HEADER HYDROLASE 24-FEB-18 6FTW
TITLE CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 4D2 CATALYTIC DOMAIN WITH
TITLE 2 INHIBITOR NPD-048
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4D;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DPDE3,PDE43;
COMPND 5 EC: 3.1.4.53;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: RESIDUES 381-740
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDE4D, DPDE3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PHOSPHODIESTERASE, HYDROLASE, CAMP HYDROLYSIS, ALTERNATIVE SPLICING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.SINGH,D.G.BROWN
REVDAT 5 17-JAN-24 6FTW 1 LINK
REVDAT 4 04-SEP-19 6FTW 1 JRNL
REVDAT 3 31-JUL-19 6FTW 1 JRNL
REVDAT 2 24-JUL-19 6FTW 1 JRNL
REVDAT 1 20-MAR-19 6FTW 0
JRNL AUTH E.DE HEUVEL,A.K.SINGH,E.EDINK,T.VAN DER MEER,
JRNL AUTH 2 M.VAN DER WOUDE,P.SADEK,M.P.KRELL-JORGENSEN,T.VAN DEN BERGH,
JRNL AUTH 3 J.VEERMAN,G.CALJON,T.D.KALEJAIYE,M.WIJTMANS,L.MAES,
JRNL AUTH 4 H.P.DE KONING,G.JAN STERK,M.SIDERIUS,I.J.P.DE ESCH,
JRNL AUTH 5 D.G.BROWN,R.LEURS
JRNL TITL ALKYNAMIDE PHTHALAZINONES AS A NEW CLASS OF TBRPDEB1
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM. V. 27 3998 2019
JRNL REFN ESSN 1464-3391
JRNL PMID 31327675
JRNL DOI 10.1016/J.BMC.2019.06.027
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 90714
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4729
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) : 2.16
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6591
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 349
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 348
REMARK 3 SOLVENT ATOMS : 551
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : -1.12000
REMARK 3 B33 (A**2) : 0.56000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.202
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11082 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10230 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14972 ; 1.761 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 23766 ; 1.091 ; 2.984
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1300 ; 5.867 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 551 ;35.182 ;24.864
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1917 ;15.593 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;19.212 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1709 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11984 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2093 ; 0.002 ; 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): 5212 ; 3.887 ; 4.600
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5211 ; 3.885 ; 4.600
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6508 ; 5.383 ; 6.879
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6509 ; 5.383 ; 6.880
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5870 ; 4.797 ; 5.077
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5871 ; 4.796 ; 5.077
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8465 ; 6.976 ; 7.412
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13065 ; 8.333 ;55.318
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13066 ; 8.332 ;55.320
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 : 1.20
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 6FTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : CRL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95516
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 65.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 1.06300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3SL3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3350, 30% ETHYLENE GLYCOL, 0.1
REMARK 280 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 49.57000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.03000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.71500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.03000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.57000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.71500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 GLY A 75
REMARK 465 SER A 76
REMARK 465 HIS A 77
REMARK 465 MET A 78
REMARK 465 ILE A 79
REMARK 465 PRO A 80
REMARK 465 GLN A 412
REMARK 465 SER A 413
REMARK 465 PRO A 414
REMARK 465 SER A 415
REMARK 465 PRO A 416
REMARK 465 ALA A 417
REMARK 465 PRO A 418
REMARK 465 ASP A 419
REMARK 465 ASP A 420
REMARK 465 PRO A 421
REMARK 465 GLU A 422
REMARK 465 GLU A 423
REMARK 465 GLY A 424
REMARK 465 ARG A 425
REMARK 465 GLN A 426
REMARK 465 GLY A 427
REMARK 465 GLN A 428
REMARK 465 THR A 429
REMARK 465 GLU A 430
REMARK 465 LYS A 431
REMARK 465 PHE A 432
REMARK 465 GLN A 433
REMARK 465 PHE A 434
REMARK 465 GLU A 435
REMARK 465 LEU A 436
REMARK 465 THR A 437
REMARK 465 LEU A 438
REMARK 465 GLY B 75
REMARK 465 SER B 76
REMARK 465 HIS B 77
REMARK 465 MET B 78
REMARK 465 ILE B 79
REMARK 465 PRO B 80
REMARK 465 ARG B 81
REMARK 465 PHE B 82
REMARK 465 GLY B 83
REMARK 465 VAL B 84
REMARK 465 LYS B 85
REMARK 465 THR B 86
REMARK 465 GLU B 87
REMARK 465 GLN B 88
REMARK 465 SER B 413
REMARK 465 PRO B 414
REMARK 465 SER B 415
REMARK 465 PRO B 416
REMARK 465 ALA B 417
REMARK 465 PRO B 418
REMARK 465 ASP B 419
REMARK 465 ASP B 420
REMARK 465 PRO B 421
REMARK 465 GLU B 422
REMARK 465 GLU B 423
REMARK 465 GLY B 424
REMARK 465 ARG B 425
REMARK 465 GLN B 426
REMARK 465 GLY B 427
REMARK 465 GLN B 428
REMARK 465 THR B 429
REMARK 465 GLU B 430
REMARK 465 LYS B 431
REMARK 465 PHE B 432
REMARK 465 GLN B 433
REMARK 465 PHE B 434
REMARK 465 GLU B 435
REMARK 465 LEU B 436
REMARK 465 THR B 437
REMARK 465 LEU B 438
REMARK 465 GLY C 75
REMARK 465 SER C 76
REMARK 465 HIS C 77
REMARK 465 MET C 78
REMARK 465 ILE C 79
REMARK 465 PRO C 80
REMARK 465 ARG C 81
REMARK 465 PHE C 82
REMARK 465 GLY C 83
REMARK 465 VAL C 84
REMARK 465 LYS C 85
REMARK 465 THR C 86
REMARK 465 GLU C 87
REMARK 465 GLN C 412
REMARK 465 SER C 413
REMARK 465 PRO C 414
REMARK 465 SER C 415
REMARK 465 PRO C 416
REMARK 465 ALA C 417
REMARK 465 PRO C 418
REMARK 465 ASP C 419
REMARK 465 ASP C 420
REMARK 465 PRO C 421
REMARK 465 GLU C 422
REMARK 465 GLU C 423
REMARK 465 GLY C 424
REMARK 465 ARG C 425
REMARK 465 GLN C 426
REMARK 465 GLY C 427
REMARK 465 GLN C 428
REMARK 465 THR C 429
REMARK 465 GLU C 430
REMARK 465 LYS C 431
REMARK 465 PHE C 432
REMARK 465 GLN C 433
REMARK 465 PHE C 434
REMARK 465 GLU C 435
REMARK 465 LEU C 436
REMARK 465 THR C 437
REMARK 465 LEU C 438
REMARK 465 GLY D 75
REMARK 465 SER D 76
REMARK 465 HIS D 77
REMARK 465 MET D 78
REMARK 465 ILE D 79
REMARK 465 PRO D 80
REMARK 465 ARG D 81
REMARK 465 PHE D 82
REMARK 465 GLY D 83
REMARK 465 VAL D 84
REMARK 465 LYS D 85
REMARK 465 THR D 86
REMARK 465 GLU D 87
REMARK 465 SER D 413
REMARK 465 PRO D 414
REMARK 465 SER D 415
REMARK 465 PRO D 416
REMARK 465 ALA D 417
REMARK 465 PRO D 418
REMARK 465 ASP D 419
REMARK 465 ASP D 420
REMARK 465 PRO D 421
REMARK 465 GLU D 422
REMARK 465 GLU D 423
REMARK 465 GLY D 424
REMARK 465 ARG D 425
REMARK 465 GLN D 426
REMARK 465 GLY D 427
REMARK 465 GLN D 428
REMARK 465 THR D 429
REMARK 465 GLU D 430
REMARK 465 LYS D 431
REMARK 465 PHE D 432
REMARK 465 GLN D 433
REMARK 465 PHE D 434
REMARK 465 GLU D 435
REMARK 465 LEU D 436
REMARK 465 THR D 437
REMARK 465 LEU D 438
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 OD2 ASP C 345 NH2 ARG C 348 1.89
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 ASP A 266 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 201 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP B 201 CB - CG - OD2 ANGL. DEV. = -5.7 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 PHE A 82 92.54 86.47
REMARK 500 LEU A 104 141.76 -38.63
REMARK 500 ALA A 183 17.97 53.50
REMARK 500 ASP A 225 13.68 54.98
REMARK 500 SER A 227 51.00 37.44
REMARK 500 VAL A 292 41.02 -163.66
REMARK 500 SER A 294 -89.35 72.19
REMARK 500 MET A 357 -1.27 70.37
REMARK 500 ILE A 376 -60.39 -121.38
REMARK 500 ASP B 90 -60.09 13.26
REMARK 500 ASP B 98 0.63 -68.04
REMARK 500 TYR B 159 -61.83 -108.22
REMARK 500 ALA B 180 1.86 -65.33
REMARK 500 ALA B 183 17.34 59.99
REMARK 500 ASP B 225 15.62 58.53
REMARK 500 SER B 227 52.00 39.37
REMARK 500 GLU B 243 -166.79 -74.40
REMARK 500 LEU B 319 30.34 -93.48
REMARK 500 MET B 357 -0.43 84.71
REMARK 500 ASN B 362 61.77 -156.85
REMARK 500 ILE B 376 -59.85 -129.49
REMARK 500 ALA C 183 6.30 54.98
REMARK 500 ASP C 225 16.83 59.22
REMARK 500 LEU C 300 -76.76 -121.63
REMARK 500 ASP C 301 -59.61 98.31
REMARK 500 ILE C 376 -58.21 -120.92
REMARK 500 LEU D 104 134.60 -39.88
REMARK 500 TYR D 159 -64.63 -108.80
REMARK 500 ASN D 161 -169.22 -127.09
REMARK 500 ALA D 183 14.80 55.08
REMARK 500 ASN D 224 47.22 36.89
REMARK 500 LEU D 319 34.39 -98.41
REMARK 500 MET D 357 -11.56 79.46
REMARK 500 ASN D 362 57.73 -112.54
REMARK 500 ILE D 376 -60.21 -121.69
REMARK 500
REMARK 500 REMARK: NULL
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 A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 164 NE2
REMARK 620 2 HIS A 200 NE2 92.9
REMARK 620 3 ASP A 201 OD2 87.8 84.8
REMARK 620 4 ASP A 318 OD1 84.6 86.2 167.9
REMARK 620 5 HOH A 626 O 168.1 98.5 89.9 99.4
REMARK 620 6 HOH A 649 O 91.0 175.8 97.0 92.5 77.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 201 OD1
REMARK 620 2 HOH A 613 O 84.3
REMARK 620 3 HOH A 626 O 93.3 100.6
REMARK 620 4 HOH A 628 O 164.8 86.9 100.5
REMARK 620 5 HOH A 688 O 86.6 89.0 170.4 80.9
REMARK 620 6 HOH A 717 O 96.8 172.3 87.0 90.3 83.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 164 NE2
REMARK 620 2 HIS B 200 NE2 94.2
REMARK 620 3 ASP B 201 OD2 86.2 88.3
REMARK 620 4 ASP B 318 OD1 88.0 88.0 172.9
REMARK 620 5 HOH B 626 O 171.9 93.8 94.1 92.2
REMARK 620 6 HOH B 673 O 93.2 170.9 97.4 87.1 78.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 201 OD1
REMARK 620 2 HOH B 614 O 85.0
REMARK 620 3 HOH B 626 O 89.0 97.2
REMARK 620 4 HOH B 646 O 96.1 90.6 171.1
REMARK 620 5 HOH B 654 O 171.9 87.1 93.8 82.3
REMARK 620 6 HOH B 658 O 89.3 174.3 82.4 90.3 98.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 164 NE2
REMARK 620 2 HIS C 200 NE2 87.4
REMARK 620 3 ASP C 201 OD2 88.2 85.0
REMARK 620 4 ASP C 318 OD1 87.5 94.4 175.7
REMARK 620 5 HOH C 625 O 170.5 102.0 91.1 93.2
REMARK 620 6 HOH C 658 O 94.6 176.7 97.7 83.0 76.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 201 OD1
REMARK 620 2 HOH C 607 O 76.5
REMARK 620 3 HOH C 625 O 95.5 99.5
REMARK 620 4 HOH C 645 O 163.4 88.3 93.5
REMARK 620 5 HOH C 657 O 90.2 87.7 171.7 82.5
REMARK 620 6 HOH C 675 O 97.1 172.1 85.6 97.4 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 164 NE2
REMARK 620 2 HIS D 200 NE2 95.3
REMARK 620 3 ASP D 201 OD2 86.8 84.7
REMARK 620 4 ASP D 318 OD1 86.6 91.1 171.8
REMARK 620 5 HOH D 617 O 168.2 96.4 92.4 95.0
REMARK 620 6 HOH D 654 O 93.7 170.6 98.1 87.2 74.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 201 OD1
REMARK 620 2 HOH D 617 O 96.5
REMARK 620 3 HOH D 652 O 82.0 94.7
REMARK 620 4 HOH D 671 O 168.2 89.3 87.3
REMARK 620 5 HOH D 689 O 90.3 172.0 90.3 84.7
REMARK 620 6 HOH D 709 O 91.9 82.2 172.8 99.0 93.5
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE D 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E6Z D 516
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FTM RELATED DB: PDB
DBREF 6FTW A 79 438 UNP Q08499 PDE4D_HUMAN 381 740
DBREF 6FTW B 79 438 UNP Q08499 PDE4D_HUMAN 381 740
DBREF 6FTW C 79 438 UNP Q08499 PDE4D_HUMAN 381 740
DBREF 6FTW D 79 438 UNP Q08499 PDE4D_HUMAN 381 740
SEQADV 6FTW GLY A 75 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW SER A 76 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW HIS A 77 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW MET A 78 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW GLY B 75 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW SER B 76 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW HIS B 77 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW MET B 78 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW GLY C 75 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW SER C 76 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW HIS C 77 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW MET C 78 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW GLY D 75 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW SER D 76 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW HIS D 77 UNP Q08499 EXPRESSION TAG
SEQADV 6FTW MET D 78 UNP Q08499 EXPRESSION TAG
SEQRES 1 A 364 GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU
SEQRES 2 A 364 GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN
SEQRES 3 A 364 LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER
SEQRES 4 A 364 GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE
SEQRES 5 A 364 GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL
SEQRES 6 A 364 ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS
SEQRES 7 A 364 TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA
SEQRES 8 A 364 ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR
SEQRES 9 A 364 PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU
SEQRES 10 A 364 ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS
SEQRES 11 A 364 PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER
SEQRES 12 A 364 GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU
SEQRES 13 A 364 ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU
SEQRES 14 A 364 GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN
SEQRES 15 A 364 ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU
SEQRES 16 A 364 ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP
SEQRES 17 A 364 LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER
SEQRES 18 A 364 GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN
SEQRES 19 A 364 VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN
SEQRES 20 A 364 PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP
SEQRES 21 A 364 ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU
SEQRES 22 A 364 ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS
SEQRES 23 A 364 HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE
SEQRES 24 A 364 ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP
SEQRES 25 A 364 LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU
SEQRES 26 A 364 GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN
SEQRES 27 A 364 SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG
SEQRES 28 A 364 GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU
SEQRES 1 B 364 GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU
SEQRES 2 B 364 GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN
SEQRES 3 B 364 LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER
SEQRES 4 B 364 GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE
SEQRES 5 B 364 GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL
SEQRES 6 B 364 ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS
SEQRES 7 B 364 TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA
SEQRES 8 B 364 ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR
SEQRES 9 B 364 PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU
SEQRES 10 B 364 ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS
SEQRES 11 B 364 PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER
SEQRES 12 B 364 GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU
SEQRES 13 B 364 ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU
SEQRES 14 B 364 GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN
SEQRES 15 B 364 ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU
SEQRES 16 B 364 ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP
SEQRES 17 B 364 LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER
SEQRES 18 B 364 GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN
SEQRES 19 B 364 VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN
SEQRES 20 B 364 PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP
SEQRES 21 B 364 ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU
SEQRES 22 B 364 ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS
SEQRES 23 B 364 HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE
SEQRES 24 B 364 ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP
SEQRES 25 B 364 LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU
SEQRES 26 B 364 GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN
SEQRES 27 B 364 SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG
SEQRES 28 B 364 GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU
SEQRES 1 C 364 GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU
SEQRES 2 C 364 GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN
SEQRES 3 C 364 LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER
SEQRES 4 C 364 GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE
SEQRES 5 C 364 GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL
SEQRES 6 C 364 ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS
SEQRES 7 C 364 TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA
SEQRES 8 C 364 ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR
SEQRES 9 C 364 PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU
SEQRES 10 C 364 ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS
SEQRES 11 C 364 PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER
SEQRES 12 C 364 GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU
SEQRES 13 C 364 ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU
SEQRES 14 C 364 GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN
SEQRES 15 C 364 ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU
SEQRES 16 C 364 ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP
SEQRES 17 C 364 LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER
SEQRES 18 C 364 GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN
SEQRES 19 C 364 VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN
SEQRES 20 C 364 PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP
SEQRES 21 C 364 ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU
SEQRES 22 C 364 ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS
SEQRES 23 C 364 HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE
SEQRES 24 C 364 ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP
SEQRES 25 C 364 LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU
SEQRES 26 C 364 GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN
SEQRES 27 C 364 SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG
SEQRES 28 C 364 GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU
SEQRES 1 D 364 GLY SER HIS MET ILE PRO ARG PHE GLY VAL LYS THR GLU
SEQRES 2 D 364 GLN GLU ASP VAL LEU ALA LYS GLU LEU GLU ASP VAL ASN
SEQRES 3 D 364 LYS TRP GLY LEU HIS VAL PHE ARG ILE ALA GLU LEU SER
SEQRES 4 D 364 GLY ASN ARG PRO LEU THR VAL ILE MET HIS THR ILE PHE
SEQRES 5 D 364 GLN GLU ARG ASP LEU LEU LYS THR PHE LYS ILE PRO VAL
SEQRES 6 D 364 ASP THR LEU ILE THR TYR LEU MET THR LEU GLU ASP HIS
SEQRES 7 D 364 TYR HIS ALA ASP VAL ALA TYR HIS ASN ASN ILE HIS ALA
SEQRES 8 D 364 ALA ASP VAL VAL GLN SER THR HIS VAL LEU LEU SER THR
SEQRES 9 D 364 PRO ALA LEU GLU ALA VAL PHE THR ASP LEU GLU ILE LEU
SEQRES 10 D 364 ALA ALA ILE PHE ALA SER ALA ILE HIS ASP VAL ASP HIS
SEQRES 11 D 364 PRO GLY VAL SER ASN GLN PHE LEU ILE ASN THR ASN SER
SEQRES 12 D 364 GLU LEU ALA LEU MET TYR ASN ASP SER SER VAL LEU GLU
SEQRES 13 D 364 ASN HIS HIS LEU ALA VAL GLY PHE LYS LEU LEU GLN GLU
SEQRES 14 D 364 GLU ASN CYS ASP ILE PHE GLN ASN LEU THR LYS LYS GLN
SEQRES 15 D 364 ARG GLN SER LEU ARG LYS MET VAL ILE ASP ILE VAL LEU
SEQRES 16 D 364 ALA THR ASP MET SER LYS HIS MET ASN LEU LEU ALA ASP
SEQRES 17 D 364 LEU LYS THR MET VAL GLU THR LYS LYS VAL THR SER SER
SEQRES 18 D 364 GLY VAL LEU LEU LEU ASP ASN TYR SER ASP ARG ILE GLN
SEQRES 19 D 364 VAL LEU GLN ASN MET VAL HIS CYS ALA ASP LEU SER ASN
SEQRES 20 D 364 PRO THR LYS PRO LEU GLN LEU TYR ARG GLN TRP THR ASP
SEQRES 21 D 364 ARG ILE MET GLU GLU PHE PHE ARG GLN GLY ASP ARG GLU
SEQRES 22 D 364 ARG GLU ARG GLY MET GLU ILE SER PRO MET CYS ASP LYS
SEQRES 23 D 364 HIS ASN ALA SER VAL GLU LYS SER GLN VAL GLY PHE ILE
SEQRES 24 D 364 ASP TYR ILE VAL HIS PRO LEU TRP GLU THR TRP ALA ASP
SEQRES 25 D 364 LEU VAL HIS PRO ASP ALA GLN ASP ILE LEU ASP THR LEU
SEQRES 26 D 364 GLU ASP ASN ARG GLU TRP TYR GLN SER THR ILE PRO GLN
SEQRES 27 D 364 SER PRO SER PRO ALA PRO ASP ASP PRO GLU GLU GLY ARG
SEQRES 28 D 364 GLN GLY GLN THR GLU LYS PHE GLN PHE GLU LEU THR LEU
HET ZN A 501 1
HET MG A 502 1
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET EDO A 508 4
HET EDO A 509 4
HET EDO A 510 4
HET EDO A 511 4
HET EDO A 512 4
HET EDO A 513 4
HET EDO A 514 4
HET EPE A 515 15
HET EDO A 516 4
HET E6Z A 517 31
HET ZN B 501 1
HET MG B 502 1
HET EDO B 503 4
HET EDO B 504 4
HET EDO B 505 4
HET EDO B 506 4
HET EDO B 507 4
HET EPE B 508 15
HET E6Z B 509 31
HET ZN C 501 1
HET MG C 502 1
HET EDO C 503 4
HET EDO C 504 4
HET EDO C 505 4
HET EDO C 506 4
HET EDO C 507 4
HET EDO C 508 4
HET EDO C 509 4
HET EDO C 510 4
HET EPE C 511 15
HET E6Z C 512 31
HET EDO C 513 4
HET ZN D 501 1
HET MG D 502 1
HET EDO D 503 4
HET EDO D 504 4
HET EDO D 505 4
HET EDO D 506 4
HET EDO D 507 4
HET EDO D 508 4
HET EDO D 509 4
HET EDO D 510 4
HET EDO D 511 4
HET EDO D 512 4
HET EDO D 513 4
HET EPE D 514 15
HET EDO D 515 4
HET E6Z D 516 31
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM E6Z 3-{5-[(4AR,8AS)-3-CYCLOHEPTYL-4-OXO-3,4,4A,5,8,8A-
HETNAM 2 E6Z HEXAHYDROPHTHALAZIN-1-YL]-2-METHOXYPHENYL}PROP-2-
HETNAM 3 E6Z YNAMIDE
HETSYN EDO ETHYLENE GLYCOL
HETSYN EPE HEPES
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 MG 4(MG 2+)
FORMUL 7 EDO 39(C2 H6 O2)
FORMUL 19 EPE 4(C8 H18 N2 O4 S)
FORMUL 21 E6Z 4(C25 H29 N3 O3)
FORMUL 60 HOH *551(H2 O)
HELIX 1 AA1 THR A 86 LEU A 96 1 11
HELIX 2 AA2 GLU A 97 LYS A 101 5 5
HELIX 3 AA3 HIS A 105 SER A 113 1 9
HELIX 4 AA4 ARG A 116 ARG A 129 1 14
HELIX 5 AA5 ASP A 130 LYS A 136 1 7
HELIX 6 AA6 PRO A 138 HIS A 152 1 15
HELIX 7 AA7 ASN A 161 SER A 177 1 17
HELIX 8 AA8 THR A 178 GLU A 182 5 5
HELIX 9 AA9 THR A 186 HIS A 200 1 15
HELIX 10 AB1 SER A 208 THR A 215 1 8
HELIX 11 AB2 SER A 217 TYR A 223 1 7
HELIX 12 AB3 SER A 227 LEU A 240 1 14
HELIX 13 AB4 LEU A 241 GLU A 243 5 3
HELIX 14 AB5 THR A 253 ALA A 270 1 18
HELIX 15 AB6 THR A 271 SER A 274 5 4
HELIX 16 AB7 LYS A 275 THR A 289 1 15
HELIX 17 AB8 ASN A 302 LEU A 319 1 18
HELIX 18 AB9 SER A 320 LYS A 324 5 5
HELIX 19 AC1 PRO A 325 ARG A 350 1 26
HELIX 20 AC2 ASP A 359 ALA A 363 5 5
HELIX 21 AC3 SER A 364 ILE A 376 1 13
HELIX 22 AC4 ILE A 376 VAL A 388 1 13
HELIX 23 AC5 ALA A 392 THR A 409 1 18
HELIX 24 AC6 ASP B 90 ASP B 98 1 9
HELIX 25 AC7 VAL B 99 LYS B 101 5 3
HELIX 26 AC8 HIS B 105 SER B 113 1 9
HELIX 27 AC9 ARG B 116 ARG B 129 1 14
HELIX 28 AD1 ASP B 130 LYS B 136 1 7
HELIX 29 AD2 PRO B 138 HIS B 152 1 15
HELIX 30 AD3 ASN B 161 SER B 177 1 17
HELIX 31 AD4 THR B 178 GLU B 182 5 5
HELIX 32 AD5 THR B 186 HIS B 200 1 15
HELIX 33 AD6 SER B 208 THR B 215 1 8
HELIX 34 AD7 SER B 217 TYR B 223 1 7
HELIX 35 AD8 SER B 227 LEU B 240 1 14
HELIX 36 AD9 LEU B 241 GLU B 243 5 3
HELIX 37 AE1 THR B 253 ALA B 270 1 18
HELIX 38 AE2 THR B 271 SER B 274 5 4
HELIX 39 AE3 LYS B 275 THR B 289 1 15
HELIX 40 AE4 ASN B 302 LEU B 319 1 18
HELIX 41 AE5 SER B 320 LYS B 324 5 5
HELIX 42 AE6 PRO B 325 ARG B 350 1 26
HELIX 43 AE7 SER B 364 ILE B 376 1 13
HELIX 44 AE8 ILE B 376 VAL B 388 1 13
HELIX 45 AE9 ALA B 392 THR B 409 1 18
HELIX 46 AF1 GLU C 89 GLU C 97 1 9
HELIX 47 AF2 ASP C 98 LYS C 101 5 4
HELIX 48 AF3 HIS C 105 SER C 113 1 9
HELIX 49 AF4 ARG C 116 ARG C 129 1 14
HELIX 50 AF5 ASP C 130 LYS C 136 1 7
HELIX 51 AF6 PRO C 138 HIS C 152 1 15
HELIX 52 AF7 ASN C 161 SER C 177 1 17
HELIX 53 AF8 THR C 178 GLU C 182 5 5
HELIX 54 AF9 THR C 186 HIS C 200 1 15
HELIX 55 AG1 SER C 208 THR C 215 1 8
HELIX 56 AG2 SER C 217 TYR C 223 1 7
HELIX 57 AG3 SER C 227 LEU C 240 1 14
HELIX 58 AG4 LEU C 241 GLU C 243 5 3
HELIX 59 AG5 THR C 253 ALA C 270 1 18
HELIX 60 AG6 THR C 271 SER C 274 5 4
HELIX 61 AG7 LYS C 275 THR C 289 1 15
HELIX 62 AG8 ASN C 302 LEU C 319 1 18
HELIX 63 AG9 SER C 320 LYS C 324 5 5
HELIX 64 AH1 PRO C 325 ARG C 350 1 26
HELIX 65 AH2 SER C 364 ILE C 376 1 13
HELIX 66 AH3 ILE C 376 VAL C 388 1 13
HELIX 67 AH4 ALA C 392 THR C 409 1 18
HELIX 68 AH5 GLU D 89 GLU D 97 1 9
HELIX 69 AH6 HIS D 105 SER D 113 1 9
HELIX 70 AH7 ARG D 116 ARG D 129 1 14
HELIX 71 AH8 ASP D 130 LYS D 136 1 7
HELIX 72 AH9 PRO D 138 HIS D 152 1 15
HELIX 73 AI1 ASN D 161 SER D 177 1 17
HELIX 74 AI2 THR D 178 GLU D 182 5 5
HELIX 75 AI3 THR D 186 HIS D 200 1 15
HELIX 76 AI4 SER D 208 THR D 215 1 8
HELIX 77 AI5 SER D 217 TYR D 223 1 7
HELIX 78 AI6 SER D 227 LEU D 240 1 14
HELIX 79 AI7 LEU D 241 GLU D 243 5 3
HELIX 80 AI8 THR D 253 ALA D 270 1 18
HELIX 81 AI9 THR D 271 SER D 274 5 4
HELIX 82 AJ1 LYS D 275 THR D 289 1 15
HELIX 83 AJ2 ASN D 302 LEU D 319 1 18
HELIX 84 AJ3 SER D 320 LYS D 324 5 5
HELIX 85 AJ4 PRO D 325 ARG D 350 1 26
HELIX 86 AJ5 SER D 364 ILE D 376 1 13
HELIX 87 AJ6 ILE D 376 VAL D 388 1 13
HELIX 88 AJ7 ALA D 392 SER D 408 1 17
SHEET 1 AA1 2 LYS C 291 VAL C 292 0
SHEET 2 AA1 2 LEU C 298 LEU C 299 -1 O LEU C 299 N LYS C 291
LINK NE2 HIS A 164 ZN ZN A 501 1555 1555 2.22
LINK NE2 HIS A 200 ZN ZN A 501 1555 1555 2.23
LINK OD2 ASP A 201 ZN ZN A 501 1555 1555 2.10
LINK OD1 ASP A 201 MG MG A 502 1555 1555 2.00
LINK OD1 ASP A 318 ZN ZN A 501 1555 1555 2.24
LINK ZN ZN A 501 O HOH A 626 1555 1555 2.03
LINK ZN ZN A 501 O HOH A 649 1555 1555 2.37
LINK MG MG A 502 O HOH A 613 1555 1555 2.31
LINK MG MG A 502 O HOH A 626 1555 1555 2.07
LINK MG MG A 502 O HOH A 628 1555 1555 2.24
LINK MG MG A 502 O HOH A 688 1555 1555 2.13
LINK MG MG A 502 O HOH A 717 1555 1555 2.08
LINK NE2 HIS B 164 ZN ZN B 501 1555 1555 2.17
LINK NE2 HIS B 200 ZN ZN B 501 1555 1555 2.34
LINK OD2 ASP B 201 ZN ZN B 501 1555 1555 2.25
LINK OD1 ASP B 201 MG MG B 502 1555 1555 1.97
LINK OD1 ASP B 318 ZN ZN B 501 1555 1555 2.28
LINK ZN ZN B 501 O HOH B 626 1555 1555 2.01
LINK ZN ZN B 501 O HOH B 673 1555 1555 2.23
LINK MG MG B 502 O HOH B 614 1555 1555 2.12
LINK MG MG B 502 O HOH B 626 1555 1555 2.20
LINK MG MG B 502 O HOH B 646 1555 1555 2.17
LINK MG MG B 502 O HOH B 654 1555 1555 1.96
LINK MG MG B 502 O HOH B 658 1555 1555 2.02
LINK NE2 HIS C 164 ZN ZN C 501 1555 1555 2.29
LINK NE2 HIS C 200 ZN ZN C 501 1555 1555 2.26
LINK OD2 ASP C 201 ZN ZN C 501 1555 1555 2.33
LINK OD1 ASP C 201 MG MG C 502 1555 1555 2.02
LINK OD1 ASP C 318 ZN ZN C 501 1555 1555 2.18
LINK ZN ZN C 501 O HOH C 625 1555 1555 2.15
LINK ZN ZN C 501 O HOH C 658 1555 1555 2.16
LINK MG MG C 502 O HOH C 607 1555 1555 2.05
LINK MG MG C 502 O HOH C 625 1555 1555 2.09
LINK MG MG C 502 O HOH C 645 1555 1555 2.05
LINK MG MG C 502 O HOH C 657 1555 1555 2.18
LINK MG MG C 502 O HOH C 675 1555 1555 2.01
LINK NE2 HIS D 164 ZN ZN D 501 1555 1555 2.31
LINK NE2 HIS D 200 ZN ZN D 501 1555 1555 2.16
LINK OD2 ASP D 201 ZN ZN D 501 1555 1555 2.13
LINK OD1 ASP D 201 MG MG D 502 1555 1555 2.07
LINK OD1 ASP D 318 ZN ZN D 501 1555 1555 2.24
LINK ZN ZN D 501 O HOH D 617 1555 1555 2.35
LINK ZN ZN D 501 O HOH D 654 1555 1555 2.37
LINK MG MG D 502 O HOH D 617 1555 1555 2.04
LINK MG MG D 502 O HOH D 652 1555 1555 2.03
LINK MG MG D 502 O HOH D 671 1555 1555 2.24
LINK MG MG D 502 O HOH D 689 1555 1555 2.19
LINK MG MG D 502 O HOH D 709 1555 1555 1.95
CISPEP 1 HIS A 389 PRO A 390 0 1.62
CISPEP 2 HIS B 389 PRO B 390 0 -5.80
CISPEP 3 HIS C 389 PRO C 390 0 3.05
CISPEP 4 HIS D 389 PRO D 390 0 -2.50
SITE 1 AC1 6 HIS A 164 HIS A 200 ASP A 201 ASP A 318
SITE 2 AC1 6 HOH A 626 HOH A 649
SITE 1 AC2 6 ASP A 201 HOH A 613 HOH A 626 HOH A 628
SITE 2 AC2 6 HOH A 688 HOH A 717
SITE 1 AC3 5 SER A 208 PRO A 356 CYS A 358 E6Z A 517
SITE 2 AC3 5 HOH A 618
SITE 1 AC4 5 ASN A 115 ALA A 155 ASN A 161 ASN A 162
SITE 2 AC4 5 ARG A 335
SITE 1 AC5 5 THR A 186 GLU A 189 SER A 259 MET A 263
SITE 2 AC5 5 EDO A 512
SITE 1 AC6 6 GLU A 218 HOH A 722 HIS C 152 LYS C 239
SITE 2 AC6 6 LEU C 240 HOH C 614
SITE 1 AC7 4 LEU A 175 THR A 178 TRP A 384 ASP A 391
SITE 1 AC8 3 THR A 134 LYS A 136 EDO A 509
SITE 1 AC9 5 THR A 134 PHE A 135 ASN A 251 GLN A 256
SITE 2 AC9 5 EDO A 508
SITE 1 AD1 4 HIS A 152 GLU A 243 SER C 217 ARG C 350
SITE 1 AD2 6 PHE A 238 PHE A 249 ARG A 257 ARG A 261
SITE 2 AD2 6 HOH A 633 HOH A 642
SITE 1 AD3 6 SER A 259 LYS A 262 TYR A 303 EDO A 505
SITE 2 AD3 6 EDO A 514 HOH A 660
SITE 1 AD4 7 ARG A 116 GLU A 150 ASP A 151 TYR A 153
SITE 2 AD4 7 HOH A 604 HOH A 719 EDO C 510
SITE 1 AD5 3 EDO A 512 HOH A 602 HOH A 721
SITE 1 AD6 9 HIS A 105 VAL A 106 PHE A 107 ARG A 108
SITE 2 AD6 9 GLU A 111 GLN A 327 LEU A 328 GLN A 331
SITE 3 AD6 9 HOH A 691
SITE 1 AD7 5 LYS A 262 ASP A 266 HOH A 700 HOH B 619
SITE 2 AD7 5 HOH B 655
SITE 1 AD8 15 MET A 273 ASP A 318 LEU A 319 THR A 333
SITE 2 AD8 15 ILE A 336 MET A 337 MET A 357 SER A 368
SITE 3 AD8 15 GLN A 369 PHE A 372 ILE A 376 EDO A 503
SITE 4 AD8 15 HOH A 618 HOH A 693 HOH A 717
SITE 1 AD9 6 HIS B 164 HIS B 200 ASP B 201 ASP B 318
SITE 2 AD9 6 HOH B 626 HOH B 673
SITE 1 AE1 6 ASP B 201 HOH B 614 HOH B 626 HOH B 646
SITE 2 AE1 6 HOH B 654 HOH B 658
SITE 1 AE2 3 SER B 208 PRO B 356 HOH B 630
SITE 1 AE3 5 GLU B 218 EDO B 507 HOH B 632 MET C 222
SITE 2 AE3 5 LYS D 239
SITE 1 AE4 4 ASN B 115 ALA B 155 ASN B 162 ARG B 335
SITE 1 AE5 6 PHE B 211 ASN B 214 GLU B 347 MET B 352
SITE 2 AE5 6 GLU B 353 SER B 355
SITE 1 AE6 3 GLU B 218 EDO B 504 LYS D 239
SITE 1 AE7 8 HIS B 105 VAL B 106 PHE B 107 ARG B 108
SITE 2 AE7 8 GLU B 111 GLN B 327 LEU B 328 GLN B 331
SITE 1 AE8 11 MET B 273 ASP B 318 ILE B 336 MET B 337
SITE 2 AE8 11 MET B 357 VAL B 365 SER B 368 GLN B 369
SITE 3 AE8 11 PHE B 372 HOH B 671 HOH B 673
SITE 1 AE9 6 HIS C 164 HIS C 200 ASP C 201 ASP C 318
SITE 2 AE9 6 HOH C 625 HOH C 658
SITE 1 AF1 6 ASP C 201 HOH C 607 HOH C 625 HOH C 645
SITE 2 AF1 6 HOH C 657 HOH C 675
SITE 1 AF2 4 PHE C 249 ARG C 257 HOH C 605 HOH C 653
SITE 1 AF3 4 LEU C 175 THR C 178 TRP C 384 ALA C 392
SITE 1 AF4 3 LYS A 239 MET B 222 GLU C 218
SITE 1 AF5 3 THR C 148 HIS C 152 GLU C 243
SITE 1 AF6 5 ASN C 115 ARG C 116 GLU C 150 ASP C 151
SITE 2 AF6 5 TYR C 153
SITE 1 AF7 3 PRO C 356 E6Z C 512 HOH C 638
SITE 1 AF8 3 LYS C 262 ASP C 266 ASP D 225
SITE 1 AF9 5 GLY A 114 ASN A 115 EDO A 513 ARG C 342
SITE 2 AF9 5 HOH C 619
SITE 1 AG1 8 HIS C 105 VAL C 106 PHE C 107 ARG C 108
SITE 2 AG1 8 GLU C 111 GLN C 327 LEU C 328 GLN C 331
SITE 1 AG2 12 HIS C 160 MET C 273 LEU C 319 ILE C 336
SITE 2 AG2 12 MET C 337 MET C 357 SER C 368 GLN C 369
SITE 3 AG2 12 PHE C 372 EDO C 508 HOH C 638 HOH C 656
SITE 1 AG3 3 ASN C 214 GLU C 353 GLN D 258
SITE 1 AG4 6 HIS D 164 HIS D 200 ASP D 201 ASP D 318
SITE 2 AG4 6 HOH D 617 HOH D 654
SITE 1 AG5 6 ASP D 201 HOH D 617 HOH D 652 HOH D 671
SITE 2 AG5 6 HOH D 689 HOH D 709
SITE 1 AG6 4 SER D 294 SER D 295 HOH D 609 HOH D 660
SITE 1 AG7 4 PHE D 340 PRO D 356 CYS D 358 E6Z D 516
SITE 1 AG8 5 PHE D 238 ARG D 257 ARG D 261 HOH D 647
SITE 2 AG8 5 HOH D 672
SITE 1 AG9 4 HOH C 621 LYS D 262 ASP D 266 HOH D 657
SITE 1 AH1 4 ASN D 115 ALA D 155 ASN D 161 ASN D 162
SITE 1 AH2 6 LEU D 175 THR D 178 TRP D 384 VAL D 388
SITE 2 AH2 6 ASP D 391 HOH D 662
SITE 1 AH3 6 GLN D 250 LEU D 252 THR D 253 ARG D 257
SITE 2 AH3 6 HOH D 632 HOH D 728
SITE 1 AH4 4 ARG D 129 LEU D 131 ASP D 187 ILE D 190
SITE 1 AH5 1 GLU D 182
SITE 1 AH6 1 GLN D 393
SITE 1 AH7 1 ASP D 98
SITE 1 AH8 7 ASP C 394 HIS D 105 VAL D 106 PHE D 107
SITE 2 AH8 7 ARG D 108 LEU D 328 GLN D 331
SITE 1 AH9 2 HIS D 152 GLU D 243
SITE 1 AI1 10 MET D 273 ASP D 318 LEU D 319 ILE D 336
SITE 2 AI1 10 MET D 337 MET D 357 SER D 368 GLN D 369
SITE 3 AI1 10 PHE D 372 EDO D 504
CRYST1 99.140 111.430 160.060 90.00 90.00 90.00 P 21 21 21 16
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 0.010087 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008974 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006248 0.00000
(ATOM LINES ARE NOT SHOWN.)
END