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HEADER HYDROLASE/HYDROLASE INHIBITOR 25-OCT-10 3PE6
TITLE CRYSTAL STRUCTURE OF A SOLUBLE FORM OF HUMAN MGLL IN COMPLEX WITH AN
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SHORT FORM OF MGLL (UNP RESIDUES 11 TO 313);
COMPND 5 SYNONYM: MGLL PROTEIN, ISOFORM CRA_B, CDNA, FLJ96595, HOMO SAPIENS
COMPND 6 MONOGLYCERIDE LIPASE (MGLL), MRNA;
COMPND 7 EC: 3.1.1.23;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MGLL, HCG_40840;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS ALPHA-BETA HYDROLASE FOLD, LIPASE, 2-ARACHIDONYL-GLYCEROL, MEMBRANE
KEYWDS 2 ASSOCIATED, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SCHUBERT,C.SCHALK-HIH
REVDAT 1 02-MAR-11 3PE6 0
JRNL AUTH C.SCHALK-HIHI,C.SCHUBERT,R.ALEXANDER,S.BAYOUMY,J.C.CLEMENTE,
JRNL AUTH 2 I.DECKMAN,R.L.DESJARLAIS,K.C.DZORDZORME,C.M.FLORES,
JRNL AUTH 3 B.GRASBERGER,J.K.KRANZ,F.LEWANDOWSKI,L.LIU,H.MA,D.MAGUIRE,
JRNL AUTH 4 M.J.MACIELAG,M.E.MCDONNELL,T.M.HAARLANDER,R.MILLER,
JRNL AUTH 5 C.MILLIGAN,C.REYNOLDS,L.C.KUO
JRNL TITL CRYSTAL STRUCTURE OF A SOLUBLE FORM OF HUMAN MONOGLYCERIDE
JRNL TITL 2 LIPASE IN COMPLEX WITH AN INHIBITOR AT 1.35 A RESOLUTION.
JRNL REF PROTEIN SCI. 2011
JRNL REFN ESSN 1469-896X
JRNL PMID 21308848
JRNL DOI 10.1002/PRO.596
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 71433
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.115
REMARK 3 R VALUE (WORKING SET) : 0.114
REMARK 3 FREE R VALUE : 0.147
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.510
REMARK 3 FREE R VALUE TEST SET COUNT : 1794
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 30.4282 - 3.1732 0.92 5823 149 0.1448 0.1572
REMARK 3 2 3.1732 - 2.5190 1.00 6081 157 0.1059 0.1288
REMARK 3 3 2.5190 - 2.2007 0.99 6004 154 0.0926 0.1135
REMARK 3 4 2.2007 - 1.9996 0.99 5980 154 0.0871 0.1208
REMARK 3 5 1.9996 - 1.8563 0.98 5904 152 0.0874 0.1350
REMARK 3 6 1.8563 - 1.7468 0.97 5851 152 0.0845 0.1289
REMARK 3 7 1.7468 - 1.6594 0.96 5747 143 0.0842 0.1077
REMARK 3 8 1.6594 - 1.5871 0.92 5463 140 0.0880 0.1353
REMARK 3 9 1.5871 - 1.5260 0.86 5166 130 0.0969 0.1431
REMARK 3 10 1.5260 - 1.4734 0.82 4923 128 0.1120 0.1883
REMARK 3 11 1.4734 - 1.4273 0.79 4695 123 0.1352 0.1938
REMARK 3 12 1.4273 - 1.3865 0.72 4306 112 0.1643 0.2418
REMARK 3 13 1.3865 - 1.3500 0.63 3696 100 0.2193 0.3219
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 : 0.46
REMARK 3 B_SOL : 66.86
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.57860
REMARK 3 B22 (A**2) : -2.39610
REMARK 3 B33 (A**2) : -0.76410
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 : 0.014 4904
REMARK 3 ANGLE : 1.435 8951
REMARK 3 CHIRALITY : 0.104 383
REMARK 3 PLANARITY : 0.011 742
REMARK 3 DIHEDRAL : 17.877 1279
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 3PE6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062268.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79919
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 34.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.760
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: PDB ENTRY 1A8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME5000 MES GLUCOPYRANOSIDE, PH
REMARK 280 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 30.30100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.30100
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.97350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.07250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.97350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.07250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.30100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.97350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.07250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 30.30100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.97350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 64.07250
REMARK 290 SMTRY3 8 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: 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 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 A 475 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 THR A 296
REMARK 465 ALA A 297
REMARK 465 GLY A 298
REMARK 465 THR A 299
REMARK 465 ALA A 300
REMARK 465 SER A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
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 HH21 ARG A 240 O HOH A 423 1.65
REMARK 500 HD2 HIS A 94 O HOH A 346 1.75
REMARK 500 OE1 GLN A 108 HE2 HIS A 138 1.83
REMARK 500 H GLY A 236 O HOH A 413 1.83
REMARK 500 O ALA A 164 H ASN A 168 1.87
REMARK 500 HH22 ARG A 135 O HOH A 590 1.87
REMARK 500 O ALA A 254 HZ1 LYS A 259 1.89
REMARK 500 OG SER A 237 H GLY A 266 1.89
REMARK 500 O ASP A 76 HG SER A 83 1.90
REMARK 500 O GLY A 85 HH22 ARG A 87 1.90
REMARK 500 HH11 ARG A 240 O HOH A 336 1.91
REMARK 500 HD1 HIS A 284 O HOH A 513 1.92
REMARK 500 O SER A 83 HH21 ARG A 87 1.92
REMARK 500 H SER A 55 OD1 ASP A 76 1.92
REMARK 500 O PRO A 276 H ASN A 280 1.93
REMARK 500 HE2 HIS A 54 OD2 ASP A 197 1.93
REMARK 500 O LEU A 22 H LEU A 30 1.93
REMARK 500 O ALA A 216 H VAL A 220 1.93
REMARK 500 OD2 ASP A 239 HD1 HIS A 269 1.93
REMARK 500 HH11 ARG A 57 OD2 ASP A 197 1.94
REMARK 500 HD1 HIS A 77 O HOH A 361 1.94
REMARK 500 H SER A 48 O LEU A 119 1.94
REMARK 500 HE ARG A 9 O HOH A 623 1.95
REMARK 500 O SER A 281 H GLU A 285 1.96
REMARK 500 O PHE A 159 H ALA A 163 1.96
REMARK 500 H LYS A 206 O HOH A 380 1.97
REMARK 500 H LYS A 42 O ASP A 69 1.97
REMARK 500 O VAL A 100 H VAL A 104 1.98
REMARK 500 HE ARG A 57 O HOH A 406 1.98
REMARK 500 O THR A 10 H SER A 13 1.98
REMARK 500 HH21 ARG A 202 O HOH A 647 1.98
REMARK 500 H THR A 10 O ILE A 14 1.98
REMARK 500 H ALA A 51 O01 ZYH A 304 1.99
REMARK 500 O THR A 10 H SER A 13 1.99
REMARK 500 H ARG A 202 O HOH A 525 1.99
REMARK 500 O MET A 251 HZ3 LYS A 259 1.99
REMARK 500 O VAL A 116 H ALA A 140 1.99
REMARK 500 OD1 ASP A 197 H LEU A 199 2.00
REMARK 500 H GLY A 50 OE2 GLU A 53 2.00
REMARK 500 O ASN A 287 H SER A 291 2.00
REMARK 500 HZ2 LYS A 262 O HOH A 318 2.00
REMARK 500 HH22 ARG A 33 O HOH A 363 2.00
REMARK 500 OD2 ASP A 92 HH12 ARG A 219 2.00
REMARK 500 O VAL A 278 H VAL A 282 2.00
REMARK 500 H SER A 146 O LEU A 234 2.00
REMARK 500 HH21 ARG A 8 OE1 GLU A 84 2.00
REMARK 500 H ILE A 179 O HOH A 379 2.01
REMARK 500 O TYR A 29 H GLU A 84 2.01
REMARK 500 H GLY A 39 O HOH A 524 2.01
REMARK 500 OD2 ASP A 76 H GLN A 82 2.01
REMARK 500
REMARK 500 THIS ENTRY HAS 280 CLOSE CONTACTS
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 H GLU A 265 O HOH A 448 4555 1.93
REMARK 500 HH11 ARG A 135 O HOH A 604 6455 1.98
REMARK 500 O LEU A 261 H LEU A 261 4555 1.98
REMARK 500 HH11 ARG A 8 O HOH A 498 6455 2.02
REMARK 500 HH11 ARG A 8 O HOH A 498 6455 2.05
REMARK 500 H LYS A 259 O HOH A 369 4555 2.07
REMARK 500 H VAL A 23 OG SER A 196 6455 2.07
REMARK 500 HE21 GLN A 102 O SER A 196 6455 2.09
REMARK 500 HH11 ARG A 202 O HOH A 426 6454 2.10
REMARK 500 O HOH A 615 O HOH A 627 3554 2.11
REMARK 500 HG21 THR A 189 O HOH A 664 6454 2.16
REMARK 500 HG23 THR A 189 O HOH A 664 6454 2.16
REMARK 500 H VAL A 23 OG SER A 196 6455 2.18
REMARK 500 HZ1 LYS A 262 O HOH A 585 4555 2.19
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 ARG A 8 CG - CD - NE ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 LYS A 109 CD - CE - NZ ANGL. DEV. = 15.2 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 SER A 13 13.84 87.81
REMARK 500 GLU A 53 -152.58 -118.85
REMARK 500 SER A 122 -128.11 62.79
REMARK 500 VAL A 170 56.73 35.26
REMARK 500 GLU A 274 -166.27 -100.90
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 339 DISTANCE = 8.44 ANGSTROMS
REMARK 525 HOH A 351 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A 497 DISTANCE = 5.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYH A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JW8 RELATED DB: PDB
REMARK 900 RELATED ID: 3JWE RELATED DB: PDB
REMARK 900 RELATED ID: 3HJU RELATED DB: PDB
DBREF 3PE6 A 1 303 UNP Q6IBG9 Q6IBG9_HUMAN 11 313
SEQADV 3PE6 ALA A 36 UNP Q6IBG9 LYS 46 ENGINEERED MUTATION
SEQADV 3PE6 SER A 169 UNP Q6IBG9 LEU 179 ENGINEERED MUTATION
SEQADV 3PE6 SER A 176 UNP Q6IBG9 LEU 186 ENGINEERED MUTATION
SEQRES 1 A 303 MET PRO GLU GLU SER SER PRO ARG ARG THR PRO GLN SER
SEQRES 2 A 303 ILE PRO TYR GLN ASP LEU PRO HIS LEU VAL ASN ALA ASP
SEQRES 3 A 303 GLY GLN TYR LEU PHE CYS ARG TYR TRP ALA PRO THR GLY
SEQRES 4 A 303 THR PRO LYS ALA LEU ILE PHE VAL SER HIS GLY ALA GLY
SEQRES 5 A 303 GLU HIS SER GLY ARG TYR GLU GLU LEU ALA ARG MET LEU
SEQRES 6 A 303 MET GLY LEU ASP LEU LEU VAL PHE ALA HIS ASP HIS VAL
SEQRES 7 A 303 GLY HIS GLY GLN SER GLU GLY GLU ARG MET VAL VAL SER
SEQRES 8 A 303 ASP PHE HIS VAL PHE VAL ARG ASP VAL LEU GLN HIS VAL
SEQRES 9 A 303 ASP SER MET GLN LYS ASP TYR PRO GLY LEU PRO VAL PHE
SEQRES 10 A 303 LEU LEU GLY HIS SER MET GLY GLY ALA ILE ALA ILE LEU
SEQRES 11 A 303 THR ALA ALA GLU ARG PRO GLY HIS PHE ALA GLY MET VAL
SEQRES 12 A 303 LEU ILE SER PRO LEU VAL LEU ALA ASN PRO GLU SER ALA
SEQRES 13 A 303 THR THR PHE LYS VAL LEU ALA ALA LYS VAL LEU ASN SER
SEQRES 14 A 303 VAL LEU PRO ASN LEU SER SER GLY PRO ILE ASP SER SER
SEQRES 15 A 303 VAL LEU SER ARG ASN LYS THR GLU VAL ASP ILE TYR ASN
SEQRES 16 A 303 SER ASP PRO LEU ILE CYS ARG ALA GLY LEU LYS VAL CYS
SEQRES 17 A 303 PHE GLY ILE GLN LEU LEU ASN ALA VAL SER ARG VAL GLU
SEQRES 18 A 303 ARG ALA LEU PRO LYS LEU THR VAL PRO PHE LEU LEU LEU
SEQRES 19 A 303 GLN GLY SER ALA ASP ARG LEU CYS ASP SER LYS GLY ALA
SEQRES 20 A 303 TYR LEU LEU MET GLU LEU ALA LYS SER GLN ASP LYS THR
SEQRES 21 A 303 LEU LYS ILE TYR GLU GLY ALA TYR HIS VAL LEU HIS LYS
SEQRES 22 A 303 GLU LEU PRO GLU VAL THR ASN SER VAL PHE HIS GLU ILE
SEQRES 23 A 303 ASN MET TRP VAL SER GLN ARG THR ALA THR ALA GLY THR
SEQRES 24 A 303 ALA SER PRO PRO
HET ZYH A 304 63
HETNAM ZYH (2-CYCLOHEXYL-1,3-BENZOXAZOL-6-YL){3-[4-(PYRIMIDIN-2-
HETNAM 2 ZYH YL)PIPERAZIN-1-YL]AZETIDIN-1-YL}METHANONE
FORMUL 2 ZYH C25 H30 N6 O2
FORMUL 3 HOH *360(H2 O)
HELIX 1 1 PRO A 15 LEU A 19 5 5
HELIX 2 2 HIS A 54 ARG A 57 5 4
HELIX 3 3 TYR A 58 LEU A 68 1 11
HELIX 4 4 PHE A 93 TYR A 111 1 19
HELIX 5 5 SER A 122 ARG A 135 1 14
HELIX 6 6 ASN A 152 SER A 169 1 18
HELIX 7 7 ASP A 180 LEU A 184 5 5
HELIX 8 8 ASN A 187 SER A 196 1 10
HELIX 9 9 LYS A 206 LEU A 224 1 19
HELIX 10 10 PRO A 225 LEU A 227 5 3
HELIX 11 11 ASP A 243 ALA A 254 1 12
HELIX 12 12 VAL A 270 GLU A 274 5 5
HELIX 13 13 LEU A 275 ARG A 293 1 19
SHEET 1 A 8 HIS A 21 VAL A 23 0
SHEET 2 A 8 TYR A 29 TRP A 35 -1 O LEU A 30 N LEU A 22
SHEET 3 A 8 LEU A 70 HIS A 75 -1 O VAL A 72 N TRP A 35
SHEET 4 A 8 ALA A 43 SER A 48 1 N ILE A 45 O PHE A 73
SHEET 5 A 8 VAL A 116 HIS A 121 1 O LEU A 119 N SER A 48
SHEET 6 A 8 GLY A 141 ILE A 145 1 O ILE A 145 N GLY A 120
SHEET 7 A 8 PHE A 231 GLY A 236 1 O LEU A 232 N LEU A 144
SHEET 8 A 8 LYS A 259 TYR A 264 1 O THR A 260 N LEU A 233
SITE 1 AC1 14 GLY A 50 ALA A 51 GLU A 53 HIS A 121
SITE 2 AC1 14 SER A 122 MET A 123 SER A 181 LEU A 184
SITE 3 AC1 14 TYR A 194 LEU A 241 VAL A 270 HOH A 365
SITE 4 AC1 14 HOH A 406 HOH A 441
CRYST1 93.947 128.145 60.602 90.00 90.00 90.00 C 2 2 21 8
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 0.010644 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016501 0.00000
TER 4760 ALA A 295
MASTER 409 0 1 13 8 0 4 6 2631 1 63 24
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