HEADER HYDROLASE 01-MAY-16 5JO3
TITLE PDE5A FOR NAV1.7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN CONTAINING RESIDUES 534-858;
COMPND 5 SYNONYM: CGMP-BINDING CGMP-SPECIFIC PHOSPHODIESTERASE,CGB-PDE;
COMPND 6 EC: 3.1.4.35;
COMPND 7 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: PDE5A, PDE5;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.STORER,J.CHRENCIK
REVDAT 3 06-MAR-24 5JO3 1 LINK
REVDAT 2 09-AUG-17 5JO3 1 REMARK
REVDAT 1 03-MAY-17 5JO3 0
JRNL AUTH A.BELL,A.BENT,P.BRADLEY,P.ERDMAN,M.DE GROOT,R.LEWTHWAITE,
JRNL AUTH 2 I.MARSH,S.RANSLEY,N.SCIAMMETTA,R.SMITH,N.SWAIN,R.TORELLA,
JRNL AUTH 3 I.STORER
JRNL TITL PDE5A FOR NAV1.7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.6
REMARK 3 NUMBER OF REFLECTIONS : 43300
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2327
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1677
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 44.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2611
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 367
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.82000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.049
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2688 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3637 ; 1.137 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 322 ; 5.013 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;37.409 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 497 ;12.618 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;12.661 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 410 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2013 ; 0.005 ; 0.021
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): 1616 ; 0.621 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2609 ; 1.250 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1072 ; 2.270 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1028 ; 3.865 ; 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 : 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 : 1.40
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 5JO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45627
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 44.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.11500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4K 10% ISOPROPANOL 0.1M HEPES
REMARK 280 PH 7.4, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 27.92000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 27.92000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.05000
REMARK 290 SMTRY3 4 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 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 B1136 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1175 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 GLU B 534
REMARK 465 GLU B 535
REMARK 465 GLU B 536
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 OH TYR B 676 O HOH B 1001 1.92
REMARK 500 CE2 TYR B 676 O HOH B 1013 2.12
REMARK 500 OD2 ASP B 687 O HOH B 1002 2.19
REMARK 500 N ARG B 538 O HOH B 1003 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 B 1278 O HOH B 1286 2656 2.04
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 ARG B 538 -58.34 76.41
REMARK 500 LYS B 630 -82.71 -85.97
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 B1366 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B1367 DISTANCE = 6.43 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 B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 617 NE2
REMARK 620 2 HIS B 653 NE2 100.6
REMARK 620 3 ASP B 654 OD2 90.2 87.6
REMARK 620 4 ASP B 764 OD2 87.8 88.7 175.5
REMARK 620 5 HOH B1041 O 86.9 167.4 102.5 81.4
REMARK 620 6 HOH B1086 O 164.0 95.4 90.3 92.6 77.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 654 OD1
REMARK 620 2 HOH B1027 O 79.6
REMARK 620 3 HOH B1029 O 162.0 85.4
REMARK 620 4 HOH B1086 O 92.8 92.7 97.9
REMARK 620 5 HOH B1120 O 86.7 87.0 82.6 179.4
REMARK 620 6 HOH B1172 O 100.8 175.7 93.4 91.6 88.8
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 B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LK B 903
DBREF 5JO3 B 534 858 UNP O76074 PDE5A_HUMAN 534 858
SEQADV 5JO3 PRO B 658 UNP O76074 ARG 658 CONFLICT
SEQADV 5JO3 SER B 661 UNP O76074 ASN 661 CONFLICT
SEQADV 5JO3 GLN B 663 UNP O76074 SER 663 CONFLICT
SEQADV 5JO3 PHE B 664 UNP O76074 TYR 664 CONFLICT
SEQADV 5JO3 LEU B 665 UNP O76074 ILE 665 CONFLICT
SEQADV 5JO3 ILE B 666 UNP O76074 GLN 666 CONFLICT
SEQADV 5JO3 ASN B 667 UNP O76074 ARG 667 CONFLICT
SEQADV 5JO3 THR B 668 UNP O76074 SER 668 CONFLICT
SEQADV 5JO3 ASN B 669 UNP O76074 GLU 669 CONFLICT
SEQADV 5JO3 SER B 670 UNP O76074 HIS 670 CONFLICT
SEQADV 5JO3 GLU B 671 UNP O76074 PRO 671 CONFLICT
SEQADV 5JO3 LEU B 674 UNP O76074 GLN 674 CONFLICT
SEQADV 5JO3 MET B 675 UNP O76074 LEU 675 CONFLICT
SEQADV 5JO3 ASN B 677 UNP O76074 INSERTION
SEQADV 5JO3 ASP B 678 UNP O76074 CYS 677 CONFLICT
SEQADV 5JO3 GLU B 679 UNP O76074 HIS 678 CONFLICT
SEQADV 5JO3 VAL B 681 UNP O76074 ILE 680 CONFLICT
SEQADV 5JO3 LEU B 681A UNP O76074 MET 681 CONFLICT
SEQADV 5JO3 GLU B 751 UNP O76074 GLN 751 CONFLICT
SEQRES 1 B 326 GLU GLU GLU THR ARG GLU LEU GLN SER LEU ALA ALA ALA
SEQRES 2 B 326 VAL VAL PRO SER ALA GLN THR LEU LYS ILE THR ASP PHE
SEQRES 3 B 326 SER PHE SER ASP PHE GLU LEU SER ASP LEU GLU THR ALA
SEQRES 4 B 326 LEU CYS THR ILE ARG MET PHE THR ASP LEU ASN LEU VAL
SEQRES 5 B 326 GLN ASN PHE GLN MET LYS HIS GLU VAL LEU CYS ARG TRP
SEQRES 6 B 326 ILE LEU SER VAL LYS LYS ASN TYR ARG LYS ASN VAL ALA
SEQRES 7 B 326 TYR HIS ASN TRP ARG HIS ALA PHE ASN THR ALA GLN CYS
SEQRES 8 B 326 MET PHE ALA ALA LEU LYS ALA GLY LYS ILE GLN ASN LYS
SEQRES 9 B 326 LEU THR ASP LEU GLU ILE LEU ALA LEU LEU ILE ALA ALA
SEQRES 10 B 326 LEU SER HIS ASP LEU ASP HIS PRO GLY VAL SER ASN GLN
SEQRES 11 B 326 PHE LEU ILE ASN THR ASN SER GLU LEU ALA LEU MET TYR
SEQRES 12 B 326 ASN ASP GLU SER VAL LEU GLU HIS HIS HIS PHE ASP GLN
SEQRES 13 B 326 CYS LEU MET ILE LEU ASN SER PRO GLY ASN GLN ILE LEU
SEQRES 14 B 326 SER GLY LEU SER ILE GLU GLU TYR LYS THR THR LEU LYS
SEQRES 15 B 326 ILE ILE LYS GLN ALA ILE LEU ALA THR ASP LEU ALA LEU
SEQRES 16 B 326 TYR ILE LYS ARG ARG GLY GLU PHE PHE GLU LEU ILE ARG
SEQRES 17 B 326 LYS ASN GLN PHE ASN LEU GLU ASP PRO HIS GLU LYS GLU
SEQRES 18 B 326 LEU PHE LEU ALA MET LEU MET THR ALA CYS ASP LEU SER
SEQRES 19 B 326 ALA ILE THR LYS PRO TRP PRO ILE GLN GLN ARG ILE ALA
SEQRES 20 B 326 GLU LEU VAL ALA THR GLU PHE PHE ASP GLN GLY ASP ARG
SEQRES 21 B 326 GLU ARG LYS GLU LEU ASN ILE GLU PRO THR ASP LEU MET
SEQRES 22 B 326 ASN ARG GLU LYS LYS ASN LYS ILE PRO SER MET GLN VAL
SEQRES 23 B 326 GLY PHE ILE ASP ALA ILE CYS LEU GLN LEU TYR GLU ALA
SEQRES 24 B 326 LEU THR HIS VAL SER GLU ASP CYS PHE PRO LEU LEU ASP
SEQRES 25 B 326 GLY CYS ARG LYS ASN ARG GLN LYS TRP GLN ALA LEU ALA
SEQRES 26 B 326 GLU
HET ZN B 901 1
HET ZN B 902 1
HET 6LK B 903 26
HETNAM ZN ZINC ION
HETNAM 6LK 1-(5-CHLORO-6-METHOXYPYRIDIN-3-YL)-3-METHYL-N-
HETNAM 2 6LK (METHYLSULFONYL)-1H-INDAZOLE-5-CARBOXAMIDE
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 6LK C16 H15 CL N4 O4 S
FORMUL 5 HOH *367(H2 O)
HELIX 1 AA1 ARG B 538 ALA B 546 1 9
HELIX 2 AA2 SER B 550 LYS B 555 1 6
HELIX 3 AA3 SER B 567 LEU B 582 1 16
HELIX 4 AA4 LYS B 591 ASN B 605 1 15
HELIX 5 AA5 ASN B 614 LYS B 630 1 17
HELIX 6 AA6 ILE B 634 LEU B 638 5 5
HELIX 7 AA7 THR B 639 HIS B 653 1 15
HELIX 8 AA8 SER B 661 THR B 668 1 8
HELIX 9 AA9 SER B 670 TYR B 676 1 7
HELIX 10 AB1 SER B 680 ASN B 694 1 16
HELIX 11 AB2 SER B 705 THR B 723 1 19
HELIX 12 AB3 ASP B 724 LYS B 741 1 18
HELIX 13 AB4 ASP B 748 LEU B 765 1 18
HELIX 14 AB5 SER B 766 LYS B 770 5 5
HELIX 15 AB6 PRO B 771 ASN B 798 1 28
HELIX 16 AB7 THR B 802 ASN B 811 5 10
HELIX 17 AB8 LYS B 812 CYS B 825 1 14
HELIX 18 AB9 CYS B 825 SER B 836 1 12
HELIX 19 AC1 CYS B 839 GLU B 858 1 20
LINK NE2 HIS B 617 ZN ZN B 901 1555 1555 2.08
LINK NE2 HIS B 653 ZN ZN B 901 1555 1555 2.13
LINK OD2 ASP B 654 ZN ZN B 901 1555 1555 2.09
LINK OD1 ASP B 654 ZN ZN B 902 1555 1555 2.20
LINK OD2 ASP B 764 ZN ZN B 901 1555 1555 2.11
LINK ZN ZN B 901 O HOH B1041 1555 1555 2.40
LINK ZN ZN B 901 O HOH B1086 1555 1555 2.20
LINK ZN ZN B 902 O HOH B1027 1555 1555 2.19
LINK ZN ZN B 902 O HOH B1029 1555 1555 2.15
LINK ZN ZN B 902 O HOH B1086 1555 1555 2.03
LINK ZN ZN B 902 O HOH B1120 1555 1555 2.22
LINK ZN ZN B 902 O HOH B1172 1555 1555 2.04
SITE 1 AC1 6 HIS B 617 HIS B 653 ASP B 654 ASP B 764
SITE 2 AC1 6 HOH B1041 HOH B1086
SITE 1 AC2 6 ASP B 654 HOH B1027 HOH B1029 HOH B1086
SITE 2 AC2 6 HOH B1120 HOH B1172
SITE 1 AC3 13 LEU B 765 ALA B 767 ILE B 768 GLN B 775
SITE 2 AC3 13 ALA B 779 LEU B 804 MET B 816 GLN B 817
SITE 3 AC3 13 PHE B 820 HOH B1107 HOH B1196 HOH B1270
SITE 4 AC3 13 HOH B1300
CRYST1 55.840 76.100 80.920 90.00 102.56 90.00 C 1 2 1 4
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 0.017908 0.000000 0.003990 0.00000
SCALE2 0.000000 0.013141 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012661 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
