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HEADER HYDROLASE 04-JAN-16 5HCU
TITLE CRYSTAL STRUCTURE OF MOUSE ACETYLCHOINESTERASE INHIBITED BY DFP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 32-571;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.H.TRAN,L.TONG
REVDAT 1 20-JAN-16 5HCU 0
SPRSDE 20-JAN-16 5HCU 5DTG
JRNL AUTH F.S.KATZ,S.PECIC,T.H.TRAN,I.TRAKHT,L.SCHNEIDER,Z.ZHU,
JRNL AUTH 2 L.TON-THAT,M.LUZAC,V.ZLATANIC,S.DAMERA,J.MACDONALD,
JRNL AUTH 3 D.W.LANDRY,L.TONG,M.N.STOJANOVIC
JRNL TITL DISCOVERY OF NEW CLASSES OF COMPOUNDS THAT REACTIVATE
JRNL TITL 2 ACETYLCHOLINESTERASE INHIBITED BY ORGANOPHOSPHATES.
JRNL REF CHEMBIOCHEM V. 16 2205 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 26350723
JRNL DOI 10.1002/CBIC.201500348
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 65006
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3968
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 46.2386 - 7.3243 0.98 2835 160 0.1774 0.1792
REMARK 3 2 7.3243 - 5.8171 1.00 2796 135 0.1850 0.1947
REMARK 3 3 5.8171 - 5.0829 1.00 2736 151 0.1686 0.2135
REMARK 3 4 5.0829 - 4.6186 1.00 2680 155 0.1488 0.1855
REMARK 3 5 4.6186 - 4.2878 1.00 2727 145 0.1501 0.1617
REMARK 3 6 4.2878 - 4.0352 1.00 2703 136 0.1667 0.2125
REMARK 3 7 4.0352 - 3.8332 1.00 2677 161 0.1733 0.2225
REMARK 3 8 3.8332 - 3.6664 1.00 2688 140 0.1821 0.2117
REMARK 3 9 3.6664 - 3.5253 1.00 2656 154 0.1972 0.2198
REMARK 3 10 3.5253 - 3.4037 1.00 2707 104 0.2208 0.2683
REMARK 3 11 3.4037 - 3.2973 1.00 2682 131 0.2283 0.2596
REMARK 3 12 3.2973 - 3.2031 1.00 2698 128 0.2429 0.2734
REMARK 3 13 3.2031 - 3.1188 1.00 2654 147 0.2378 0.2862
REMARK 3 14 3.1188 - 3.0427 1.00 2666 132 0.2370 0.2556
REMARK 3 15 3.0427 - 2.9735 1.00 2670 168 0.2452 0.3017
REMARK 3 16 2.9735 - 2.9103 1.00 2610 136 0.2552 0.2753
REMARK 3 17 2.9103 - 2.8520 1.00 2684 153 0.2651 0.2664
REMARK 3 18 2.8520 - 2.7982 1.00 2639 145 0.2581 0.3165
REMARK 3 19 2.7982 - 2.7483 1.00 2685 134 0.2688 0.3119
REMARK 3 20 2.7483 - 2.7017 1.00 2638 140 0.2575 0.2769
REMARK 3 21 2.7017 - 2.6581 1.00 2655 132 0.2674 0.2916
REMARK 3 22 2.6581 - 2.6172 1.00 2627 136 0.2730 0.2948
REMARK 3 23 2.6172 - 2.5787 1.00 2676 150 0.2863 0.3388
REMARK 3 24 2.5787 - 2.5424 1.00 2616 148 0.2925 0.3145
REMARK 3 25 2.5424 - 2.5081 1.00 2672 143 0.3048 0.3156
REMARK 3 26 2.5081 - 2.4755 1.00 2650 128 0.3199 0.4255
REMARK 3 27 2.4755 - 2.4445 1.00 2651 142 0.3539 0.3686
REMARK 3 28 2.4445 - 2.4151 0.98 2590 134 0.3614 0.3678
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.011 8615
REMARK 3 ANGLE : 1.215 11765
REMARK 3 CHIRALITY : 0.057 1262
REMARK 3 PLANARITY : 0.009 1548
REMARK 3 DIHEDRAL : 14.386 3099
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9512 -8.6213 -11.0868
REMARK 3 T TENSOR
REMARK 3 T11: 0.4298 T22: 0.4008
REMARK 3 T33: 0.4358 T12: -0.0437
REMARK 3 T13: -0.0079 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.2407 L22: 0.1387
REMARK 3 L33: 1.1646 L12: -0.0803
REMARK 3 L13: -0.4727 L23: -0.1366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.0184 S13: 0.0733
REMARK 3 S21: 0.0214 S22: -0.0290 S23: -0.0607
REMARK 3 S31: -0.1511 S32: 0.0415 S33: 0.0307
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID A
REMARK 3 SELECTION : CHAIN B AND SEGID B
REMARK 3 ATOM PAIRS NUMBER : 4840
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5HCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216790.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76507
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.415
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
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: 2HA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% V/V PEG 600, 0.1 M SODIUM CITRATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 39.28750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.30850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.17300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.30850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.28750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.17300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 ASP B -2
REMARK 465 PRO B -1
REMARK 465 MET B 0
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 SER B 495
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG B 356 NE CZ
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 CB ASN A 265 OE1 GLU A 268 1.67
REMARK 500 NH1 ARG A 485 O HOH A 601 1.80
REMARK 500 NH2 ARG A 356 OG1 THR A 383 1.86
REMARK 500 ND2 ASN A 265 OE2 GLU A 268 1.89
REMARK 500 OE1 GLU A 166 O HOH A 602 1.91
REMARK 500 OE2 GLU A 243 NH1 ARG A 246 1.98
REMARK 500 ND2 ASN B 67 O HOH B 601 2.12
REMARK 500 NH1 ARG A 45 OE1 GLU A 51 2.12
REMARK 500 NH2 ARG B 424 O HOH B 602 2.14
REMARK 500 CE2 PHE B 295 CD2 PHE B 338 2.17
REMARK 500 O ASP A 134 O HOH A 603 2.17
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 THR A 63 NH1 ARG B 493 4445 1.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 258 CD PRO A 258 N -0.108
REMARK 500 PRO A 290 CD PRO A 290 N -0.119
REMARK 500 GLU B 202 C MIS B 203 N 0.145
REMARK 500 MIS B 203 C ALA B 204 N 0.180
REMARK 500 ARG B 356 CD ARG B 356 NE -0.109
REMARK 500 ARG B 356 CZ ARG B 356 NH2 -0.167
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 MIS A 203 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLN B 7 C - N - CA ANGL. DEV. = -15.6 DEGREES
REMARK 500 ARG B 356 NH1 - CZ - NH2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG B 356 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 GLN B 369 C - N - CA ANGL. DEV. = -27.6 DEGREES
REMARK 500 GLN B 369 O - C - N ANGL. DEV. = -22.1 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 47 -3.45 72.28
REMARK 500 MIS A 203 -125.28 60.11
REMARK 500 ASP A 306 -79.58 -127.92
REMARK 500 TYR A 341 55.14 -108.04
REMARK 500 VAL A 407 -62.77 -129.23
REMARK 500 HIS A 447 123.75 -38.57
REMARK 500 ASN A 514 -167.40 -160.82
REMARK 500 PHE B 47 -3.84 72.80
REMARK 500 ALA B 62 51.17 -119.21
REMARK 500 MIS B 203 -124.00 59.83
REMARK 500 ASP B 306 -78.94 -128.69
REMARK 500 TYR B 341 54.44 -107.68
REMARK 500 VAL B 407 -62.68 -131.26
REMARK 500 HIS B 447 123.98 -39.02
REMARK 500 ASN B 514 -169.37 -162.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN B 7 -14.27
REMARK 500 GLN B 369 -29.53
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5HCU A 1 540 UNP P21836 ACES_MOUSE 32 571
DBREF 5HCU B 1 540 UNP P21836 ACES_MOUSE 32 571
SEQADV 5HCU ASP A -2 UNP P21836 EXPRESSION TAG
SEQADV 5HCU PRO A -1 UNP P21836 EXPRESSION TAG
SEQADV 5HCU MET A 0 UNP P21836 EXPRESSION TAG
SEQADV 5HCU ASP B -2 UNP P21836 EXPRESSION TAG
SEQADV 5HCU PRO B -1 UNP P21836 EXPRESSION TAG
SEQADV 5HCU MET B 0 UNP P21836 EXPRESSION TAG
SEQRES 1 A 543 ASP PRO MET GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL
SEQRES 2 A 543 ARG VAL ARG GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS
SEQRES 3 A 543 ALA PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO
SEQRES 4 A 543 PHE ALA GLU PRO PRO VAL GLY SER ARG ARG PHE MET PRO
SEQRES 5 A 543 PRO GLU PRO LYS ARG PRO TRP SER GLY VAL LEU ASP ALA
SEQRES 6 A 543 THR THR PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR
SEQRES 7 A 543 LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO
SEQRES 8 A 543 ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL
SEQRES 9 A 543 TRP THR PRO TYR PRO ARG PRO ALA SER PRO THR PRO VAL
SEQRES 10 A 543 LEU ILE TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA
SEQRES 11 A 543 ALA SER LEU ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN
SEQRES 12 A 543 VAL GLU GLY ALA VAL LEU VAL SER MET ASN TYR ARG VAL
SEQRES 13 A 543 GLY THR PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU
SEQRES 14 A 543 ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA
SEQRES 15 A 543 LEU GLN TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY
SEQRES 16 A 543 ASP PRO MET SER VAL THR LEU PHE GLY GLU MIS ALA GLY
SEQRES 17 A 543 ALA ALA SER VAL GLY MET HIS ILE LEU SER LEU PRO SER
SEQRES 18 A 543 ARG SER LEU PHE HIS ARG ALA VAL LEU GLN SER GLY THR
SEQRES 19 A 543 PRO ASN GLY PRO TRP ALA THR VAL SER ALA GLY GLU ALA
SEQRES 20 A 543 ARG ARG ARG ALA THR LEU LEU ALA ARG LEU VAL GLY CYS
SEQRES 21 A 543 PRO PRO GLY GLY ALA GLY GLY ASN ASP THR GLU LEU ILE
SEQRES 22 A 543 ALA CYS LEU ARG THR ARG PRO ALA GLN ASP LEU VAL ASP
SEQRES 23 A 543 HIS GLU TRP HIS VAL LEU PRO GLN GLU SER ILE PHE ARG
SEQRES 24 A 543 PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER
SEQRES 25 A 543 ASP THR PRO GLU ALA LEU ILE ASN THR GLY ASP PHE GLN
SEQRES 26 A 543 ASP LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY
SEQRES 27 A 543 SER TYR PHE LEU VAL TYR GLY VAL PRO GLY PHE SER LYS
SEQRES 28 A 543 ASP ASN GLU SER LEU ILE SER ARG ALA GLN PHE LEU ALA
SEQRES 29 A 543 GLY VAL ARG ILE GLY VAL PRO GLN ALA SER ASP LEU ALA
SEQRES 30 A 543 ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS
SEQRES 31 A 543 PRO GLU ASP PRO THR HIS LEU ARG ASP ALA MET SER ALA
SEQRES 32 A 543 VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN
SEQRES 33 A 543 LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR
SEQRES 34 A 543 ALA TYR ILE PHE GLU HIS ARG ALA SER THR LEU THR TRP
SEQRES 35 A 543 PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU
SEQRES 36 A 543 PHE ILE PHE GLY LEU PRO LEU ASP PRO SER LEU ASN TYR
SEQRES 37 A 543 THR THR GLU GLU ARG ILE PHE ALA GLN ARG LEU MET LYS
SEQRES 38 A 543 TYR TRP THR ASN PHE ALA ARG THR GLY ASP PRO ASN ASP
SEQRES 39 A 543 PRO ARG ASP SER LYS SER PRO GLN TRP PRO PRO TYR THR
SEQRES 40 A 543 THR ALA ALA GLN GLN TYR VAL SER LEU ASN LEU LYS PRO
SEQRES 41 A 543 LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN THR CYS ALA
SEQRES 42 A 543 PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU
SEQRES 1 B 543 ASP PRO MET GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL
SEQRES 2 B 543 ARG VAL ARG GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS
SEQRES 3 B 543 ALA PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO
SEQRES 4 B 543 PHE ALA GLU PRO PRO VAL GLY SER ARG ARG PHE MET PRO
SEQRES 5 B 543 PRO GLU PRO LYS ARG PRO TRP SER GLY VAL LEU ASP ALA
SEQRES 6 B 543 THR THR PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR
SEQRES 7 B 543 LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO
SEQRES 8 B 543 ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL
SEQRES 9 B 543 TRP THR PRO TYR PRO ARG PRO ALA SER PRO THR PRO VAL
SEQRES 10 B 543 LEU ILE TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA
SEQRES 11 B 543 ALA SER LEU ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN
SEQRES 12 B 543 VAL GLU GLY ALA VAL LEU VAL SER MET ASN TYR ARG VAL
SEQRES 13 B 543 GLY THR PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU
SEQRES 14 B 543 ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA
SEQRES 15 B 543 LEU GLN TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY
SEQRES 16 B 543 ASP PRO MET SER VAL THR LEU PHE GLY GLU MIS ALA GLY
SEQRES 17 B 543 ALA ALA SER VAL GLY MET HIS ILE LEU SER LEU PRO SER
SEQRES 18 B 543 ARG SER LEU PHE HIS ARG ALA VAL LEU GLN SER GLY THR
SEQRES 19 B 543 PRO ASN GLY PRO TRP ALA THR VAL SER ALA GLY GLU ALA
SEQRES 20 B 543 ARG ARG ARG ALA THR LEU LEU ALA ARG LEU VAL GLY CYS
SEQRES 21 B 543 PRO PRO GLY GLY ALA GLY GLY ASN ASP THR GLU LEU ILE
SEQRES 22 B 543 ALA CYS LEU ARG THR ARG PRO ALA GLN ASP LEU VAL ASP
SEQRES 23 B 543 HIS GLU TRP HIS VAL LEU PRO GLN GLU SER ILE PHE ARG
SEQRES 24 B 543 PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER
SEQRES 25 B 543 ASP THR PRO GLU ALA LEU ILE ASN THR GLY ASP PHE GLN
SEQRES 26 B 543 ASP LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY
SEQRES 27 B 543 SER TYR PHE LEU VAL TYR GLY VAL PRO GLY PHE SER LYS
SEQRES 28 B 543 ASP ASN GLU SER LEU ILE SER ARG ALA GLN PHE LEU ALA
SEQRES 29 B 543 GLY VAL ARG ILE GLY VAL PRO GLN ALA SER ASP LEU ALA
SEQRES 30 B 543 ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS
SEQRES 31 B 543 PRO GLU ASP PRO THR HIS LEU ARG ASP ALA MET SER ALA
SEQRES 32 B 543 VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN
SEQRES 33 B 543 LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR
SEQRES 34 B 543 ALA TYR ILE PHE GLU HIS ARG ALA SER THR LEU THR TRP
SEQRES 35 B 543 PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU
SEQRES 36 B 543 PHE ILE PHE GLY LEU PRO LEU ASP PRO SER LEU ASN TYR
SEQRES 37 B 543 THR THR GLU GLU ARG ILE PHE ALA GLN ARG LEU MET LYS
SEQRES 38 B 543 TYR TRP THR ASN PHE ALA ARG THR GLY ASP PRO ASN ASP
SEQRES 39 B 543 PRO ARG ASP SER LYS SER PRO GLN TRP PRO PRO TYR THR
SEQRES 40 B 543 THR ALA ALA GLN GLN TYR VAL SER LEU ASN LEU LYS PRO
SEQRES 41 B 543 LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN THR CYS ALA
SEQRES 42 B 543 PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU
MODRES 5HCU MIS A 203 SER MODIFIED RESIDUE
MODRES 5HCU MIS B 203 SER MODIFIED RESIDUE
HET MIS A 203 13
HET MIS B 203 13
HETNAM MIS MONOISOPROPYLPHOSPHORYLSERINE
FORMUL 1 MIS 2(C6 H14 N O6 P)
FORMUL 3 HOH *131(H2 O)
HELIX 1 AA1 MET A 0 GLU A 4 5 5
HELIX 2 AA2 VAL A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 GLY A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 ILE A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 MIS A 203 LEU A 214 1 12
HELIX 10 AB1 SER A 215 SER A 220 1 6
HELIX 11 AB2 ALA A 241 VAL A 255 1 15
HELIX 12 AB3 ASP A 266 ARG A 276 1 11
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 THR A 311 GLY A 319 1 9
HELIX 15 AB6 GLY A 335 VAL A 340 1 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 GLN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASN A 464 5 9
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 PHE A 535 1 11
HELIX 25 AC7 LEU A 536 LEU A 540 5 5
HELIX 26 AC8 VAL B 42 ARG B 46 5 5
HELIX 27 AC9 PHE B 80 MET B 85 1 6
HELIX 28 AD1 LEU B 130 ASP B 134 5 5
HELIX 29 AD2 GLY B 135 GLY B 143 1 9
HELIX 30 AD3 VAL B 153 LEU B 159 1 7
HELIX 31 AD4 ASN B 170 ILE B 187 1 18
HELIX 32 AD5 ALA B 188 PHE B 190 5 3
HELIX 33 AD6 MIS B 203 LEU B 214 1 12
HELIX 34 AD7 SER B 215 SER B 220 1 6
HELIX 35 AD8 SER B 240 VAL B 255 1 16
HELIX 36 AD9 ASP B 266 ARG B 276 1 11
HELIX 37 AE1 PRO B 277 GLU B 285 1 9
HELIX 38 AE2 THR B 311 GLY B 319 1 9
HELIX 39 AE3 GLY B 335 VAL B 340 1 6
HELIX 40 AE4 SER B 355 VAL B 367 1 13
HELIX 41 AE5 SER B 371 THR B 383 1 13
HELIX 42 AE6 ASP B 390 VAL B 407 1 18
HELIX 43 AE7 VAL B 407 GLN B 421 1 15
HELIX 44 AE8 PRO B 440 GLY B 444 5 5
HELIX 45 AE9 GLU B 450 PHE B 455 1 6
HELIX 46 AF1 GLY B 456 ASN B 464 5 9
HELIX 47 AF2 THR B 466 GLY B 487 1 22
HELIX 48 AF3 ARG B 525 PHE B 535 1 11
HELIX 49 AF4 LEU B 536 LEU B 540 5 5
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 AA211 ILE A 20 ALA A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 2 VAL A 239 SER A 240 0
SHEET 2 AA4 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA5 3 LEU B 9 VAL B 12 0
SHEET 2 AA5 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 AA5 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA611 ILE B 20 ALA B 24 0
SHEET 2 AA611 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA611 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA611 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 AA611 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA611 GLY B 192 GLU B 202 1 O THR B 198 N VAL B 114
SHEET 7 AA611 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA611 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA611 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA611 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA611 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA7 2 VAL B 68 CYS B 69 0
SHEET 2 AA7 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.07
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.08
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK C GLU A 202 N MIS A 203 1555 1555 1.43
LINK C MIS A 203 N ALA A 204 1555 1555 1.35
LINK C GLU B 202 N MIS B 203 1555 1555 1.48
LINK C MIS B 203 N ALA B 204 1555 1555 1.52
CISPEP 1 TYR A 105 PRO A 106 0 -1.90
CISPEP 2 TYR B 105 PRO B 106 0 2.93
CISPEP 3 CYS B 257 PRO B 258 0 -3.16
CRYST1 78.575 114.346 226.617 90.00 90.00 90.00 P 21 21 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 0.012727 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004413 0.00000
TER 4208 LEU A 540
TER 8363 LEU B 540
MASTER 408 0 2 49 34 0 0 6 8492 2 42 84
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