HEADER HYDROLASE 17-OCT-16 5H2Q
TITLE CRYSTAL STRUCTURE OF T BRUCEI PHOSPHODIESTERASE B2 BOUND TO COMPOUND
TITLE 2 13E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 586-918;
COMPND 5 EC: 3.1.4.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;
SOURCE 3 ORGANISM_TAXID: 185431;
SOURCE 4 STRAIN: 927/4 GUTAT10.1
KEYWDS PHOSPHODIESTERASE INHIBITOR, TRYPANOSOMA BRUCEI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.NOBLE
REVDAT 2 08-NOV-23 5H2Q 1 LINK
REVDAT 1 01-NOV-17 5H2Q 0
JRNL AUTH P.S.NG,C.G.NOBLE,F.S.B.NG,S.H.CHEW,C.C.LIM,V.MANOHARAN,
JRNL AUTH 2 K.F.WAN,P.VACHASPATI,M.KAISER,N.L.MA,P.GEDECK,C.KOUNDE,
JRNL AUTH 3 S.P.S.RAO
JRNL TITL TRYPANOSOMAL PHOSPHODIESTERASE B1 AND B2 AS A POTENTIAL
JRNL TITL 2 THERAPY FOR HUMAN AFRICAN TRYPANOSOMIASIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 78106
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) : 0.172
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3932
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5725
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2162
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5441
REMARK 3 BIN R VALUE (WORKING SET) : 0.2154
REMARK 3 BIN FREE R VALUE : 0.2309
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.96
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 284
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 : 5274
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.54600
REMARK 3 B22 (A**2) : -2.54600
REMARK 3 B33 (A**2) : 5.09200
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) : 0.176
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.103
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.096
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.096
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.092
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 : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5466 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7391 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1988 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 150 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 809 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5466 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 694 ; 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 : 7218 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.95
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.86
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.24
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5H2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001902.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-14
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78106
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 84.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 4I15
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% PEG 3350, 0.1 M MES, PH 5.5 AND
REMARK 280 0.2 M MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 40.14667
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 80.29333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.29333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.14667
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 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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1302 LIES ON A SPECIAL POSITION.
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 GLY A 582
REMARK 465 SER A 583
REMARK 465 HIS A 584
REMARK 465 MET A 585
REMARK 465 VAL A 586
REMARK 465 THR A 587
REMARK 465 GLU A 917
REMARK 465 ALA A 918
REMARK 465 GLY B 582
REMARK 465 SER B 583
REMARK 465 HIS B 584
REMARK 465 MET B 585
REMARK 465 VAL B 586
REMARK 465 SER B 802
REMARK 465 TYR B 803
REMARK 465 ASN B 804
REMARK 465 ALA B 918
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 802 125.16 -24.65
REMARK 500 VAL A 882 -73.48 -123.13
REMARK 500 CYS A 894 -38.51 -164.74
REMARK 500 LEU A 895 58.37 -92.44
REMARK 500 VAL B 882 -66.69 -124.84
REMARK 500 CYS B 894 -38.32 -159.40
REMARK 500 LEU B 895 59.31 -91.97
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 A1477 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1478 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A1479 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH B1465 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B1466 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B1467 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B1468 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH B1469 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH B1470 DISTANCE = 7.54 ANGSTROMS
REMARK 525 HOH B1471 DISTANCE = 9.78 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 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 673 NE2
REMARK 620 2 HIS A 709 NE2 99.4
REMARK 620 3 ASP A 710 OD2 90.3 87.4
REMARK 620 4 ASP A 823 OD1 93.3 88.8 175.2
REMARK 620 5 HOH A1101 O 166.8 93.8 88.7 88.6
REMARK 620 6 HOH A1199 O 89.7 167.8 100.8 82.5 77.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 710 OD1
REMARK 620 2 HOH A1101 O 90.2
REMARK 620 3 HOH A1106 O 86.1 91.9
REMARK 620 4 HOH A1116 O 170.8 91.5 84.8
REMARK 620 5 HOH A1122 O 92.6 177.2 88.4 85.7
REMARK 620 6 HOH A1291 O 97.8 88.0 176.0 91.3 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 673 NE2
REMARK 620 2 HIS B 709 NE2 98.8
REMARK 620 3 ASP B 710 OD2 92.9 82.8
REMARK 620 4 ASP B 823 OD1 93.8 91.9 172.0
REMARK 620 5 HOH B1102 O 163.1 97.9 87.3 87.6
REMARK 620 6 HOH B1108 O 91.4 169.2 100.3 83.9 72.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 710 OD1
REMARK 620 2 HOH B1102 O 94.3
REMARK 620 3 HOH B1106 O 86.9 95.4
REMARK 620 4 HOH B1137 O 174.4 87.4 87.7
REMARK 620 5 HOH B1155 O 94.0 168.4 93.1 85.1
REMARK 620 6 HOH B1267 O 93.8 83.4 178.8 91.7 88.0
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 ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LLI A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LLI B 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H2R RELATED DB: PDB
DBREF 5H2Q A 586 918 UNP Q38F42 Q38F42_TRYB2 586 918
DBREF 5H2Q B 586 918 UNP Q38F42 Q38F42_TRYB2 586 918
SEQADV 5H2Q GLY A 582 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q SER A 583 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q HIS A 584 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q MET A 585 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q GLY B 582 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q SER B 583 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q HIS B 584 UNP Q38F42 EXPRESSION TAG
SEQADV 5H2Q MET B 585 UNP Q38F42 EXPRESSION TAG
SEQRES 1 A 337 GLY SER HIS MET VAL THR ALA ILE THR ASN ARG GLU ARG
SEQRES 2 A 337 GLU ALA VAL LEU ARG ILE GLU PHE PRO ASN VAL ASP VAL
SEQRES 3 A 337 THR ASP ILE ASP PHE ASP LEU PHE GLN ALA ARG GLU SER
SEQRES 4 A 337 THR ASP LYS PRO LEU ASP VAL ALA ALA ALA ILE ALA TYR
SEQRES 5 A 337 ARG LEU LEU LEU GLY SER GLY LEU PRO GLN LYS PHE GLY
SEQRES 6 A 337 CYS SER ASP GLU VAL LEU LEU ASN PHE ILE LEU GLN CYS
SEQRES 7 A 337 ARG LYS LYS TYR ARG ASN VAL PRO TYR HIS ASN PHE TYR
SEQRES 8 A 337 HIS VAL VAL ASP VAL CYS GLN THR ILE TYR THR PHE LEU
SEQRES 9 A 337 TYR ARG GLY ASN VAL TYR GLU LYS LEU THR GLU LEU GLU
SEQRES 10 A 337 CYS PHE VAL LEU LEU ILE THR ALA LEU VAL HIS ASP LEU
SEQRES 11 A 337 ASP HIS MET GLY LEU ASN ASN SER PHE TYR LEU LYS THR
SEQRES 12 A 337 GLU SER PRO LEU GLY ILE LEU SER SER ALA SER GLY ASN
SEQRES 13 A 337 LYS SER VAL LEU GLU VAL HIS HIS CYS ASN LEU ALA VAL
SEQRES 14 A 337 GLU ILE LEU SER ASP PRO GLU SER ASP VAL PHE GLY GLY
SEQRES 15 A 337 LEU GLU GLY ALA GLU ARG THR LEU ALA PHE ARG SER MET
SEQRES 16 A 337 ILE ASP CYS VAL LEU ALA THR ASP MET ALA ARG HIS SER
SEQRES 17 A 337 GLU PHE LEU GLU LYS TYR LEU GLU LEU MET LYS THR SER
SEQRES 18 A 337 TYR ASN VAL ASP ASP SER ASP HIS ARG GLN MET THR MET
SEQRES 19 A 337 ASP VAL LEU MET LYS ALA GLY ASP ILE SER ASN VAL THR
SEQRES 20 A 337 LYS PRO PHE ASP ILE SER ARG GLN TRP ALA MET ALA VAL
SEQRES 21 A 337 THR GLU GLU PHE TYR ARG GLN GLY ASP MET GLU LYS GLU
SEQRES 22 A 337 ARG GLY VAL GLU VAL LEU PRO MET PHE ASP ARG SER LYS
SEQRES 23 A 337 ASN MET GLU LEU ALA LYS GLY GLN ILE GLY PHE ILE ASP
SEQRES 24 A 337 PHE VAL ALA ALA PRO PHE PHE GLN LYS ILE VAL ASP ALA
SEQRES 25 A 337 CYS LEU GLN GLY MET GLN TRP THR VAL ASP ARG THR LYS
SEQRES 26 A 337 SER ASN ARG ALA GLN TRP GLU ARG VAL LEU GLU ALA
SEQRES 1 B 337 GLY SER HIS MET VAL THR ALA ILE THR ASN ARG GLU ARG
SEQRES 2 B 337 GLU ALA VAL LEU ARG ILE GLU PHE PRO ASN VAL ASP VAL
SEQRES 3 B 337 THR ASP ILE ASP PHE ASP LEU PHE GLN ALA ARG GLU SER
SEQRES 4 B 337 THR ASP LYS PRO LEU ASP VAL ALA ALA ALA ILE ALA TYR
SEQRES 5 B 337 ARG LEU LEU LEU GLY SER GLY LEU PRO GLN LYS PHE GLY
SEQRES 6 B 337 CYS SER ASP GLU VAL LEU LEU ASN PHE ILE LEU GLN CYS
SEQRES 7 B 337 ARG LYS LYS TYR ARG ASN VAL PRO TYR HIS ASN PHE TYR
SEQRES 8 B 337 HIS VAL VAL ASP VAL CYS GLN THR ILE TYR THR PHE LEU
SEQRES 9 B 337 TYR ARG GLY ASN VAL TYR GLU LYS LEU THR GLU LEU GLU
SEQRES 10 B 337 CYS PHE VAL LEU LEU ILE THR ALA LEU VAL HIS ASP LEU
SEQRES 11 B 337 ASP HIS MET GLY LEU ASN ASN SER PHE TYR LEU LYS THR
SEQRES 12 B 337 GLU SER PRO LEU GLY ILE LEU SER SER ALA SER GLY ASN
SEQRES 13 B 337 LYS SER VAL LEU GLU VAL HIS HIS CYS ASN LEU ALA VAL
SEQRES 14 B 337 GLU ILE LEU SER ASP PRO GLU SER ASP VAL PHE GLY GLY
SEQRES 15 B 337 LEU GLU GLY ALA GLU ARG THR LEU ALA PHE ARG SER MET
SEQRES 16 B 337 ILE ASP CYS VAL LEU ALA THR ASP MET ALA ARG HIS SER
SEQRES 17 B 337 GLU PHE LEU GLU LYS TYR LEU GLU LEU MET LYS THR SER
SEQRES 18 B 337 TYR ASN VAL ASP ASP SER ASP HIS ARG GLN MET THR MET
SEQRES 19 B 337 ASP VAL LEU MET LYS ALA GLY ASP ILE SER ASN VAL THR
SEQRES 20 B 337 LYS PRO PHE ASP ILE SER ARG GLN TRP ALA MET ALA VAL
SEQRES 21 B 337 THR GLU GLU PHE TYR ARG GLN GLY ASP MET GLU LYS GLU
SEQRES 22 B 337 ARG GLY VAL GLU VAL LEU PRO MET PHE ASP ARG SER LYS
SEQRES 23 B 337 ASN MET GLU LEU ALA LYS GLY GLN ILE GLY PHE ILE ASP
SEQRES 24 B 337 PHE VAL ALA ALA PRO PHE PHE GLN LYS ILE VAL ASP ALA
SEQRES 25 B 337 CYS LEU GLN GLY MET GLN TRP THR VAL ASP ARG THR LYS
SEQRES 26 B 337 SER ASN ARG ALA GLN TRP GLU ARG VAL LEU GLU ALA
HET ZN A1001 1
HET MG A1002 1
HET LLI A1003 35
HET ZN B1001 1
HET MG B1002 1
HET LLI B1003 35
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM LLI (4~{A}~{S},8~{A}~{R})-2-CYCLOHEPTYL-4-[4-METHOXY-3-[2-
HETNAM 2 LLI (2-OXIDANYLIDENEIMIDAZOLIDIN-1-YL)ETHOXY]PHENYL]-
HETNAM 3 LLI 4~{A},5,8,8~{A}-TETRAHYDROPHTHALAZIN-1-ONE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 LLI 2(C27 H36 N4 O4)
FORMUL 9 HOH *750(H2 O)
HELIX 1 AA1 THR A 590 ARG A 599 1 10
HELIX 2 AA2 ASP A 613 SER A 620 1 8
HELIX 3 AA3 LYS A 623 GLY A 640 1 18
HELIX 4 AA4 GLY A 640 PHE A 645 1 6
HELIX 5 AA5 SER A 648 LYS A 662 1 15
HELIX 6 AA6 ASN A 670 ARG A 687 1 18
HELIX 7 AA7 ASN A 689 LEU A 694 5 6
HELIX 8 AA8 THR A 695 HIS A 709 1 15
HELIX 9 AA9 ASN A 717 THR A 724 1 8
HELIX 10 AB1 SER A 726 GLY A 736 1 11
HELIX 11 AB2 SER A 739 SER A 754 1 16
HELIX 12 AB3 ASP A 755 ASP A 759 5 5
HELIX 13 AB4 GLU A 765 ALA A 782 1 18
HELIX 14 AB5 THR A 783 ALA A 786 5 4
HELIX 15 AB6 ARG A 787 MET A 799 1 13
HELIX 16 AB7 ASP A 807 ILE A 824 1 18
HELIX 17 AB8 SER A 825 LYS A 829 5 5
HELIX 18 AB9 PRO A 830 GLY A 856 1 27
HELIX 19 AC1 LEU A 860 ASP A 864 5 5
HELIX 20 AC2 GLU A 870 VAL A 882 1 13
HELIX 21 AC3 VAL A 882 CYS A 894 1 13
HELIX 22 AC4 LEU A 895 GLY A 897 5 3
HELIX 23 AC5 MET A 898 LEU A 916 1 19
HELIX 24 AC6 THR B 590 ARG B 599 1 10
HELIX 25 AC7 ASP B 613 SER B 620 1 8
HELIX 26 AC8 LYS B 623 SER B 639 1 17
HELIX 27 AC9 GLY B 640 PHE B 645 1 6
HELIX 28 AD1 SER B 648 LYS B 662 1 15
HELIX 29 AD2 ASN B 670 ARG B 687 1 18
HELIX 30 AD3 ASN B 689 LEU B 694 5 6
HELIX 31 AD4 THR B 695 HIS B 709 1 15
HELIX 32 AD5 ASN B 717 THR B 724 1 8
HELIX 33 AD6 SER B 726 GLY B 736 1 11
HELIX 34 AD7 SER B 739 SER B 754 1 16
HELIX 35 AD8 ASP B 755 ASP B 759 5 5
HELIX 36 AD9 GLU B 765 ALA B 782 1 18
HELIX 37 AE1 THR B 783 ALA B 786 5 4
HELIX 38 AE2 ARG B 787 LYS B 800 1 14
HELIX 39 AE3 ASP B 807 ILE B 824 1 18
HELIX 40 AE4 SER B 825 LYS B 829 5 5
HELIX 41 AE5 PRO B 830 ARG B 855 1 26
HELIX 42 AE6 LEU B 860 ASN B 868 5 9
HELIX 43 AE7 GLU B 870 VAL B 882 1 13
HELIX 44 AE8 VAL B 882 CYS B 894 1 13
HELIX 45 AE9 LEU B 895 GLY B 897 5 3
HELIX 46 AF1 MET B 898 GLU B 917 1 20
LINK NE2 HIS A 673 ZN ZN A1001 1555 1555 2.13
LINK NE2 HIS A 709 ZN ZN A1001 1555 1555 2.13
LINK OD2 ASP A 710 ZN ZN A1001 1555 1555 2.05
LINK OD1 ASP A 710 MG MG A1002 1555 1555 2.07
LINK OD1 ASP A 823 ZN ZN A1001 1555 1555 2.16
LINK ZN ZN A1001 O HOH A1101 1555 1555 2.28
LINK ZN ZN A1001 O HOH A1199 1555 1555 2.19
LINK MG MG A1002 O HOH A1101 1555 1555 2.09
LINK MG MG A1002 O HOH A1106 1555 1555 2.19
LINK MG MG A1002 O HOH A1116 1555 1555 2.19
LINK MG MG A1002 O HOH A1122 1555 1555 2.12
LINK MG MG A1002 O HOH A1291 1555 1555 2.06
LINK NE2 HIS B 673 ZN ZN B1001 1555 1555 2.19
LINK NE2 HIS B 709 ZN ZN B1001 1555 1555 2.09
LINK OD2 ASP B 710 ZN ZN B1001 1555 1555 2.09
LINK OD1 ASP B 710 MG MG B1002 1555 1555 2.03
LINK OD1 ASP B 823 ZN ZN B1001 1555 1555 2.09
LINK ZN ZN B1001 O HOH B1102 1555 1555 2.39
LINK ZN ZN B1001 O HOH B1108 1555 1555 2.24
LINK MG MG B1002 O HOH B1102 1555 1555 2.11
LINK MG MG B1002 O HOH B1106 1555 1555 2.10
LINK MG MG B1002 O HOH B1137 1555 1555 2.14
LINK MG MG B1002 O HOH B1155 1555 1555 2.14
LINK MG MG B1002 O HOH B1267 1555 1555 2.12
SITE 1 AC1 6 HIS A 673 HIS A 709 ASP A 710 ASP A 823
SITE 2 AC1 6 HOH A1101 HOH A1199
SITE 1 AC2 6 ASP A 710 HOH A1101 HOH A1106 HOH A1116
SITE 2 AC2 6 HOH A1122 HOH A1291
SITE 1 AC3 10 MET A 785 ASN A 826 VAL A 841 THR A 842
SITE 2 AC3 10 PHE A 845 MET A 862 GLY A 874 GLN A 875
SITE 3 AC3 10 PHE A 878 HOH A1175
SITE 1 AC4 6 HIS B 673 HIS B 709 ASP B 710 ASP B 823
SITE 2 AC4 6 HOH B1102 HOH B1108
SITE 1 AC5 6 ASP B 710 HOH B1102 HOH B1106 HOH B1137
SITE 2 AC5 6 HOH B1155 HOH B1267
SITE 1 AC6 10 MET B 785 ASN B 826 VAL B 841 THR B 842
SITE 2 AC6 10 MET B 862 GLY B 874 GLN B 875 PHE B 878
SITE 3 AC6 10 HOH B1104 HOH B1245
CRYST1 97.210 97.210 120.440 90.00 90.00 120.00 P 31 2 1 12
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 0.010287 0.005939 0.000000 0.00000
SCALE2 0.000000 0.011878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008303 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
