HEADER HYDROLASE 28-FEB-17 5NAT
TITLE COMPLEMENT FACTOR D IN COMPLEX WITH THE INHIBITOR (S)-PYRROLIDINE-1,2-
TITLE 2 DICARBOXYLIC ACID 1-[(1-METHYL-1H-INDOL-3-YL)-AMIDE] 2-[(3-
TITLE 3 TRIFLUOROMETHOXY-PHENYL)-AMIDE]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT FACTOR D;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADIPSIN,C3 CONVERTASE ACTIVATOR,PROPERDIN FACTOR D;
COMPND 5 EC: 3.4.21.46
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MAC SWEENEY,N.OSTERMANN
REVDAT 2 02-OCT-19 5NAT 1 JRNL
REVDAT 1 21-MAR-18 5NAT 0
JRNL AUTH E.LORTHIOIS,K.ANDERSON,A.VULPETTI,O.ROGEL,F.CUMIN,
JRNL AUTH 2 N.OSTERMANN,S.STEINBACHER,A.MAC SWEENEY,O.DELGADO,S.M.LIAO,
JRNL AUTH 3 S.RANDL,S.RUDISSER,S.DUSSAUGE,K.FETTIS,L.KIEFFER,
JRNL AUTH 4 A.DE ERKENEZ,L.YANG,C.HARTWIEG,U.A.ARGIKAR,L.R.LA BONTE,
JRNL AUTH 5 R.NEWTON,V.KANSARA,S.FLOHR,U.HOMMEL,B.JAFFEE,J.MAIBAUM
JRNL TITL DISCOVERY OF HIGHLY POTENT AND SELECTIVE SMALL-MOLECULE
JRNL TITL 2 REVERSIBLE FACTOR D INHIBITORS DEMONSTRATING ALTERNATIVE
JRNL TITL 3 COMPLEMENT PATHWAY INHIBITION IN VIVO.
JRNL REF J.MED.CHEM. V. 60 5717 2017
JRNL REFN ISSN 0022-2623
JRNL PMID 28621538
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00425
REMARK 2
REMARK 2 RESOLUTION. 1.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0063
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 61837
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1711
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 261
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
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): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64856
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.170
REMARK 200 RESOLUTION RANGE LOW (A) : 53.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.190
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.88
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MM NACL + 1 UL RESERVOIR SOLUTION,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 24.83800
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
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 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 SER A 244
REMARK 465 ALA A 245
REMARK 465 ALA A 246
REMARK 465 ALA A 247
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 ARG A 20 CZ NH1 NH2
REMARK 480 ASP A 61 CG OD1 OD2
REMARK 480 ARG A 170A CD NE CZ NH1 NH2
REMARK 480 LYS A 192 CE NZ
REMARK 480 LYS A 223A CG CD CE NZ
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 ARG A 20 NE ARG A 20 CZ 0.120
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 ARG A 20 CD - NE - CZ ANGL. DEV. = -11.0 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.9 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 ALA A 61B -127.87 50.04
REMARK 500 HIS A 171 -108.91 -102.33
REMARK 500 ARG A 187 -44.10 73.20
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 A 20 0.11 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 A 661 DISTANCE = 6.37 ANGSTROMS
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8RT A 303
DBREF 5NAT A 16 243 UNP P00746 CFAD_HUMAN 26 253
SEQADV 5NAT SER A 244 UNP P00746 EXPRESSION TAG
SEQADV 5NAT ALA A 245 UNP P00746 EXPRESSION TAG
SEQADV 5NAT ALA A 246 UNP P00746 EXPRESSION TAG
SEQADV 5NAT ALA A 247 UNP P00746 EXPRESSION TAG
SEQRES 1 A 232 ILE LEU GLY GLY ARG GLU ALA GLU ALA HIS ALA ARG PRO
SEQRES 2 A 232 TYR MET ALA SER VAL GLN LEU ASN GLY ALA HIS LEU CYS
SEQRES 3 A 232 GLY GLY VAL LEU VAL ALA GLU GLN TRP VAL LEU SER ALA
SEQRES 4 A 232 ALA HIS CYS LEU GLU ASP ALA ALA ASP GLY LYS VAL GLN
SEQRES 5 A 232 VAL LEU LEU GLY ALA HIS SER LEU SER GLN PRO GLU PRO
SEQRES 6 A 232 SER LYS ARG LEU TYR ASP VAL LEU ARG ALA VAL PRO HIS
SEQRES 7 A 232 PRO ASP SER GLN PRO ASP THR ILE ASP HIS ASP LEU LEU
SEQRES 8 A 232 LEU LEU GLN LEU SER GLU LYS ALA THR LEU GLY PRO ALA
SEQRES 9 A 232 VAL ARG PRO LEU PRO TRP GLN ARG VAL ASP ARG ASP VAL
SEQRES 10 A 232 ALA PRO GLY THR LEU CYS ASP VAL ALA GLY TRP GLY ILE
SEQRES 11 A 232 VAL ASN HIS ALA GLY ARG ARG PRO ASP SER LEU GLN HIS
SEQRES 12 A 232 VAL LEU LEU PRO VAL LEU ASP ARG ALA THR CYS ASN ARG
SEQRES 13 A 232 ARG THR HIS HIS ASP GLY ALA ILE THR GLU ARG LEU MET
SEQRES 14 A 232 CYS ALA GLU SER ASN ARG ARG ASP SER CYS LYS GLY ASP
SEQRES 15 A 232 SER GLY GLY PRO LEU VAL CYS GLY GLY VAL LEU GLU GLY
SEQRES 16 A 232 VAL VAL THR SER GLY SER ARG VAL CYS GLY ASN ARG LYS
SEQRES 17 A 232 LYS PRO GLY ILE TYR THR ARG VAL ALA SER TYR ALA ALA
SEQRES 18 A 232 TRP ILE ASP SER VAL LEU ALA SER ALA ALA ALA
HET GOL A 301 6
HET GOL A 302 6
HET 8RT A 303 32
HETNAM GOL GLYCEROL
HETNAM 8RT (2~{S})-~{N}1-(1-METHYLINDOL-3-YL)-~{N}2-[3-
HETNAM 2 8RT (TRIFLUOROMETHYLOXY)PHENYL]PYRROLIDINE-1,2-
HETNAM 3 8RT DICARBOXAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 8RT C22 H21 F3 N4 O3
FORMUL 5 HOH *261(H2 O)
HELIX 1 AA1 ALA A 55 GLU A 60 5 6
HELIX 2 AA2 ASP A 164 ASN A 169 1 6
HELIX 3 AA3 TYR A 234 ALA A 243 1 10
SHEET 1 AA1 8 ARG A 20 GLU A 21 0
SHEET 2 AA1 8 GLN A 156 LEU A 163 -1 O HIS A 157 N ARG A 20
SHEET 3 AA1 8 LEU A 180 ALA A 183 -1 O CYS A 182 N LEU A 163
SHEET 4 AA1 8 GLY A 226 ARG A 230 -1 O TYR A 228 N MET A 181
SHEET 5 AA1 8 VAL A 208 VAL A 213 -1 N VAL A 212 O THR A 229
SHEET 6 AA1 8 PRO A 198 CYS A 201 -1 N LEU A 199 O GLU A 210
SHEET 7 AA1 8 LEU A 135 GLY A 140 -1 N ASP A 137 O VAL A 200
SHEET 8 AA1 8 GLN A 156 LEU A 163 -1 O LEU A 160 N CYS A 136
SHEET 1 AA2 7 MET A 30 LEU A 35 0
SHEET 2 AA2 7 ALA A 39 ALA A 48 -1 O CYS A 42 N VAL A 33
SHEET 3 AA2 7 TRP A 51 SER A 54 -1 O LEU A 53 N VAL A 45
SHEET 4 AA2 7 LEU A 104 LEU A 108 -1 O LEU A 106 N VAL A 52
SHEET 5 AA2 7 ARG A 81 PRO A 90 -1 N VAL A 89 O LEU A 105
SHEET 6 AA2 7 VAL A 64 LEU A 68 -1 N VAL A 66 O TYR A 83
SHEET 7 AA2 7 MET A 30 LEU A 35 -1 N GLN A 34 O GLN A 65
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.05
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.05
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.04
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.02
SITE 1 AC1 9 ASP A 129A VAL A 130 VAL A 162 LEU A 163
SITE 2 AC1 9 ASP A 164 ARG A 165 MET A 181 CYS A 182
SITE 3 AC1 9 HOH A 489
SITE 1 AC2 6 LEU A 135 VAL A 200 CYS A 201 GLY A 202
SITE 2 AC2 6 GLY A 207 HOH A 441
SITE 1 AC3 19 HIS A 40 LEU A 41 CYS A 42 HIS A 57
SITE 2 AC3 19 CYS A 58 TRP A 141 GLY A 142 ILE A 143
SITE 3 AC3 19 ARG A 151 CYS A 191 LYS A 192 GLY A 193
SITE 4 AC3 19 SER A 195 SER A 215 GLY A 216 SER A 217
SITE 5 AC3 19 ARG A 218 HOH A 498 HOH A 526
CRYST1 39.438 49.676 55.562 90.00 106.02 90.00 P 1 21 1 2
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 0.025356 0.000000 0.007278 0.00000
SCALE2 0.000000 0.020130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018725 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
