23: 0.0357
REMARK 3 S31: 0.0484 S32: -0.0226 S33: -0.0005
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 147 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6407 -5.0148 -9.8209
REMARK 3 T TENSOR
REMARK 3 T11: 0.0107 T22: 0.1014
REMARK 3 T33: 0.0155 T12: 0.0176
REMARK 3 T13: 0.0015 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.4131 L22: 0.2629
REMARK 3 L33: 1.5499 L12: 0.0051
REMARK 3 L13: 0.2364 L23: -0.0201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: -0.0163 S13: -0.0498
REMARK 3 S21: 0.0039 S22: -0.0169 S23: 0.0059
REMARK 3 S31: -0.0502 S32: 0.1304 S33: -0.0180
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 : B 1 B 138
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4997 6.5446 21.6831
REMARK 3 T TENSOR
REMARK 3 T11: 0.0209 T22: 0.2941
REMARK 3 T33: 0.0704 T12: 0.0091
REMARK 3 T13: 0.0124 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 2.6037 L22: 1.6152
REMARK 3 L33: 2.0131 L12: 0.8296
REMARK 3 L13: -0.0997 L23: 0.3049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0878 S12: -0.2310 S13: 0.1163
REMARK 3 S21: 0.1322 S22: -0.1542 S23: 0.2521
REMARK 3 S31: 0.0959 S32: -0.3092 S33: 0.0664
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 : B 139 B 297
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4443 7.2846 17.3257
REMARK 3 T TENSOR
REMARK 3 T11: 0.0057 T22: 0.1224
REMARK 3 T33: 0.0169 T12: -0.0168
REMARK 3 T13: 0.0032 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.4422 L22: 0.9992
REMARK 3 L33: 2.2568 L12: 0.2980
REMARK 3 L13: -0.0488 L23: 0.1631
REMARK 3 S TENSOR
REMARK 3 S11: 0.0658 S12: -0.0399 S13: 0.0866
REMARK 3 S21: -0.0006 S22: -0.0319 S23: 0.1177
REMARK 3 S31: -0.0248 S32: -0.1067 S33: -0.0339
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. DISORDERED SIDECHAINS HAVE AN OCCUPANCY OF 0
REMARK 4
REMARK 4 4CJX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1290059299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37335
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 64.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 4A26
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 6000, 0.1 M CITRIC ACID PH
REMARK 280 5.0
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 29.11000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.45400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.66250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.45400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.11000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.66250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.8 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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 LEU A 298
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 LEU B 298
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 LYS A 18 CE NZ
REMARK 480 GLU A 28 CD OE1 OE2
REMARK 480 ARG A 29 NE CZ NH1 NH2
REMARK 480 LYS A 32 CG CD CE NZ
REMARK 480 ARG A 136 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU A 137 CB CG CD OE1 OE2
REMARK 480 ASN A 139 CA C O CB CG OD1 ND2
REMARK 480 ARG A 155 NE CZ NH1 NH2
REMARK 480 ARG A 293 CD NE CZ NH1 NH2
REMARK 480 LYS B 14 CD CE NZ
REMARK 480 LYS B 18 CD CE NZ
REMARK 480 GLU B 19 CG CD OE1 OE2
REMARK 480 GLU B 28 CD OE1 OE2
REMARK 480 LYS B 32 CB CG CD CE NZ
REMARK 480 LYS B 47 CE NZ
REMARK 480 ARG B 66 CZ NH1 NH2
REMARK 480 ARG B 83 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG B 87 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 115 CE NZ
REMARK 480 ARG B 293 CG CD NE CZ NH1 NH2
REMARK 480 ARG B 296 CG CD NE CZ NH1 NH2
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 NH1 ARG A 46 CE LYS B 32 4555 1.78
REMARK 500 NH1 ARG A 46 NZ LYS B 32 4555 1.85
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 LYS A 18 CD LYS A 18 CE -0.315
REMARK 500 GLU A 28 CG GLU A 28 CD -0.566
REMARK 500 ARG A 29 CD ARG A 29 NE -0.483
REMARK 500 ARG A 136 CA ARG A 136 CB 0.171
REMARK 500 ARG A 155 CD ARG A 155 NE -0.151
REMARK 500 LYS B 18 CG LYS B 18 CD -0.229
REMARK 500 GLU B 19 CB GLU B 19 CG -0.192
REMARK 500 LYS B 32 CA LYS B 32 CB -0.271
REMARK 500 LYS B 47 CD LYS B 47 CE -0.507
REMARK 500 LYS B 115 CD LYS B 115 CE -0.697
REMARK 500 ARG B 296 CB ARG B 296 CG -0.178
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 LYS A 18 CG - CD - CE ANGL. DEV. = 23.7 DEGREES
REMARK 500 GLU A 28 CB - CG - CD ANGL. DEV. = 27.6 DEGREES
REMARK 500 ARG A 29 CG - CD - NE ANGL. DEV. = 26.0 DEGREES
REMARK 500 ARG A 136 CB - CA - C ANGL. DEV. = -14.8 DEGREES
REMARK 500 ARG A 136 N - CA - CB ANGL. DEV. = -16.2 DEGREES
REMARK 500 ASN A 139 C - N - CA ANGL. DEV. = -19.4 DEGREES
REMARK 500 ASN A 139 N - CA - CB ANGL. DEV. = 16.6 DEGREES
REMARK 500 ASN A 139 N - CA - C ANGL. DEV. = -31.2 DEGREES
REMARK 500 PRO A 140 C - N - CA ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO A 140 C - N - CD ANGL. DEV. = 19.1 DEGREES
REMARK 500 ARG A 155 CG - CD - NE ANGL. DEV. = 36.7 DEGREES
REMARK 500 ARG A 155 CD - NE - CZ ANGL. DEV. = 24.0 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLU B 19 CA - CB - CG ANGL. DEV. = 26.7 DEGREES
REMARK 500 LYS B 32 CB - CA - C ANGL. DEV. = 19.2 DEGREES
REMARK 500 LYS B 47 CG - CD - CE ANGL. DEV. = 27.5 DEGREES
REMARK 500 LYS B 47 CD - CE - NZ ANGL. DEV. = 18.8 DEGREES
REMARK 500 LYS B 115 CG - CD - CE ANGL. DEV. = 58.8 DEGREES
REMARK 500 LYS B 115 CD - CE - NZ ANGL. DEV. = 28.8 DEGREES
REMARK 500 ARG B 296 CA - CB - CG ANGL. DEV. = -16.7 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 A 32 58.04 37.16
REMARK 500 GLU A 137 -7.67 -53.30
REMARK 500 ARG A 171 29.87 -141.94
REMARK 500 ALA A 175 -74.33 -130.23
REMARK 500 TYR B 31 74.89 -105.01
REMARK 500 LYS B 32 95.08 -15.04
REMARK 500 ALA B 175 -90.25 -126.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 66 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2023 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B2142 DISTANCE = 6.16 ANGSTROMS
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: (2S)-2-[[4-[[2,4-BIS(AZANYL)-6-OXIDANYLIDENE-1H-
REMARK 630 PYRIMIDIN-5-YL]CARBAMOYLAMINO]PHENYL]CARBONYLAMINO]PENTANEDIOIC
REMARK 630 ACID
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 9L9 A 1300
REMARK 630 9L9 B 1298
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 9LO GLU
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9L9 A 1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9L9 B 1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 1301
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 T80A
DBREF 4CJX A 1 298 UNP Q57WP0 Q57WP0_TRYB2 1 298
DBREF 4CJX B 1 298 UNP Q57WP0 Q57WP0_TRYB2 1 298
SEQADV 4CJX MET A -20 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLY A -19 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER A -18 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER A -17 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A -16 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A -15 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A -14 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A -13 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A -12 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A -11 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER A -10 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER A -9 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLY A -8 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLU A -7 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX ASN A -6 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX LEU A -5 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX TYR A -4 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX PHE A -3 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLN A -2 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLY A -1 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS A 0 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX ALA A 80 UNP Q57WP0 THR 80 CONFLICT
SEQADV 4CJX MET B -20 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLY B -19 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER B -18 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER B -17 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B -16 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B -15 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B -14 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B -13 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B -12 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B -11 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER B -10 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX SER B -9 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLY B -8 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLU B -7 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX ASN B -6 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX LEU B -5 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX TYR B -4 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX PHE B -3 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLN B -2 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX GLY B -1 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX HIS B 0 UNP Q57WP0 EXPRESSION TAG
SEQADV 4CJX ALA B 80 UNP Q57WP0 THR 80 CONFLICT
SEQRES 1 A 319 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 319 GLU ASN LEU TYR PHE GLN GLY HIS MET PRO GLU ALA VAL
SEQRES 3 A 319 VAL ILE ASP GLY ARG ALA VAL ALA LYS ALA ILE GLN LYS
SEQRES 4 A 319 GLU LEU THR GLU GLU VAL ALA LEU LEU GLU ARG ARG TYR
SEQRES 5 A 319 LYS GLY ARG ARG PRO GLY LEU SER THR ILE ILE CYS GLY
SEQRES 6 A 319 LYS ARG LYS ASP SER GLN THR TYR VAL ARG LEU LYS ARG
SEQRES 7 A 319 LYS ALA ALA ALA ALA CYS GLY PHE ARG ASN PHE SER VAL
SEQRES 8 A 319 GLU LEU PRO ALA ASN VAL THR GLN GLU ALA LEU GLU ARG
SEQRES 9 A 319 GLU VAL ILE ARG LEU ASN GLU GLU GLU ALA CYS HIS SER
SEQRES 10 A 319 ILE VAL VAL GLN LEU PRO LEU PRO PRO HIS ILE ASP LYS
SEQRES 11 A 319 VAL ALA ALA LEU SER LYS ILE LYS PRO GLU LYS ASP ALA
SEQRES 12 A 319 ASP CYS LEU LEU PRO VAL ASN VAL GLY GLN LEU HIS ILE
SEQRES 13 A 319 ARG GLU ARG ASN PRO ALA ILE VAL PRO CYS THR ALA SER
SEQRES 14 A 319 ALA VAL MET GLU LEU LEU ARG CYS SER GLY VAL GLU ILE
SEQRES 15 A 319 CYS GLY LYS ARG VAL VAL VAL LEU GLY ARG GLY ASP ILE
SEQRES 16 A 319 ALA GLY LEU PRO VAL ALA THR LEU LEU ALA ASN GLU ASP
SEQRES 17 A 319 ALA THR VAL THR VAL VAL HIS SER ALA THR PRO LEU CYS
SEQRES 18 A 319 ASP ILE ALA ASP ILE VAL ARG ALA SER ASP ILE VAL VAL
SEQRES 19 A 319 SER ALA ALA GLY GLN PRO GLY LEU VAL ARG GLY GLU TRP
SEQRES 20 A 319 ILE LYS LEU GLY ALA ALA VAL ILE ASP VAL GLY THR THR
SEQRES 21 A 319 PRO VAL ALA ASP PRO SER LYS VAL PRO GLY TYR ARG LEU
SEQRES 22 A 319 VAL GLY ASP VAL CYS PHE ASP VAL ALA ARG LYS ARG ALA
SEQRES 23 A 319 ALA TYR ILE THR PRO VAL PRO GLY GLY VAL GLY PRO VAL
SEQRES 24 A 319 THR VAL SER MET LEU LEU LYS ASN THR LEU THR MET PHE
SEQRES 25 A 319 LYS ARG SER VAL ARG ALA LEU
SEQRES 1 B 319 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 319 GLU ASN LEU TYR PHE GLN GLY HIS MET PRO GLU ALA VAL
SEQRES 3 B 319 VAL ILE ASP GLY ARG ALA VAL ALA LYS ALA ILE GLN LYS
SEQRES 4 B 319 GLU LEU THR GLU GLU VAL ALA LEU LEU GLU ARG ARG TYR
SEQRES 5 B 319 LYS GLY ARG ARG PRO GLY LEU SER THR ILE ILE CYS GLY
SEQRES 6 B 319 LYS ARG LYS ASP SER GLN THR TYR VAL ARG LEU LYS ARG
SEQRES 7 B 319 LYS ALA ALA ALA ALA CYS GLY PHE ARG ASN PHE SER VAL
SEQRES 8 B 319 GLU LEU PRO ALA ASN VAL THR GLN GLU ALA LEU GLU ARG
SEQRES 9 B 319 GLU VAL ILE ARG LEU ASN GLU GLU GLU ALA CYS HIS SER
SEQRES 10 B 319 ILE VAL VAL GLN LEU PRO LEU PRO PRO HIS ILE ASP LYS
SEQRES 11 B 319 VAL ALA ALA LEU SER LYS ILE LYS PRO GLU LYS ASP ALA
SEQRES 12 B 319 ASP CYS LEU LEU PRO VAL ASN VAL GLY GLN LEU HIS ILE
SEQRES 13 B 319 ARG GLU ARG ASN PRO ALA ILE VAL PRO CYS THR ALA SER
SEQRES 14 B 319 ALA VAL MET GLU LEU LEU ARG CYS SER GLY VAL GLU ILE
SEQRES 15 B 319 CYS GLY LYS ARG VAL VAL VAL LEU GLY ARG GLY ASP ILE
SEQRES 16 B 319 ALA GLY LEU PRO VAL ALA THR LEU LEU ALA ASN GLU ASP
SEQRES 17 B 319 ALA THR VAL THR VAL VAL HIS SER ALA THR PRO LEU CYS
SEQRES 18 B 319 ASP ILE ALA ASP ILE VAL ARG ALA SER ASP ILE VAL VAL
SEQRES 19 B 319 SER ALA ALA GLY GLN PRO GLY LEU VAL ARG GLY GLU TRP
SEQRES 20 B 319 ILE LYS LEU GLY ALA ALA VAL ILE ASP VAL GLY THR THR
SEQRES 21 B 319 PRO VAL ALA ASP PRO SER LYS VAL PRO GLY TYR ARG LEU
SEQRES 22 B 319 VAL GLY ASP VAL CYS PHE ASP VAL ALA ARG LYS ARG ALA
SEQRES 23 B 319 ALA TYR ILE THR PRO VAL PRO GLY GLY VAL GLY PRO VAL
SEQRES 24 B 319 THR VAL SER MET LEU LEU LYS ASN THR LEU THR MET PHE
SEQRES 25 B 319 LYS ARG SER VAL ARG ALA LEU
HET GOL A1298 6
HET PEG A1299 7
HET 9L9 A1300 31
HET NAP A1301 48
HET 9L9 B1298 31
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 9L9 (2S)-2-[[4-[[2,4-BIS(AZANYL)-6-OXIDANYLIDENE-1H-
HETNAM 2 9L9 PYRIMIDIN-5-
HETNAM 3 9L9 YL]CARBAMOYLAMINO]PHENYL]CARBONYLAMINO]PENTANEDIOIC
HETNAM 4 9L9 ACID
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 GOL C3 H8 O3
FORMUL 4 PEG C4 H10 O3
FORMUL 5 9L9 2(C17 H19 N7 O7)
FORMUL 6 NAP C21 H28 N7 O17 P3
FORMUL 8 HOH *322(H2 O)
HELIX 1 1 ASP A 8 TYR A 31 1 24
HELIX 2 2 ARG A 46 CYS A 63 1 18
HELIX 3 3 THR A 77 GLU A 91 1 15
HELIX 4 4 ASP A 108 SER A 114 1 7
HELIX 5 5 LYS A 117 LYS A 120 5 4
HELIX 6 6 LEU A 126 GLY A 131 1 6
HELIX 7 7 PRO A 144 GLY A 158 1 15
HELIX 8 8 ALA A 175 GLU A 186 1 12
HELIX 9 9 PRO A 198 ALA A 208 1 11
HELIX 10 10 ARG A 223 ILE A 227 5 5
HELIX 11 11 CYS A 257 ARG A 262 1 6
HELIX 12 12 GLY A 274 ALA A 297 1 24
HELIX 13 13 ASP B 8 TYR B 31 1 24
HELIX 14 14 ARG B 46 CYS B 63 1 18
HELIX 15 15 THR B 77 GLU B 90 1 14
HELIX 16 16 ASP B 108 SER B 114 1 7
HELIX 17 17 LYS B 117 LYS B 120 5 4
HELIX 18 18 LEU B 126 GLY B 131 1 6
HELIX 19 19 PRO B 144 GLY B 158 1 15
HELIX 20 20 ALA B 175 GLU B 186 1 12
HELIX 21 21 PRO B 198 ALA B 208 1 11
HELIX 22 22 ARG B 223 ILE B 227 5 5
HELIX 23 23 CYS B 257 ARG B 262 1 6
HELIX 24 24 GLY B 274 ARG B 296 1 23
SHEET 1 AA12 VAL A 5 VAL A 6 0
SHEET 2 AA12 TYR A 267 ILE A 268 1 N ILE A 268 O VAL A 5
SHEET 3 AA12 ALA A 232 ASP A 235 1 N VAL A 233 O TYR A 267
SHEET 4 AA12 ILE A 211 SER A 214 1 O VAL A 212 N ILE A 234
SHEET 5 AA12 ARG A 165 LEU A 169 1 O ARG A 165 N ILE A 211
SHEET 6 AA12 THR A 189 VAL A 193 1 O THR A 189 N VAL A 166
SHEET 7 AA12 THR B 189 VAL B 193 -1 O VAL B 190 N VAL A 192
SHEET 8 AA12 ARG B 165 LEU B 169 1 O VAL B 166 N THR B 191
SHEET 9 AA12 ILE B 211 SER B 214 1 O ILE B 211 N VAL B 167
SHEET 10 AA12 ALA B 232 ASP B 235 1 O ALA B 232 N VAL B 212
SHEET 11 AA12 TYR B 267 ILE B 268 1 O TYR B 267 N VAL B 233
SHEET 12 AA12 VAL B 5 VAL B 6 1 O VAL B 5 N ILE B 268
SHEET 1 AB 3 ARG A 66 LEU A 72 0
SHEET 2 AB 3 GLY A 37 CYS A 43 1 O LEU A 38 N PHE A 68
SHEET 3 AB 3 SER A 96 VAL A 99 1 O SER A 96 N SER A 39
SHEET 1 AC 2 THR A 239 ALA A 242 0
SHEET 2 AC 2 TYR A 250 VAL A 253 -1 O ARG A 251 N VAL A 241
SHEET 1 BA 3 ARG B 66 LEU B 72 0
SHEET 2 BA 3 GLY B 37 CYS B 43 1 O LEU B 38 N PHE B 68
SHEET 3 BA 3 SER B 96 VAL B 99 1 O SER B 96 N SER B 39
SHEET 1 BB 2 THR B 239 ALA B 242 0
SHEET 2 BB 2 TYR B 250 VAL B 253 -1 O ARG B 251 N VAL B 241
CISPEP 1 LEU A 101 PRO A 102 0 2.80
CISPEP 2 VAL A 271 PRO A 272 0 -0.60
CISPEP 3 LEU B 101 PRO B 102 0 3.77
CISPEP 4 VAL B 271 PRO B 272 0 -1.22
SITE 1 AC1 4 ASP A 259 HOH A2171 LYS B 246 ARG B 251
SITE 1 AC2 7 VAL A 110 SER A 114 LEU A 125 ASP A 173
SITE 2 AC2 7 HOH A2177 HIS B 134 ILE B 135
SITE 1 AC3 19 TYR A 52 LEU A 55 LYS A 56 VAL A 99
SITE 2 AC3 19 GLN A 100 LEU A 101 ASP A 123 ILE A 174
SITE 3 AC3 19 PRO A 272 GLY A 273 GLY A 276 PRO A 277
SITE 4 AC3 19 NAP A1301 HOH A2042 HOH A2046 HOH A2102
SITE 5 AC3 19 HOH A2173 HOH A2178 HOH A2179
SITE 1 AC4 21 ARG B 10 TYR B 52 LEU B 55 LYS B 56
SITE 2 AC4 21 VAL B 99 GLN B 100 LEU B 101 ASP B 123
SITE 3 AC4 21 ILE B 174 LEU B 252 PRO B 272 GLY B 273
SITE 4 AC4 21 GLY B 276 PRO B 277 HOH B2031 HOH B2068
SITE 5 AC4 21 HOH B2069 HOH B2137 HOH B2139 HOH B2140
SITE 6 AC4 21 HOH B2141
SITE 1 AC5 22 ASP A 48 TYR A 52 PRO A 102 GLY A 170
SITE 2 AC5 22 ARG A 171 GLY A 172 ILE A 174 ALA A 175
SITE 3 AC5 22 HIS A 194 SER A 195 ALA A 215 ALA A 216
SITE 4 AC5 22 GLY A 217 GLN A 218 VAL A 236 GLY A 237
SITE 5 AC5 22 THR A 238 9L9 A1300 HOH A2040 HOH A2142
SITE 6 AC5 22 HOH A2180 ARG B 30
CRYST1 58.220 77.325 128.908 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 0.017176 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007757 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
