HEADER HYDROLASE 15-DEC-15 5FCK
TITLE COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5
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;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CFD, DF, PFD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MAC SWEENEY
REVDAT 4 10-JAN-24 5FCK 1 REMARK
REVDAT 3 23-NOV-16 5FCK 1 JRNL
REVDAT 2 02-NOV-16 5FCK 1 JRNL
REVDAT 1 26-OCT-16 5FCK 0
JRNL AUTH J.MAIBAUM,S.M.LIAO,A.VULPETTI,N.OSTERMANN,S.RANDL,
JRNL AUTH 2 S.RUDISSER,E.LORTHIOIS,P.ERBEL,B.KINZEL,F.A.KOLB,S.BARBIERI,
JRNL AUTH 3 J.WAGNER,C.DURAND,K.FETTIS,S.DUSSAUGE,N.HUGHES,O.DELGADO,
JRNL AUTH 4 U.HOMMEL,T.GOULD,A.MAC SWEENEY,B.GERHARTZ,F.CUMIN,S.FLOHR,
JRNL AUTH 5 A.SCHUBART,B.JAFFEE,R.HARRISON,A.M.RISITANO,J.EDER,
JRNL AUTH 6 K.ANDERSON
JRNL TITL SMALL-MOLECULE FACTOR D INHIBITORS TARGETING THE ALTERNATIVE
JRNL TITL 2 COMPLEMENT PATHWAY.
JRNL REF NAT.CHEM.BIOL. V. 12 1105 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 27775713
JRNL DOI 10.1038/NCHEMBIO.2208
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 13764
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 725
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 554
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 49.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 29
REMARK 3 BIN FREE R VALUE : 0.2230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1684
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.761
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1786 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1681 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2444 ; 1.914 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3861 ; 0.890 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 231 ; 6.735 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 72 ;31.280 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 277 ;15.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;23.378 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 276 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2026 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 391 ; 0.001 ; 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): 906 ; 1.521 ; 1.628
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 905 ; 1.510 ; 1.626
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1131 ; 2.203 ; 2.430
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1132 ; 2.205 ; 2.433
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 880 ; 2.127 ; 1.916
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 838 ; 2.076 ; 1.935
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1247 ; 3.303 ; 2.787
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2075 ; 4.471 ;13.418
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1989 ; 4.506 ;13.326
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 : 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 5FCK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14490
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 22.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.19400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5FBE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL FD SOLUTION (18 MG/ML FD, 10 MM
REMARK 280 TRIS PH 7.0, 100 MM NACL) WAS MIXED WITH 1 UL RESERVOIR SOLUTION
REMARK 280 (25% PEG3350, 100 MM TRIS PH 8.0) AND EQUILIBRATED AGAINST 1 ML
REMARK 280 RESERVOIR SOLUTION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 24.37100
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: 120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 GLU A 59A
REMARK 465 ASP A 59B
REMARK 465 ALA A 59C
REMARK 465 ALA A 59D
REMARK 465 ALA A 245
REMARK 465 ALA A 246
REMARK 465 ALA A 247
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 ARG A 187 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 O HOH A 413 O HOH A 432 1455 1.17
REMARK 500 O HOH A 401 O HOH A 463 2545 1.18
REMARK 500 O HOH A 408 O HOH A 468 2545 1.36
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 27 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 VAL A 138 CG1 - CB - CG2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 VAL A 219 CB - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = -3.4 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 54 -151.46 -151.93
REMARK 500 HIS A 171 -112.27 -113.30
REMARK 500 ARG A 187 -35.72 70.23
REMARK 500 PRO A 225 152.54 -49.61
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 5WC A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
DBREF 5FCK A 16 243 UNP P00746 CFAD_HUMAN 26 253
SEQADV 5FCK SER A 244 UNP P00746 EXPRESSION TAG
SEQADV 5FCK ALA A 245 UNP P00746 EXPRESSION TAG
SEQADV 5FCK ALA A 246 UNP P00746 EXPRESSION TAG
SEQADV 5FCK 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 5WC A 301 34
HET SO4 A 302 5
HETNAM 5WC 1-[2-[(1~{R},3~{S},5~{R})-3-[[(1~{R})-1-(3-CHLORANYL-2-
HETNAM 2 5WC FLUORANYL-PHENYL)ETHYL]CARBAMOYL]-2-
HETNAM 3 5WC AZABICYCLO[3.1.0]HEXAN-2-YL]-2-OXIDANYLIDENE-
HETNAM 4 5WC ETHYL]PYRAZOLO[3,4-C]PYRIDINE-3-CARBOXAMIDE
HETNAM SO4 SULFATE ION
FORMUL 2 5WC C23 H22 CL F N6 O3
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *89(H2 O)
HELIX 1 AA1 ALA A 55 LEU A 59 5 5
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 GLY A 211
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 LEU A 41 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 SER A 32 O LEU A 67
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 2.02
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.04
SITE 1 AC1 21 HIS A 40 LEU A 41 CYS A 42 HIS A 57
SITE 2 AC1 21 CYS A 58 TRP A 141 ILE A 143 ARG A 151
SITE 3 AC1 21 SER A 190 CYS A 191 LYS A 192 GLY A 193
SITE 4 AC1 21 SER A 195 VAL A 213 THR A 214 SER A 215
SITE 5 AC1 21 GLY A 216 ARG A 218 CYS A 220 HOH A 406
SITE 6 AC1 21 HOH A 466
SITE 1 AC2 10 GLU A 21 ALA A 22 ARG A 179 ALA A 232
SITE 2 AC2 10 SER A 233 TYR A 234 ALA A 235 ALA A 236
SITE 3 AC2 10 HOH A 416 HOH A 417
CRYST1 38.266 48.742 54.730 90.00 108.82 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 0.026133 0.000000 0.008905 0.00000
SCALE2 0.000000 0.020516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019303 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
