HEADER HYDROLASE/HYDROLASE INHIBITOR 13-APR-15 4ZAE
TITLE DEVELOPMENT OF A NOVEL CLASS OF POTENT AND SELECTIVE FIXA INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR IX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PEPTIDASE S1 DOMAIN (UNP RESIDUES 227-461);
COMPND 5 SYNONYM: CHRISTMAS FACTOR,PLASMA THROMBOPLASTIN COMPONENT,PTC;
COMPND 6 EC: 3.4.21.22;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: COAGULATION FACTOR IX;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: EG-LIKE 2 DOMAIN (UNP RESIDUES 131-191);
COMPND 13 SYNONYM: CHRISTMAS FACTOR,PLASMA THROMBOPLASTIN COMPONENT,PTC;
COMPND 14 EC: 3.4.21.22;
COMPND 15 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: F9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: F9;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE PROTEINASE, BLOOD COAGULATION, COAGULATION FACTOR, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HRUZA,P.REICHERT
REVDAT 4 27-SEP-23 4ZAE 1 REMARK
REVDAT 3 22-NOV-17 4ZAE 1 JRNL REMARK
REVDAT 2 28-OCT-15 4ZAE 1 JRNL
REVDAT 1 03-JUN-15 4ZAE 0
JRNL AUTH T.ZHANG,P.ANDRE,T.J.BATEMAN,Y.H.CHEN,K.DESAI,K.ELLSWORTH,
JRNL AUTH 2 W.M.GEISSLER,L.GUO,A.HRUZA,T.JIAN,D.MENG,D.L.PARKER,X.QIAN,
JRNL AUTH 3 P.REICHERT,E.C.SHERER,M.SHU,C.J.SMITH,L.M.SONATORE,
JRNL AUTH 4 R.TSCHIRRET-GUTH,A.F.NOLTING,R.ORR,L.C.CAMPEAU,K.ARAKI,
JRNL AUTH 5 T.NISHIMURA,I.SAKURADA,H.B.WOOD
JRNL TITL DEVELOPMENT OF A NOVEL CLASS OF POTENT AND SELECTIVE FIXA
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 4945 2015
JRNL REFN ESSN 1464-3405
JRNL PMID 25978966
JRNL DOI 10.1016/J.BMCL.2015.04.057
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 29369
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1475
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.93
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2884
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1869
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2729
REMARK 3 BIN R VALUE (WORKING SET) : 0.1865
REMARK 3 BIN FREE R VALUE : 0.1940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 155
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2240
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03610
REMARK 3 B22 (A**2) : -1.03610
REMARK 3 B33 (A**2) : 2.07220
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.193
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.099
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.094
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.138
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.095
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4602 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8304 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 991 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 56 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 738 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4602 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 4 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 299 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5054 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.26
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 13.63
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4237 -33.6780 -3.2478
REMARK 3 T TENSOR
REMARK 3 T11: 0.0193 T22: -0.1265
REMARK 3 T33: -0.1313 T12: -0.0014
REMARK 3 T13: 0.0285 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.3272 L22: 1.5309
REMARK 3 L33: 2.1672 L12: 0.5150
REMARK 3 L13: -0.3743 L23: -0.5158
REMARK 3 S TENSOR
REMARK 3 S11: -0.1630 S12: 0.1004 S13: -0.1161
REMARK 3 S21: -0.2253 S22: 0.0764 S23: 0.0107
REMARK 3 S31: 0.4164 S32: -0.0006 S33: 0.0867
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8375 -28.4724 19.8828
REMARK 3 T TENSOR
REMARK 3 T11: 0.0057 T22: 0.0246
REMARK 3 T33: -0.0651 T12: 0.0041
REMARK 3 T13: -0.0154 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.0688 L22: 1.5175
REMARK 3 L33: 1.7873 L12: -0.0410
REMARK 3 L13: 0.4718 L23: -0.6983
REMARK 3 S TENSOR
REMARK 3 S11: -0.0313 S12: -0.1136 S13: 0.0783
REMARK 3 S21: 0.1096 S22: -0.1052 S23: -0.0300
REMARK 3 S31: -0.1626 S32: 0.2136 S33: 0.1365
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION DECEMBER 29
REMARK 200 DATA SCALING SOFTWARE : SCALA, AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29508
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.857
REMARK 200 RESOLUTION RANGE LOW (A) : 63.728
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.57500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.575
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: 1RFN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM CHES, PH 9.0, 1.3 M TRI-SODIUM
REMARK 280 CITRATE AND 3 MM COMPOUND (CROSS SEEDED WITH CRYSTALS GROWN FROM
REMARK 280 50 MM TRIS, PH 7.2, 1.45 M AMMONIUM SULFATE, 2.0 M SODIUM
REMARK 280 CHLORIDE AND 3 MM COMPOUND), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.72600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.70932
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.57900
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 49.72600
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 28.70932
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.57900
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 49.72600
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 28.70932
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.57900
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.41864
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 63.15800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 57.41864
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 63.15800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 57.41864
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.15800
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: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 THR A 245
REMARK 465 MET B 84
REMARK 465 ASP B 85
REMARK 465 SER B 141
REMARK 465 LYS B 142
REMARK 465 LEU B 143
REMARK 465 THR B 144
REMARK 465 ARG B 145
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 THR B 140 CB OG1 CG2
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 HIS A 71 -64.19 -134.74
REMARK 500 HIS A 78 -38.32 88.97
REMARK 500 SER A 214 -73.11 -114.31
REMARK 500 GLU A 217 -108.97 -117.45
REMARK 500 GLN B 97 -78.89 -113.62
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 588 DISTANCE = 7.45 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 88.8
REMARK 620 3 GLU A 75 O 167.3 84.6
REMARK 620 4 GLU A 77 OE1 93.7 89.6 97.1
REMARK 620 5 GLU A 80 OE2 98.6 171.1 87.2 94.9
REMARK 620 6 HOH A 406 O 85.9 96.6 84.1 173.8 79.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4M1 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 303
DBREF 4ZAE A 16 245 UNP P00740 FA9_HUMAN 227 461
DBREF 4ZAE B 85 145 UNP P00740 FA9_HUMAN 131 191
SEQADV 4ZAE ALA A 150 UNP P00740 ARG 364 ENGINEERED MUTATION
SEQADV 4ZAE MET B 84 UNP P00740 INITIATING METHIONINE
SEQRES 1 A 235 VAL VAL GLY GLY GLU ASP ALA LYS PRO GLY GLN PHE PRO
SEQRES 2 A 235 TRP GLN VAL VAL LEU ASN GLY LYS VAL ASP ALA PHE CYS
SEQRES 3 A 235 GLY GLY SER ILE VAL ASN GLU LYS TRP ILE VAL THR ALA
SEQRES 4 A 235 ALA HIS CYS VAL GLU THR GLY VAL LYS ILE THR VAL VAL
SEQRES 5 A 235 ALA GLY GLU HIS ASN ILE GLU GLU THR GLU HIS THR GLU
SEQRES 6 A 235 GLN LYS ARG ASN VAL ILE ARG ILE ILE PRO HIS HIS ASN
SEQRES 7 A 235 TYR ASN ALA ALA ILE ASN LYS TYR ASN HIS ASP ILE ALA
SEQRES 8 A 235 LEU LEU GLU LEU ASP GLU PRO LEU VAL LEU ASN SER TYR
SEQRES 9 A 235 VAL THR PRO ILE CYS ILE ALA ASP LYS GLU TYR THR ASN
SEQRES 10 A 235 ILE PHE LEU LYS PHE GLY SER GLY TYR VAL SER GLY TRP
SEQRES 11 A 235 GLY ARG VAL PHE HIS LYS GLY ALA SER ALA LEU VAL LEU
SEQRES 12 A 235 GLN TYR LEU ARG VAL PRO LEU VAL ASP ARG ALA THR CYS
SEQRES 13 A 235 LEU ARG SER THR LYS PHE THR ILE TYR ASN ASN MET PHE
SEQRES 14 A 235 CYS ALA GLY PHE HIS GLU GLY GLY ARG ASP SER CYS GLN
SEQRES 15 A 235 GLY ASP SER GLY GLY PRO HIS VAL THR GLU VAL GLU GLY
SEQRES 16 A 235 THR SER PHE LEU THR GLY ILE ILE SER TRP GLY GLU GLU
SEQRES 17 A 235 CYS ALA MET LYS GLY LYS TYR GLY ILE TYR THR LYS VAL
SEQRES 18 A 235 SER ARG TYR VAL ASN TRP ILE LYS GLU LYS THR LYS LEU
SEQRES 19 A 235 THR
SEQRES 1 B 62 MET ASP VAL THR CYS ASN ILE LYS ASN GLY ARG CYS GLU
SEQRES 2 B 62 GLN PHE CYS LYS ASN SER ALA ASP ASN LYS VAL VAL CYS
SEQRES 3 B 62 SER CYS THR GLU GLY TYR ARG LEU ALA GLU ASN GLN LYS
SEQRES 4 B 62 SER CYS GLU PRO ALA VAL PRO PHE PRO CYS GLY ARG VAL
SEQRES 5 B 62 SER VAL SER GLN THR SER LYS LEU THR ARG
HET 4M1 A 301 57
HET NA A 302 1
HET NHE A 303 30
HETNAM 4M1 2,6-DICHLORO-N-[(2R)-2-(5,6-DIMETHYL-1H-BENZIMIDAZOL-2-
HETNAM 2 4M1 YL)-2-PHENYLETHYL]-4-(4H-1,2,4-TRIAZOL-4-YL)BENZAMIDE
HETNAM NA SODIUM ION
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL 3 4M1 C26 H22 CL2 N6 O
FORMUL 4 NA NA 1+
FORMUL 5 NHE C8 H17 N O3 S
FORMUL 6 HOH *260(H2 O)
HELIX 1 AA1 ALA A 55 VAL A 59 5 5
HELIX 2 AA2 ASP A 125 PHE A 133 1 11
HELIX 3 AA3 ASP A 164 SER A 171 1 8
HELIX 4 AA4 TYR A 234 LYS A 243 1 10
HELIX 5 AA5 ILE B 90 CYS B 95 5 6
HELIX 6 AA6 ALA B 103 ASN B 105 5 3
SHEET 1 AA1 8 GLU A 20 ASP A 21 0
SHEET 2 AA1 8 GLN A 156 VAL A 163 -1 O TYR A 157 N GLU A 20
SHEET 3 AA1 8 MET A 180 ALA A 183 -1 O CYS A 182 N VAL A 163
SHEET 4 AA1 8 GLY A 226 LYS A 230 -1 O TYR A 228 N PHE A 181
SHEET 5 AA1 8 THR A 206 TRP A 215 -1 N TRP A 215 O ILE A 227
SHEET 6 AA1 8 PRO A 198 VAL A 203 -1 N VAL A 203 O THR A 206
SHEET 7 AA1 8 SER A 135 GLY A 140 -1 N TYR A 137 O VAL A 200
SHEET 8 AA1 8 GLN A 156 VAL A 163 -1 O VAL A 160 N GLY A 136
SHEET 1 AA2 7 GLN A 30 ASN A 34 0
SHEET 2 AA2 7 CYS A 42 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 AA2 7 TRP A 51 THR A 54 -1 O TRP A 51 N VAL A 47
SHEET 4 AA2 7 ALA A 104 LEU A 108 -1 O LEU A 106 N ILE A 52
SHEET 5 AA2 7 GLN A 81 PRO A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 AA2 7 THR A 65 ALA A 68 -1 N ALA A 68 O GLN A 81
SHEET 7 AA2 7 GLN A 30 ASN A 34 -1 N ASN A 34 O THR A 65
SHEET 1 AA3 2 PHE B 98 SER B 102 0
SHEET 2 AA3 2 LYS B 106 SER B 110 -1 O VAL B 108 N LYS B 100
SHEET 1 AA4 2 TYR B 115 LEU B 117 0
SHEET 2 AA4 2 CYS B 124 PRO B 126 -1 O GLU B 125 N ARG B 116
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.05
SSBOND 2 CYS A 122 CYS B 132 1555 1555 2.08
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.02
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.04
SSBOND 5 CYS B 88 CYS B 99 1555 1555 2.06
SSBOND 6 CYS B 95 CYS B 109 1555 1555 2.02
SSBOND 7 CYS B 111 CYS B 124 1555 1555 2.10
LINK OE1 GLU A 70 NA NA A 302 1555 1555 2.23
LINK O ASN A 72 NA NA A 302 1555 1555 2.38
LINK O GLU A 75 NA NA A 302 1555 1555 2.24
LINK OE1 GLU A 77 NA NA A 302 1555 1555 2.43
LINK OE2 GLU A 80 NA NA A 302 1555 1555 2.42
LINK NA NA A 302 O HOH A 406 1555 1555 2.53
SITE 1 AC1 13 ARG A 87 TYR A 99 ARG A 143 PHE A 174
SITE 2 AC1 13 SER A 190 CYS A 191 GLN A 192 ILE A 213
SITE 3 AC1 13 TRP A 215 GLY A 216 GLU A 217 CYS A 220
SITE 4 AC1 13 HOH A 476
SITE 1 AC2 6 GLU A 70 ASN A 72 GLU A 75 GLU A 77
SITE 2 AC2 6 GLU A 80 HOH A 406
SITE 1 AC3 11 ASP A 21 LYS A 132 PHE A 145 ALA A 152
SITE 2 AC3 11 LEU A 153 VAL A 154 HOH A 451 HOH A 480
SITE 3 AC3 11 HOH A 511 HOH A 528 HOH A 558
CRYST1 99.452 99.452 94.737 90.00 90.00 120.00 H 3 9
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 0.010055 0.005805 0.000000 0.00000
SCALE2 0.000000 0.011611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010556 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
