HEADER OXIDOREDUCTASE 04-SEP-08 3EEL
TITLE CANDIDA GLABRATA DIHYDROFOLATE REDUCTASE COMPLEXED WITH 2,4-DIAMINO-5-
TITLE 2 [3-METHYL-3-(3-METHOXY-5-(3,5-DIMETHYLPHENYL)PHENYL)PROP-1-YNYL]-6-
TITLE 3 METHYLPYRIMIDINE(UCP11153TM) AND NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA GLABRATA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5478;
SOURCE 5 GENE: CAGL0J03894G;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENZYME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LIU,A.ANDERSON
REVDAT 4 21-FEB-24 3EEL 1 REMARK SEQADV
REVDAT 3 25-OCT-17 3EEL 1 REMARK
REVDAT 2 20-NOV-13 3EEL 1 FORMUL HET HETATM HETNAM
REVDAT 2 2 1 HETSYN VERSN
REVDAT 1 18-AUG-09 3EEL 0
JRNL AUTH J.LIU,D.B.BOLSTAD,A.E.SMITH,N.D.PRIESTLEY,D.L.WRIGHT,
JRNL AUTH 2 A.C.ANDERSON
JRNL TITL PROBING THE ACTIVE SITE OF CANDIDA GLABRATA DIHYDROFOLATE
JRNL TITL 2 REDUCTASE WITH HIGH RESOLUTION CRYSTAL STRUCTURES AND THE
JRNL TITL 3 SYNTHESIS OF NEW INHIBITORS
JRNL REF CHEM.BIOL.DRUG DES. V. 73 62 2009
JRNL REFN ISSN 1747-0277
JRNL PMID 19152636
JRNL DOI 10.1111/J.1747-0285.2008.00745.X
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 28869
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1456
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1298
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3688
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 154
REMARK 3 SOLVENT ATOMS : 262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.189
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.199
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3796 ; 0.032 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5157 ; 2.839 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 446 ;22.405 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 165 ;40.358 ;23.939
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 619 ;20.649 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.889 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 557 ; 0.243 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2846 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1781 ; 0.329 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2342 ; 0.320 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 113 ; 0.169 ; 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): 100 ; 0.429 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.035 ; 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): 2366 ; 1.479 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3590 ; 2.156 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1785 ; 3.446 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1567 ; 4.543 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 6
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 153 A 154 3
REMARK 3 1 B 153 B 154 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 8 ; 0.070 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 8 ; 0.140 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 8 ; 0.180 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 8 ; 0.580 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
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 161 A 164 3
REMARK 3 1 B 161 B 164 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 16 ; 0.060 ; 0.050
REMARK 3 LOOSE POSITIONAL 2 A (A): 19 ; 0.360 ; 5.000
REMARK 3 TIGHT THERMAL 2 A (A**2): 16 ; 0.130 ; 0.500
REMARK 3 LOOSE THERMAL 2 A (A**2): 19 ; 0.560 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 105 B 106 3
REMARK 3 1 A 105 A 106 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 B (A): 8 ; 0.080 ; 0.050
REMARK 3 LOOSE POSITIONAL 3 B (A): 9 ; 0.530 ; 5.000
REMARK 3 TIGHT THERMAL 3 B (A**2): 8 ; 0.050 ; 0.500
REMARK 3 LOOSE THERMAL 3 B (A**2): 9 ; 1.240 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 111 B 112 3
REMARK 3 1 A 111 A 112 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 B (A): 8 ; 0.080 ; 0.050
REMARK 3 LOOSE POSITIONAL 4 B (A): 9 ; 0.650 ; 5.000
REMARK 3 TIGHT THERMAL 4 B (A**2): 8 ; 0.280 ; 0.500
REMARK 3 LOOSE THERMAL 4 B (A**2): 9 ; 1.450 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 148 B 149 3
REMARK 3 1 A 148 A 149 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 B (A): 8 ; 0.090 ; 0.050
REMARK 3 LOOSE POSITIONAL 5 B (A): 6 ; 0.100 ; 5.000
REMARK 3 TIGHT THERMAL 5 B (A**2): 8 ; 0.120 ; 0.500
REMARK 3 LOOSE THERMAL 5 B (A**2): 6 ; 0.460 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 46 B 47 3
REMARK 3 1 A 46 A 47 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 B (A): 8 ; 0.100 ; 0.050
REMARK 3 LOOSE POSITIONAL 6 B (A): 6 ; 0.720 ; 5.000
REMARK 3 TIGHT THERMAL 6 B (A**2): 8 ; 0.160 ; 0.500
REMARK 3 LOOSE THERMAL 6 B (A**2): 6 ; 1.450 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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
REMARK 4
REMARK 4 3EEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28869
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 42.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, MGCL2, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.49200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.74600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 173.23800
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SER A 2
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 3 CG CD CE NZ
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 SD MET A 33 O HOH A 243 2.01
REMARK 500 SD MET B 33 O HOH B 344 2.02
REMARK 500 CB ILE A 115 O HOH A 351 2.16
REMARK 500 CE1 HIS A 224 O HOH A 308 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 271 O HOH B 347 4564 1.83
REMARK 500 OE1 GLU A 191 O HOH B 311 4654 2.03
REMARK 500 OE2 GLU B 219 O HOH A 339 1655 2.14
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 CYS B 101 CB CYS B 101 SG -0.160
REMARK 500 GLY B 185 C GLY B 185 O 0.110
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 GLU A 116 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 SER B 47 N - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 GLU B 84 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 CYS B 101 CB - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU B 102 N - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 GLN B 106 N - CA - C ANGL. DEV. = 18.8 DEGREES
REMARK 500 GLY B 185 O - C - N ANGL. DEV. = -14.8 DEGREES
REMARK 500 ARG B 186 C - N - CA ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG B 186 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 LEU B 187 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 THR B 188 N - CA - CB ANGL. DEV. = 14.1 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 LEU A 85 100.16 -172.27
REMARK 500 ASP A 154 -10.49 -149.09
REMARK 500 LEU A 162 -67.77 -23.09
REMARK 500 LYS A 205 -126.84 50.50
REMARK 500 ASN B 46 -19.15 -41.08
REMARK 500 LEU B 85 99.77 -169.03
REMARK 500 SER B 97 108.00 -161.85
REMARK 500 ASN B 113 40.77 37.39
REMARK 500 THR B 149 109.49 -29.19
REMARK 500 ARG B 186 -156.75 -148.71
REMARK 500 THR B 188 121.26 -174.63
REMARK 500 LYS B 205 -131.76 51.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 83 GLU A 84 -112.90
REMARK 500 ILE A 115 GLU A 116 142.17
REMARK 500 MET A 153 ASP A 154 -149.81
REMARK 500 GLU A 161 LEU A 162 143.83
REMARK 500 GLU A 163 GLN A 164 139.25
REMARK 500 LEU A 187 THR A 188 -140.04
REMARK 500 PRO A 201 VAL A 202 136.67
REMARK 500 HIS A 223 HIS A 224 139.62
REMARK 500 ASN B 46 SER B 47 -126.63
REMARK 500 PHE B 81 ASP B 82 -119.63
REMARK 500 GLY B 83 GLU B 84 -105.15
REMARK 500 LEU B 98 ARG B 99 -141.97
REMARK 500 CYS B 101 LEU B 102 -136.25
REMARK 500 LEU B 105 GLN B 106 147.43
REMARK 500 ASN B 111 GLU B 112 145.76
REMARK 500 ILE B 115 GLU B 116 146.53
REMARK 500 THR B 148 THR B 149 136.95
REMARK 500 GLY B 185 ARG B 186 98.27
REMARK 500 ARG B 186 LEU B 187 -113.77
REMARK 500 LEU B 187 THR B 188 -119.78
REMARK 500 ASN B 193 GLY B 194 -61.29
REMARK 500 VAL B 197 LYS B 198 -140.57
REMARK 500 GLY B 199 LEU B 200 -128.46
REMARK 500 LEU B 200 PRO B 201 -140.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY B 185 -12.18
REMARK 500 LEU B 200 11.75
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 NDP A 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 53T A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 53T B 229
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EEJ RELATED DB: PDB
REMARK 900 RELATED ID: 3EEK RELATED DB: PDB
REMARK 900 RELATED ID: 3EEM RELATED DB: PDB
DBREF 3EEL A 1 217 UNP Q6FPH0 Q6FPH0_CANGA 1 217
DBREF 3EEL B 1 217 UNP Q6FPH0 Q6FPH0_CANGA 1 217
SEQADV 3EEL LEU A 218 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL GLU A 219 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 220 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 221 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 222 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 223 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 224 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 225 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 226 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS A 227 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL LEU B 218 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL GLU B 219 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 220 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 221 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 222 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 223 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 224 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 225 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 226 UNP Q6FPH0 EXPRESSION TAG
SEQADV 3EEL HIS B 227 UNP Q6FPH0 EXPRESSION TAG
SEQRES 1 A 227 MET SER LYS VAL PRO VAL VAL GLY ILE VAL ALA ALA LEU
SEQRES 2 A 227 LEU PRO GLU MET GLY ILE GLY PHE GLN GLY ASN LEU PRO
SEQRES 3 A 227 TRP ARG LEU ALA LYS GLU MET LYS TYR PHE ARG GLU VAL
SEQRES 4 A 227 THR THR LEU THR ASN ASP ASN SER LYS GLN ASN VAL VAL
SEQRES 5 A 227 ILE MET GLY ARG LYS THR TRP GLU SER ILE PRO GLN LYS
SEQRES 6 A 227 PHE ARG PRO LEU PRO LYS ARG ILE ASN VAL VAL VAL SER
SEQRES 7 A 227 ARG SER PHE ASP GLY GLU LEU ARG LYS VAL GLU ASP GLY
SEQRES 8 A 227 ILE TYR HIS SER ASN SER LEU ARG ASN CYS LEU THR ALA
SEQRES 9 A 227 LEU GLN SER SER LEU ALA ASN GLU ASN LYS ILE GLU ARG
SEQRES 10 A 227 ILE TYR ILE ILE GLY GLY GLY GLU ILE TYR ARG GLN SER
SEQRES 11 A 227 MET ASP LEU ALA ASP HIS TRP LEU ILE THR LYS ILE MET
SEQRES 12 A 227 PRO LEU PRO GLU THR THR ILE PRO GLN MET ASP THR PHE
SEQRES 13 A 227 LEU GLN LYS GLN GLU LEU GLU GLN ARG PHE TYR ASP ASN
SEQRES 14 A 227 SER ASP LYS LEU VAL ASP PHE LEU PRO SER SER ILE GLN
SEQRES 15 A 227 LEU GLU GLY ARG LEU THR SER GLN GLU TRP ASN GLY GLU
SEQRES 16 A 227 LEU VAL LYS GLY LEU PRO VAL GLN GLU LYS GLY TYR GLN
SEQRES 17 A 227 PHE TYR PHE THR LEU TYR THR LYS LYS LEU GLU HIS HIS
SEQRES 18 A 227 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 227 MET SER LYS VAL PRO VAL VAL GLY ILE VAL ALA ALA LEU
SEQRES 2 B 227 LEU PRO GLU MET GLY ILE GLY PHE GLN GLY ASN LEU PRO
SEQRES 3 B 227 TRP ARG LEU ALA LYS GLU MET LYS TYR PHE ARG GLU VAL
SEQRES 4 B 227 THR THR LEU THR ASN ASP ASN SER LYS GLN ASN VAL VAL
SEQRES 5 B 227 ILE MET GLY ARG LYS THR TRP GLU SER ILE PRO GLN LYS
SEQRES 6 B 227 PHE ARG PRO LEU PRO LYS ARG ILE ASN VAL VAL VAL SER
SEQRES 7 B 227 ARG SER PHE ASP GLY GLU LEU ARG LYS VAL GLU ASP GLY
SEQRES 8 B 227 ILE TYR HIS SER ASN SER LEU ARG ASN CYS LEU THR ALA
SEQRES 9 B 227 LEU GLN SER SER LEU ALA ASN GLU ASN LYS ILE GLU ARG
SEQRES 10 B 227 ILE TYR ILE ILE GLY GLY GLY GLU ILE TYR ARG GLN SER
SEQRES 11 B 227 MET ASP LEU ALA ASP HIS TRP LEU ILE THR LYS ILE MET
SEQRES 12 B 227 PRO LEU PRO GLU THR THR ILE PRO GLN MET ASP THR PHE
SEQRES 13 B 227 LEU GLN LYS GLN GLU LEU GLU GLN ARG PHE TYR ASP ASN
SEQRES 14 B 227 SER ASP LYS LEU VAL ASP PHE LEU PRO SER SER ILE GLN
SEQRES 15 B 227 LEU GLU GLY ARG LEU THR SER GLN GLU TRP ASN GLY GLU
SEQRES 16 B 227 LEU VAL LYS GLY LEU PRO VAL GLN GLU LYS GLY TYR GLN
SEQRES 17 B 227 PHE TYR PHE THR LEU TYR THR LYS LYS LEU GLU HIS HIS
SEQRES 18 B 227 HIS HIS HIS HIS HIS HIS
HET NDP A 228 48
HET 53T A 229 29
HET NDP B 228 48
HET 53T B 229 29
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM 53T 5-[(3R)-3-(5-METHOXY-3',5'-DIMETHYLBIPHENYL-3-YL)BUT-1-
HETNAM 2 53T YN-1-YL]-6-METHYLPYRIMIDINE-2,4-DIAMINE
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 53T 2(C24 H26 N4 O)
FORMUL 7 HOH *262(H2 O)
HELIX 1 1 LEU A 29 LEU A 42 1 14
HELIX 2 2 ARG A 56 ILE A 62 1 7
HELIX 3 3 PRO A 63 ARG A 67 5 5
HELIX 4 4 SER A 97 SER A 107 1 11
HELIX 5 5 SER A 107 GLU A 112 1 6
HELIX 6 6 GLY A 123 GLN A 129 1 7
HELIX 7 7 GLN A 158 ARG A 165 1 8
HELIX 8 8 LYS A 172 LEU A 177 1 6
HELIX 9 9 LEU B 29 LEU B 42 1 14
HELIX 10 10 ARG B 56 ILE B 62 1 7
HELIX 11 11 PRO B 63 ARG B 67 5 5
HELIX 12 12 SER B 97 GLN B 106 1 10
HELIX 13 13 SER B 107 GLU B 112 1 6
HELIX 14 14 GLY B 123 GLN B 129 1 7
HELIX 15 15 GLN B 158 ARG B 165 1 8
HELIX 16 16 LYS B 172 LEU B 177 1 6
SHEET 1 A 9 ARG A 86 GLU A 89 0
SHEET 2 A 9 ILE A 92 SER A 95 -1 O HIS A 94 N ARG A 86
SHEET 3 A 9 ILE A 73 VAL A 77 1 N VAL A 76 O TYR A 93
SHEET 4 A 9 GLN A 49 GLY A 55 1 N VAL A 52 O ILE A 73
SHEET 5 A 9 ILE A 115 ILE A 120 1 O TYR A 119 N ILE A 53
SHEET 6 A 9 VAL A 6 LEU A 13 1 N VAL A 7 O ILE A 118
SHEET 7 A 9 HIS A 136 PRO A 144 1 O LEU A 138 N GLY A 8
SHEET 8 A 9 TYR A 207 LYS A 216 -1 O GLN A 208 N MET A 143
SHEET 9 A 9 PHE A 166 ASP A 168 -1 N TYR A 167 O THR A 215
SHEET 1 B10 ARG A 86 GLU A 89 0
SHEET 2 B10 ILE A 92 SER A 95 -1 O HIS A 94 N ARG A 86
SHEET 3 B10 ILE A 73 VAL A 77 1 N VAL A 76 O TYR A 93
SHEET 4 B10 GLN A 49 GLY A 55 1 N VAL A 52 O ILE A 73
SHEET 5 B10 ILE A 115 ILE A 120 1 O TYR A 119 N ILE A 53
SHEET 6 B10 VAL A 6 LEU A 13 1 N VAL A 7 O ILE A 118
SHEET 7 B10 HIS A 136 PRO A 144 1 O LEU A 138 N GLY A 8
SHEET 8 B10 TYR A 207 LYS A 216 -1 O GLN A 208 N MET A 143
SHEET 9 B10 GLU A 195 GLU A 204 -1 N VAL A 202 O PHE A 209
SHEET 10 B10 THR A 188 TRP A 192 -1 N GLN A 190 O VAL A 197
SHEET 1 C 2 GLY A 18 GLY A 20 0
SHEET 2 C 2 THR A 155 PHE A 156 -1 O THR A 155 N ILE A 19
SHEET 1 D 9 ARG B 86 GLU B 89 0
SHEET 2 D 9 ILE B 92 SER B 95 -1 O HIS B 94 N ARG B 86
SHEET 3 D 9 ILE B 73 VAL B 77 1 N ASN B 74 O TYR B 93
SHEET 4 D 9 GLN B 49 GLY B 55 1 N VAL B 52 O ILE B 73
SHEET 5 D 9 ILE B 115 ILE B 120 1 O TYR B 119 N VAL B 51
SHEET 6 D 9 VAL B 6 LEU B 13 1 N ILE B 9 O ILE B 120
SHEET 7 D 9 HIS B 136 PRO B 144 1 O LEU B 138 N GLY B 8
SHEET 8 D 9 TYR B 207 LYS B 216 -1 O TYR B 214 N TRP B 137
SHEET 9 D 9 PHE B 166 ASP B 168 -1 N TYR B 167 O THR B 215
SHEET 1 E10 ARG B 86 GLU B 89 0
SHEET 2 E10 ILE B 92 SER B 95 -1 O HIS B 94 N ARG B 86
SHEET 3 E10 ILE B 73 VAL B 77 1 N ASN B 74 O TYR B 93
SHEET 4 E10 GLN B 49 GLY B 55 1 N VAL B 52 O ILE B 73
SHEET 5 E10 ILE B 115 ILE B 120 1 O TYR B 119 N VAL B 51
SHEET 6 E10 VAL B 6 LEU B 13 1 N ILE B 9 O ILE B 120
SHEET 7 E10 HIS B 136 PRO B 144 1 O LEU B 138 N GLY B 8
SHEET 8 E10 TYR B 207 LYS B 216 -1 O TYR B 214 N TRP B 137
SHEET 9 E10 GLU B 195 GLU B 204 -1 N VAL B 202 O PHE B 209
SHEET 10 E10 THR B 188 TRP B 192 -1 N GLN B 190 O VAL B 197
SHEET 1 F 2 GLY B 18 GLY B 20 0
SHEET 2 F 2 THR B 155 PHE B 156 -1 O THR B 155 N ILE B 19
CISPEP 1 LEU A 14 PRO A 15 0 -3.32
CISPEP 2 ARG A 67 PRO A 68 0 0.04
CISPEP 3 GLY A 122 GLY A 123 0 6.30
CISPEP 4 LEU B 14 PRO B 15 0 -1.31
CISPEP 5 ARG B 67 PRO B 68 0 -2.68
CISPEP 6 GLY B 122 GLY B 123 0 4.71
SITE 1 AC1 30 VAL A 10 ALA A 11 ILE A 19 GLY A 20
SITE 2 AC1 30 PHE A 21 GLY A 23 ASN A 24 LEU A 25
SITE 3 AC1 30 GLY A 55 ARG A 56 LYS A 57 THR A 58
SITE 4 AC1 30 VAL A 77 SER A 78 ARG A 79 ASN A 96
SITE 5 AC1 30 SER A 97 LEU A 98 ILE A 121 GLY A 123
SITE 6 AC1 30 GLY A 124 GLU A 125 ILE A 126 TYR A 127
SITE 7 AC1 30 GLN A 129 53T A 229 HOH A 244 HOH A 263
SITE 8 AC1 30 HOH A 313 HOH A 334
SITE 1 AC2 16 ILE A 9 VAL A 10 GLY A 23 GLU A 32
SITE 2 AC2 16 MET A 33 PHE A 36 THR A 58 SER A 61
SITE 3 AC2 16 PRO A 63 PHE A 66 ILE A 121 TYR A 127
SITE 4 AC2 16 THR A 140 NDP A 228 HOH A 278 GLU B 184
SITE 1 AC3 30 VAL B 10 ALA B 11 ILE B 19 GLY B 20
SITE 2 AC3 30 PHE B 21 GLY B 23 ASN B 24 LEU B 25
SITE 3 AC3 30 GLY B 55 ARG B 56 LYS B 57 THR B 58
SITE 4 AC3 30 VAL B 77 SER B 78 ARG B 79 ASN B 96
SITE 5 AC3 30 SER B 97 LEU B 98 ILE B 121 GLY B 123
SITE 6 AC3 30 GLY B 124 GLU B 125 ILE B 126 TYR B 127
SITE 7 AC3 30 GLN B 129 53T B 229 HOH B 238 HOH B 272
SITE 8 AC3 30 HOH B 320 HOH B 324
SITE 1 AC4 17 ILE B 9 VAL B 10 ALA B 11 GLY B 23
SITE 2 AC4 17 ARG B 28 GLU B 32 MET B 33 PHE B 36
SITE 3 AC4 17 THR B 58 SER B 61 PRO B 63 PHE B 66
SITE 4 AC4 17 ILE B 121 TYR B 127 THR B 140 NDP B 228
SITE 5 AC4 17 HOH B 262
CRYST1 42.830 42.830 230.984 90.00 90.00 90.00 P 41 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 0.023348 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004329 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
