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HEADER HYDROLASE 13-NOV-09 3KOO
TITLE CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SOLUBLE EPOXIDE HYDROLASE, SEH, EPOXIDE HYDRATASE, CYTOSOLIC
COMPND 5 EPOXIDE HYDROLASE, CEH;
COMPND 6 EC: 3.3.2.10;
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: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.FARROW
REVDAT 1 28-APR-10 3KOO 0
JRNL AUTH A.B.ELDRUP,F.SOLEYMANZADEH,N.A.FARROW,A.KUKULKA,
JRNL AUTH 2 S.DE LOMBAERT
JRNL TITL OPTIMIZATION OF PIPERIDYL-UREAS AS INHIBITORS OF SOLUBLE
JRNL TITL 2 EPOXIDE HYDROLASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 571 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 19969453
JRNL DOI 10.1016/J.BMCL.2009.11.091
REMARK 2
REMARK 2 RESOLUTION. 2.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 14809
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 736
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.2100 - 4.7710 0.97 3117 175 0.1910 0.2550
REMARK 3 2 4.7710 - 3.7870 0.88 2644 146 0.2230 0.3480
REMARK 3 3 3.7870 - 3.3090 0.97 2858 147 0.2130 0.3290
REMARK 3 4 3.3090 - 3.0060 0.95 2804 140 0.2350 0.3540
REMARK 3 5 3.0060 - 2.7910 0.91 2650 128 0.2620 0.3640
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 58.36
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.53800
REMARK 3 B22 (A**2) : 1.53800
REMARK 3 B33 (A**2) : -3.07600
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 4449
REMARK 3 ANGLE : 1.326 6028
REMARK 3 CHIRALITY : 0.079 657
REMARK 3 PLANARITY : 0.006 775
REMARK 3 DIHEDRAL : 21.613 1657
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KOO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15463
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 36% PEG 2250,
REMARK 280 0.1M TRIS PH 8.4, 0.6 UM B-HEXADECYL MALTOSIDE, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 161.67733
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 80.83867
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 121.25800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.41933
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 202.09667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 161.67733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 80.83867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 40.41933
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 121.25800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 202.09667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 91.76500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 121.25800
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 MET A 1
REMARK 465 THR A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
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 A 205 OG1 THR A 208 2.16
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 PRO A 17 C - N - CA ANGL. DEV. = -10.0 DEGREES
REMARK 500 PRO A 302 C - N - CA ANGL. DEV. = 10.0 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 LEU A 10 -82.57 -74.59
REMARK 500 ARG A 34 130.03 -28.19
REMARK 500 PRO A 83 155.03 -41.14
REMARK 500 ASN A 85 36.47 -95.50
REMARK 500 ARG A 130 170.22 -55.72
REMARK 500 LYS A 144 -55.95 -13.78
REMARK 500 PRO A 161 50.44 -105.46
REMARK 500 GLN A 204 -88.08 -139.59
REMARK 500 ALA A 226 100.71 -57.86
REMARK 500 SER A 231 -158.74 -97.35
REMARK 500 PRO A 234 -37.71 -33.04
REMARK 500 ASP A 236 8.81 -66.69
REMARK 500 GLU A 269 -141.63 -127.56
REMARK 500 SER A 273 0.40 -65.41
REMARK 500 ALA A 284 -17.28 -48.60
REMARK 500 LYS A 294 127.93 -37.14
REMARK 500 GLU A 311 -62.03 -18.00
REMARK 500 ASP A 335 -135.84 57.53
REMARK 500 TYR A 348 45.89 -141.86
REMARK 500 ASN A 359 -55.66 75.45
REMARK 500 SER A 374 10.41 -65.83
REMARK 500 ASN A 378 78.67 59.49
REMARK 500 VAL A 380 3.99 -62.10
REMARK 500 GLN A 388 -52.90 -11.30
REMARK 500 ALA A 411 172.30 -59.73
REMARK 500 SER A 415 148.35 -38.24
REMARK 500 VAL A 416 20.18 -142.71
REMARK 500 MET A 419 20.67 -70.15
REMARK 500 PRO A 433 -164.89 -64.45
REMARK 500 PRO A 436 136.76 -37.53
REMARK 500 LYS A 456 -75.50 -73.18
REMARK 500 MET A 469 -58.01 -168.20
REMARK 500 LYS A 495 46.72 -96.48
REMARK 500 GLN A 505 -35.99 -36.52
REMARK 500 HIS A 513 51.19 -102.50
REMARK 500 LYS A 530 52.05 -148.46
REMARK 500 ALA A 546 -101.30 -81.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 291 ASP A 292 147.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU A 16 25.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 578 DISTANCE = 8.46 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 24D A 556
DBREF 3KOO A 1 555 UNP P34913 HYES_HUMAN 1 555
SEQRES 1 A 555 MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL
SEQRES 2 A 555 LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR
SEQRES 3 A 555 GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP
SEQRES 4 A 555 ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG
SEQRES 5 A 555 LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO
SEQRES 6 A 555 LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA
SEQRES 7 A 555 LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE
SEQRES 8 A 555 PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO
SEQRES 9 A 555 MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE
SEQRES 10 A 555 THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG
SEQRES 11 A 555 ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU
SEQRES 12 A 555 LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 A 555 GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU
SEQRES 14 A 555 LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE
SEQRES 15 A 555 LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 A 555 LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR
SEQRES 17 A 555 ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU
SEQRES 18 A 555 LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO
SEQRES 19 A 555 SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG
SEQRES 20 A 555 VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA
SEQRES 21 A 555 VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 22 A 555 TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR
SEQRES 23 A 555 ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER
SEQRES 24 A 555 SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL
SEQRES 25 A 555 LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY
SEQRES 26 A 555 LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY
SEQRES 27 A 555 MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG
SEQRES 28 A 555 VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO
SEQRES 29 A 555 ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA
SEQRES 30 A 555 ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO
SEQRES 31 A 555 GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG
SEQRES 32 A 555 THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL
SEQRES 33 A 555 LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE
SEQRES 34 A 555 VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL
SEQRES 35 A 555 THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS
SEQRES 36 A 555 LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN
SEQRES 37 A 555 MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY
SEQRES 38 A 555 ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU
SEQRES 39 A 555 LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET
SEQRES 40 A 555 GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU
SEQRES 41 A 555 ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU
SEQRES 42 A 555 VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA
SEQRES 43 A 555 ARG ASN PRO PRO VAL VAL SER LYS MET
HET 24D A 556 25
HETNAM 24D N-(2,4-DICHLOROBENZYL)-4-(PYRIMIDIN-2-YLOXY)PIPERIDINE-
HETNAM 2 24D 1-CARBOXAMIDE
HETSYN 24D 4-(PYRIMIDIN-2-YLOXY)-PIPERIDINE-1-CARBOXYLIC ACID 2,4-
HETSYN 2 24D DICHLORO-BENZYLAMIDE
FORMUL 2 24D C17 H18 CL2 N4 O2
FORMUL 3 HOH *28(H2 O)
HELIX 1 1 ALA A 18 LEU A 30 1 13
HELIX 2 2 GLY A 35 GLN A 42 1 8
HELIX 3 3 LYS A 43 GLU A 47 5 5
HELIX 4 4 GLY A 48 LYS A 55 1 8
HELIX 5 5 THR A 59 ALA A 78 1 20
HELIX 6 6 SER A 87 ARG A 99 1 13
HELIX 7 7 ASN A 102 LYS A 115 1 14
HELIX 8 8 ARG A 130 GLU A 132 5 3
HELIX 9 9 ARG A 133 MET A 145 1 13
HELIX 10 10 SER A 153 GLY A 157 1 5
HELIX 11 11 GLU A 162 LYS A 174 1 13
HELIX 12 12 SER A 176 SER A 178 5 3
HELIX 13 13 ILE A 186 ASP A 195 1 10
HELIX 14 14 ASP A 205 GLY A 218 1 14
HELIX 15 15 ASN A 233 MET A 237 5 5
HELIX 16 16 SER A 270 ARG A 275 5 6
HELIX 17 17 TYR A 276 GLY A 285 1 10
HELIX 18 18 GLU A 304 TYR A 308 5 5
HELIX 19 19 CYS A 309 LYS A 323 1 15
HELIX 20 20 ASP A 335 TYR A 348 1 14
HELIX 21 21 LEU A 372 ALA A 377 1 6
HELIX 22 22 ASN A 378 VAL A 380 5 3
HELIX 23 23 PHE A 381 GLN A 388 1 8
HELIX 24 24 GLY A 391 ASN A 400 1 10
HELIX 25 25 ASN A 400 PHE A 409 1 10
HELIX 26 26 LYS A 421 GLY A 426 1 6
HELIX 27 27 THR A 443 GLY A 458 1 16
HELIX 28 28 PHE A 459 TRP A 465 1 7
HELIX 29 29 TYR A 466 ASN A 468 5 3
HELIX 30 30 MET A 469 SER A 479 1 11
HELIX 31 31 LEU A 480 ARG A 482 5 3
HELIX 32 32 VAL A 500 TRP A 510 5 11
HELIX 33 33 TRP A 525 LYS A 530 1 6
HELIX 34 34 LYS A 530 ALA A 546 1 17
SHEET 1 A 5 PHE A 149 GLU A 152 0
SHEET 2 A 5 THR A 118 THR A 123 1 N ILE A 121 O ILE A 151
SHEET 3 A 5 ALA A 5 PHE A 8 1 N PHE A 8 O ALA A 120
SHEET 4 A 5 VAL A 180 ASP A 184 1 O VAL A 181 N ALA A 5
SHEET 5 A 5 VAL A 199 LEU A 202 1 O ILE A 201 N PHE A 182
SHEET 1 B 8 HIS A 239 LYS A 245 0
SHEET 2 B 8 VAL A 248 LEU A 255 -1 O LEU A 250 N VAL A 242
SHEET 3 B 8 ARG A 287 ASP A 292 -1 O VAL A 288 N LEU A 255
SHEET 4 B 8 ALA A 260 CYS A 264 1 N VAL A 261 O ARG A 287
SHEET 5 B 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 B 8 VAL A 352 LEU A 358 1 O ALA A 356 N GLY A 333
SHEET 7 B 8 ALA A 488 ALA A 493 1 O LEU A 489 N SER A 357
SHEET 8 B 8 LEU A 514 ILE A 519 1 O GLY A 517 N MET A 490
CISPEP 1 LYS A 160 PRO A 161 0 8.65
CISPEP 2 PHE A 267 PRO A 268 0 -8.37
SITE 1 AC1 11 PHE A 267 ASP A 335 MET A 339 TYR A 383
SITE 2 AC1 11 GLN A 384 TYR A 466 PHE A 497 VAL A 498
SITE 3 AC1 11 LEU A 499 MET A 503 HIS A 524
CRYST1 91.765 91.765 242.516 90.00 90.00 120.00 P 65 2 2 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 0.010897 0.006292 0.000000 0.00000
SCALE2 0.000000 0.012583 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004123 0.00000
TER 4317 ASN A 548
MASTER 387 0 1 34 13 0 3 6 4369 1 25 43
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