HEADER HYDROLASE 09-JAN-12 4AE8
TITLE CRYSTAL STRUCTURE OF HUMAN THEM4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOESTERASE SUPERFAMILY MEMBER 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 37-240;
COMPND 5 SYNONYM: CARBOXYL-TERMINAL MODULATOR PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2
KEYWDS HYDROLASE, HOTDOG-FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR E.ZHURAVLEVA,H.GUT,D.HYNX,D.MARCELLIN,C.K.E.BLECK,C.GENOUD,P.CRON,
AUTHOR 2 J.J.KEUSCH,B.DUMMLER,M.DEGLI ESPOSTI,B.A.HEMMINGS
REVDAT 1 11-JUL-12 4AE8 0
JRNL AUTH E.ZHURAVLEVA,H.GUT,D.HYNX,D.MARCELLIN,C.K.E.BLECK,C.GENOUD,
JRNL AUTH 2 P.CRON,J.J.KEUSCH,B.DUMMLER,M.D.ESPOSTI,B.A.HEMMINGS
JRNL TITL ACYL COENZYME A THIOESTERASE THEM5/ACOT15 IS INVOLVED IN
JRNL TITL 2 CARDIOLIPIN REMODELING AND FATTY LIVER DEVELOPMENT.
JRNL REF MOL.CELL.BIOL. V. 32 2685 2012
JRNL REFN ISSN 0270-7306
JRNL PMID 22586271
JRNL DOI 10.1128/MCB.00312-12
REMARK 2
REMARK 2 RESOLUTION. 1.59 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-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) : 1.594
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.720
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.98
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.39
REMARK 3 NUMBER OF REFLECTIONS : 83488
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1867
REMARK 3 R VALUE (WORKING SET) : 0.1848
REMARK 3 FREE R VALUE : 0.2228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 4113
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 29.7250 - 4.8904 0.97 2842 149 0.2046 0.2226
REMARK 3 2 4.8904 - 3.8844 0.97 2806 159 0.1456 0.1629
REMARK 3 3 3.8844 - 3.3942 0.97 2866 140 0.1559 0.1934
REMARK 3 4 3.3942 - 3.0842 0.97 2833 164 0.1696 0.1965
REMARK 3 5 3.0842 - 2.8634 0.96 2840 125 0.1858 0.2197
REMARK 3 6 2.8634 - 2.6947 0.96 2786 154 0.1809 0.2266
REMARK 3 7 2.6947 - 2.5598 0.96 2836 138 0.1777 0.2205
REMARK 3 8 2.5598 - 2.4484 0.96 2816 142 0.1921 0.2420
REMARK 3 9 2.4484 - 2.3542 0.95 2815 126 0.1867 0.2067
REMARK 3 10 2.3542 - 2.2730 0.95 2747 158 0.1793 0.2414
REMARK 3 11 2.2730 - 2.2019 0.95 2774 146 0.1836 0.2231
REMARK 3 12 2.2019 - 2.1390 0.95 2780 150 0.1848 0.2576
REMARK 3 13 2.1390 - 2.0827 0.95 2794 143 0.1913 0.2172
REMARK 3 14 2.0827 - 2.0319 0.95 2797 151 0.1953 0.2394
REMARK 3 15 2.0319 - 1.9857 0.95 2804 124 0.1918 0.2408
REMARK 3 16 1.9857 - 1.9435 0.95 2742 140 0.1978 0.2306
REMARK 3 17 1.9435 - 1.9046 0.94 2833 158 0.1925 0.2496
REMARK 3 18 1.9046 - 1.8687 0.95 2769 151 0.1982 0.2333
REMARK 3 19 1.8687 - 1.8353 0.95 2764 139 0.1985 0.2526
REMARK 3 20 1.8353 - 1.8042 0.95 2797 150 0.2066 0.2608
REMARK 3 21 1.8042 - 1.7751 0.94 2748 156 0.2075 0.2534
REMARK 3 22 1.7751 - 1.7478 0.94 2746 141 0.2095 0.3040
REMARK 3 23 1.7478 - 1.7221 0.94 2763 153 0.2173 0.2601
REMARK 3 24 1.7221 - 1.6978 0.93 2750 131 0.2185 0.2877
REMARK 3 25 1.6978 - 1.6749 0.91 2664 117 0.2218 0.2408
REMARK 3 26 1.6749 - 1.6531 0.91 2683 141 0.2264 0.2652
REMARK 3 27 1.6531 - 1.6325 0.88 2548 140 0.2467 0.3032
REMARK 3 28 1.6325 - 1.6128 0.84 2461 133 0.2357 0.2890
REMARK 3 29 1.6128 - 1.5941 0.67 1971 94 0.2524 0.2950
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.361
REMARK 3 B_SOL : 42.575
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.43
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.7986
REMARK 3 B22 (A**2) : -0.8757
REMARK 3 B33 (A**2) : -0.9229
REMARK 3 B12 (A**2) : -3.2491
REMARK 3 B13 (A**2) : -3.2969
REMARK 3 B23 (A**2) : -0.2947
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 : 0.006 5452
REMARK 3 ANGLE : 1.023 7355
REMARK 3 CHIRALITY : 0.073 792
REMARK 3 PLANARITY : 0.005 947
REMARK 3 DIHEDRAL : 12.253 2045
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR B
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3571 -18.5941 9.8354
REMARK 3 T TENSOR
REMARK 3 T11: 0.0624 T22: 0.0756
REMARK 3 T33: 0.0670 T12: 0.0198
REMARK 3 T13: 0.0061 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.9356 L22: 0.8879
REMARK 3 L33: 0.1999 L12: 0.5324
REMARK 3 L13: -0.0591 L23: -0.0235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0316 S12: -0.0538 S13: -0.0527
REMARK 3 S21: 0.0212 S22: -0.0261 S23: -0.1161
REMARK 3 S31: 0.0182 S32: 0.0147 S33: -0.0073
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN C OR D
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3985 3.7362 41.8679
REMARK 3 T TENSOR
REMARK 3 T11: 0.0854 T22: 0.0927
REMARK 3 T33: 0.0611 T12: -0.0043
REMARK 3 T13: -0.0042 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.3817 L22: 1.3062
REMARK 3 L33: 0.2569 L12: 0.1895
REMARK 3 L13: 0.0419 L23: 0.0862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.0190 S13: 0.0449
REMARK 3 S21: -0.0808 S22: -0.0179 S23: 0.1259
REMARK 3 S31: 0.0130 S32: -0.0409 S33: 0.0048
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 4AE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JAN-12.
REMARK 100 THE PDBE ID CODE IS EBI-50890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX 225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83501
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 1.9
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.7
REMARK 200 R MERGE FOR SHELL (I) : 0.22
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.20
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3000, 0.2M NACL, 0.1M
REMARK 280 TRIS PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.9 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 30
REMARK 465 ALA A 31
REMARK 465 HIS A 32
REMARK 465 MET A 33
REMARK 465 SER A 34
REMARK 465 GLY A 35
REMARK 465 ARG A 36
REMARK 465 SER A 37
REMARK 465 SER A 38
REMARK 465 GLU A 39
REMARK 465 GLU A 40
REMARK 465 VAL A 41
REMARK 465 ARG A 81
REMARK 465 THR A 82
REMARK 465 PRO A 83
REMARK 465 THR A 84
REMARK 465 GLU A 85
REMARK 465 TRP A 86
REMARK 465 ILE A 87
REMARK 465 GLN A 88
REMARK 465 ASP A 89
REMARK 465 PHE A 90
REMARK 465 LYS A 91
REMARK 465 THR A 92
REMARK 465 HIS A 93
REMARK 465 PHE A 94
REMARK 465 LEU A 95
REMARK 465 ASP A 96
REMARK 465 PRO A 97
REMARK 465 LYS A 98
REMARK 465 LEU A 99
REMARK 465 MET A 100
REMARK 465 LYS A 101
REMARK 465 GLU A 102
REMARK 465 GLU A 103
REMARK 465 GLN A 104
REMARK 465 MET A 105
REMARK 465 SER A 106
REMARK 465 PRO A 235
REMARK 465 ALA A 236
REMARK 465 LYS A 237
REMARK 465 SER A 238
REMARK 465 LEU A 239
REMARK 465 THR A 240
REMARK 465 GLY B 30
REMARK 465 ALA B 31
REMARK 465 HIS B 32
REMARK 465 MET B 33
REMARK 465 SER B 34
REMARK 465 GLY B 35
REMARK 465 ARG B 36
REMARK 465 SER B 37
REMARK 465 SER B 38
REMARK 465 GLU B 39
REMARK 465 GLU B 40
REMARK 465 VAL B 41
REMARK 465 ILE B 42
REMARK 465 ARG B 81
REMARK 465 THR B 82
REMARK 465 PRO B 83
REMARK 465 THR B 84
REMARK 465 GLU B 85
REMARK 465 TRP B 86
REMARK 465 ILE B 87
REMARK 465 GLN B 88
REMARK 465 ASP B 89
REMARK 465 PHE B 90
REMARK 465 LYS B 91
REMARK 465 THR B 92
REMARK 465 HIS B 93
REMARK 465 PHE B 94
REMARK 465 LEU B 95
REMARK 465 ASP B 96
REMARK 465 PRO B 97
REMARK 465 LYS B 98
REMARK 465 LEU B 99
REMARK 465 MET B 100
REMARK 465 LYS B 101
REMARK 465 GLU B 102
REMARK 465 GLU B 103
REMARK 465 GLN B 104
REMARK 465 MET B 105
REMARK 465 ASN B 234
REMARK 465 PRO B 235
REMARK 465 ALA B 236
REMARK 465 LYS B 237
REMARK 465 SER B 238
REMARK 465 LEU B 239
REMARK 465 THR B 240
REMARK 465 GLY C 30
REMARK 465 ALA C 31
REMARK 465 HIS C 32
REMARK 465 MET C 33
REMARK 465 SER C 34
REMARK 465 GLY C 35
REMARK 465 ARG C 36
REMARK 465 SER C 37
REMARK 465 SER C 38
REMARK 465 GLU C 39
REMARK 465 GLU C 40
REMARK 465 VAL C 41
REMARK 465 ILE C 42
REMARK 465 PRO C 83
REMARK 465 THR C 84
REMARK 465 GLU C 85
REMARK 465 TRP C 86
REMARK 465 ILE C 87
REMARK 465 GLN C 88
REMARK 465 ASP C 89
REMARK 465 PHE C 90
REMARK 465 LYS C 91
REMARK 465 THR C 92
REMARK 465 HIS C 93
REMARK 465 PHE C 94
REMARK 465 LEU C 95
REMARK 465 ASP C 96
REMARK 465 PRO C 97
REMARK 465 LYS C 98
REMARK 465 LEU C 99
REMARK 465 MET C 100
REMARK 465 LYS C 101
REMARK 465 GLU C 102
REMARK 465 GLU C 103
REMARK 465 GLN C 104
REMARK 465 MET C 105
REMARK 465 ASN C 234
REMARK 465 PRO C 235
REMARK 465 ALA C 236
REMARK 465 LYS C 237
REMARK 465 SER C 238
REMARK 465 LEU C 239
REMARK 465 THR C 240
REMARK 465 GLY D 30
REMARK 465 ALA D 31
REMARK 465 HIS D 32
REMARK 465 MET D 33
REMARK 465 SER D 34
REMARK 465 GLY D 35
REMARK 465 ARG D 36
REMARK 465 SER D 37
REMARK 465 SER D 38
REMARK 465 GLU D 39
REMARK 465 GLU D 40
REMARK 465 VAL D 41
REMARK 465 ILE D 42
REMARK 465 LYS D 80
REMARK 465 ARG D 81
REMARK 465 THR D 82
REMARK 465 PRO D 83
REMARK 465 THR D 84
REMARK 465 GLU D 85
REMARK 465 TRP D 86
REMARK 465 ILE D 87
REMARK 465 GLN D 88
REMARK 465 ASP D 89
REMARK 465 PHE D 90
REMARK 465 LYS D 91
REMARK 465 THR D 92
REMARK 465 HIS D 93
REMARK 465 PHE D 94
REMARK 465 LEU D 95
REMARK 465 ASP D 96
REMARK 465 PRO D 97
REMARK 465 LYS D 98
REMARK 465 LEU D 99
REMARK 465 MET D 100
REMARK 465 LYS D 101
REMARK 465 GLU D 102
REMARK 465 GLU D 103
REMARK 465 GLN D 104
REMARK 465 MET D 105
REMARK 465 SER D 106
REMARK 465 PRO D 235
REMARK 465 ALA D 236
REMARK 465 LYS D 237
REMARK 465 SER D 238
REMARK 465 LEU D 239
REMARK 465 THR D 240
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 OD1 ASP B 129 O HOH B 2101 1.94
REMARK 500 OE1 GLU D 69 O HOH D 2042 2.10
REMARK 500 O HOH A 2006 O HOH A 2102 2.20
REMARK 500 O HOH A 2015 O HOH A 2026 2.12
REMARK 500 O HOH A 2060 O HOH A 2089 2.02
REMARK 500 O HOH A 2073 O HOH A 2074 1.96
REMARK 500 O HOH A 2078 O HOH A 2089 2.08
REMARK 500 O HOH A 2083 O HOH A 2118 2.17
REMARK 500 O HOH A 2096 O HOH A 2120 2.15
REMARK 500 O HOH A 2110 O HOH A 2111 2.04
REMARK 500 O HOH A 2113 O HOH A 2167 2.15
REMARK 500 O HOH A 2116 O HOH A 2176 2.10
REMARK 500 O HOH A 2118 O HOH A 2119 2.16
REMARK 500 O HOH A 2125 O HOH A 2196 2.05
REMARK 500 O HOH A 2173 O HOH A 2176 2.06
REMARK 500 O HOH B 2002 O HOH B 2011 1.89
REMARK 500 O HOH B 2051 O HOH B 2063 1.82
REMARK 500 O HOH B 2090 O HOH B 2123 2.14
REMARK 500 O HOH C 2057 O HOH B 2094 2.12
REMARK 500 O HOH C 2090 O HOH C 2091 2.07
REMARK 500 O HOH D 2006 O HOH D 2072 2.17
REMARK 500 O HOH D 2017 O HOH B 2053 2.03
REMARK 500 O HOH D 2054 O HOH D 2063 1.94
REMARK 500 O HOH D 2063 O HOH C 2071 2.13
REMARK 500 O HOH D 2087 O HOH D 2088 2.12
REMARK 500 O HOH D 2094 O HOH D 2095 2.10
REMARK 500 O HOH D 2170 O HOH D 2171 2.12
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 NZ LYS B 220 O HOH D 2144 2554 2.20
REMARK 500 NZ LYS D 232 O HOH B 2173 2556 2.10
REMARK 500 O HOH A 2016 O HOH C 2050 2545 2.13
REMARK 500 O HOH A 2026 O HOH C 2049 2545 2.07
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 47 49.42 -92.04
REMARK 500 SER B 47 34.35 -98.18
REMARK 500 GLU B 219 -1.10 72.62
REMARK 500 SER C 47 31.52 -94.83
REMARK 500 SER D 47 48.55 -92.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4AE8 A 37 240 UNP Q5T1C6 THEM4_HUMAN 37 240
DBREF 4AE8 B 37 240 UNP Q5T1C6 THEM4_HUMAN 37 240
DBREF 4AE8 C 37 240 UNP Q5T1C6 THEM4_HUMAN 37 240
DBREF 4AE8 D 37 240 UNP Q5T1C6 THEM4_HUMAN 37 240
SEQRES 1 A 211 GLY ALA HIS MET SER GLY ARG SER SER GLU GLU VAL ILE
SEQRES 2 A 211 LEU LYS ASP CYS SER VAL PRO ASN PRO SER TRP ASN LYS
SEQRES 3 A 211 ASP LEU ARG LEU LEU PHE ASP GLN PHE MET LYS LYS CYS
SEQRES 4 A 211 GLU ASP GLY SER TRP LYS ARG LEU PRO SER TYR LYS ARG
SEQRES 5 A 211 THR PRO THR GLU TRP ILE GLN ASP PHE LYS THR HIS PHE
SEQRES 6 A 211 LEU ASP PRO LYS LEU MET LYS GLU GLU GLN MET SER GLN
SEQRES 7 A 211 ALA GLN LEU PHE THR ARG SER PHE ASP ASP GLY LEU GLY
SEQRES 8 A 211 PHE GLU TYR VAL MET PHE TYR ASN ASP ILE GLU LYS ARG
SEQRES 9 A 211 MET VAL CYS LEU PHE GLN GLY GLY PRO TYR LEU GLU GLY
SEQRES 10 A 211 PRO PRO GLY PHE ILE HIS GLY GLY ALA ILE ALA THR MET
SEQRES 11 A 211 ILE ASP ALA THR VAL GLY MET CYS ALA MET MET ALA GLY
SEQRES 12 A 211 GLY ILE VAL MET THR ALA ASN LEU ASN ILE ASN TYR LYS
SEQRES 13 A 211 ARG PRO ILE PRO LEU CYS SER VAL VAL MET ILE ASN SER
SEQRES 14 A 211 GLN LEU ASP LYS VAL GLU GLY ARG LYS PHE PHE VAL SER
SEQRES 15 A 211 CYS ASN VAL GLN SER VAL ASP GLU LYS THR LEU TYR SER
SEQRES 16 A 211 GLU ALA THR SER LEU PHE ILE LYS LEU ASN PRO ALA LYS
SEQRES 17 A 211 SER LEU THR
SEQRES 1 B 211 GLY ALA HIS MET SER GLY ARG SER SER GLU GLU VAL ILE
SEQRES 2 B 211 LEU LYS ASP CYS SER VAL PRO ASN PRO SER TRP ASN LYS
SEQRES 3 B 211 ASP LEU ARG LEU LEU PHE ASP GLN PHE MET LYS LYS CYS
SEQRES 4 B 211 GLU ASP GLY SER TRP LYS ARG LEU PRO SER TYR LYS ARG
SEQRES 5 B 211 THR PRO THR GLU TRP ILE GLN ASP PHE LYS THR HIS PHE
SEQRES 6 B 211 LEU ASP PRO LYS LEU MET LYS GLU GLU GLN MET SER GLN
SEQRES 7 B 211 ALA GLN LEU PHE THR ARG SER PHE ASP ASP GLY LEU GLY
SEQRES 8 B 211 PHE GLU TYR VAL MET PHE TYR ASN ASP ILE GLU LYS ARG
SEQRES 9 B 211 MET VAL CYS LEU PHE GLN GLY GLY PRO TYR LEU GLU GLY
SEQRES 10 B 211 PRO PRO GLY PHE ILE HIS GLY GLY ALA ILE ALA THR MET
SEQRES 11 B 211 ILE ASP ALA THR VAL GLY MET CYS ALA MET MET ALA GLY
SEQRES 12 B 211 GLY ILE VAL MET THR ALA ASN LEU ASN ILE ASN TYR LYS
SEQRES 13 B 211 ARG PRO ILE PRO LEU CYS SER VAL VAL MET ILE ASN SER
SEQRES 14 B 211 GLN LEU ASP LYS VAL GLU GLY ARG LYS PHE PHE VAL SER
SEQRES 15 B 211 CYS ASN VAL GLN SER VAL ASP GLU LYS THR LEU TYR SER
SEQRES 16 B 211 GLU ALA THR SER LEU PHE ILE LYS LEU ASN PRO ALA LYS
SEQRES 17 B 211 SER LEU THR
SEQRES 1 C 211 GLY ALA HIS MET SER GLY ARG SER SER GLU GLU VAL ILE
SEQRES 2 C 211 LEU LYS ASP CYS SER VAL PRO ASN PRO SER TRP ASN LYS
SEQRES 3 C 211 ASP LEU ARG LEU LEU PHE ASP GLN PHE MET LYS LYS CYS
SEQRES 4 C 211 GLU ASP GLY SER TRP LYS ARG LEU PRO SER TYR LYS ARG
SEQRES 5 C 211 THR PRO THR GLU TRP ILE GLN ASP PHE LYS THR HIS PHE
SEQRES 6 C 211 LEU ASP PRO LYS LEU MET LYS GLU GLU GLN MET SER GLN
SEQRES 7 C 211 ALA GLN LEU PHE THR ARG SER PHE ASP ASP GLY LEU GLY
SEQRES 8 C 211 PHE GLU TYR VAL MET PHE TYR ASN ASP ILE GLU LYS ARG
SEQRES 9 C 211 MET VAL CYS LEU PHE GLN GLY GLY PRO TYR LEU GLU GLY
SEQRES 10 C 211 PRO PRO GLY PHE ILE HIS GLY GLY ALA ILE ALA THR MET
SEQRES 11 C 211 ILE ASP ALA THR VAL GLY MET CYS ALA MET MET ALA GLY
SEQRES 12 C 211 GLY ILE VAL MET THR ALA ASN LEU ASN ILE ASN TYR LYS
SEQRES 13 C 211 ARG PRO ILE PRO LEU CYS SER VAL VAL MET ILE ASN SER
SEQRES 14 C 211 GLN LEU ASP LYS VAL GLU GLY ARG LYS PHE PHE VAL SER
SEQRES 15 C 211 CYS ASN VAL GLN SER VAL ASP GLU LYS THR LEU TYR SER
SEQRES 16 C 211 GLU ALA THR SER LEU PHE ILE LYS LEU ASN PRO ALA LYS
SEQRES 17 C 211 SER LEU THR
SEQRES 1 D 211 GLY ALA HIS MET SER GLY ARG SER SER GLU GLU VAL ILE
SEQRES 2 D 211 LEU LYS ASP CYS SER VAL PRO ASN PRO SER TRP ASN LYS
SEQRES 3 D 211 ASP LEU ARG LEU LEU PHE ASP GLN PHE MET LYS LYS CYS
SEQRES 4 D 211 GLU ASP GLY SER TRP LYS ARG LEU PRO SER TYR LYS ARG
SEQRES 5 D 211 THR PRO THR GLU TRP ILE GLN ASP PHE LYS THR HIS PHE
SEQRES 6 D 211 LEU ASP PRO LYS LEU MET LYS GLU GLU GLN MET SER GLN
SEQRES 7 D 211 ALA GLN LEU PHE THR ARG SER PHE ASP ASP GLY LEU GLY
SEQRES 8 D 211 PHE GLU TYR VAL MET PHE TYR ASN ASP ILE GLU LYS ARG
SEQRES 9 D 211 MET VAL CYS LEU PHE GLN GLY GLY PRO TYR LEU GLU GLY
SEQRES 10 D 211 PRO PRO GLY PHE ILE HIS GLY GLY ALA ILE ALA THR MET
SEQRES 11 D 211 ILE ASP ALA THR VAL GLY MET CYS ALA MET MET ALA GLY
SEQRES 12 D 211 GLY ILE VAL MET THR ALA ASN LEU ASN ILE ASN TYR LYS
SEQRES 13 D 211 ARG PRO ILE PRO LEU CYS SER VAL VAL MET ILE ASN SER
SEQRES 14 D 211 GLN LEU ASP LYS VAL GLU GLY ARG LYS PHE PHE VAL SER
SEQRES 15 D 211 CYS ASN VAL GLN SER VAL ASP GLU LYS THR LEU TYR SER
SEQRES 16 D 211 GLU ALA THR SER LEU PHE ILE LYS LEU ASN PRO ALA LYS
SEQRES 17 D 211 SER LEU THR
FORMUL 5 HOH *751(H2 O)
HELIX 1 1 ASN A 54 CYS A 68 1 15
HELIX 2 2 PHE A 111 SER A 114 5 4
HELIX 3 3 PRO A 142 LEU A 144 5 3
HELIX 4 4 HIS A 152 GLY A 173 1 22
HELIX 5 5 ASN B 54 CYS B 68 1 15
HELIX 6 6 GLU B 69 GLY B 71 5 3
HELIX 7 7 PHE B 111 SER B 114 5 4
HELIX 8 8 PRO B 142 LEU B 144 5 3
HELIX 9 9 HIS B 152 GLY B 173 1 22
HELIX 10 10 ASN C 54 GLU C 69 1 16
HELIX 11 11 PHE C 111 SER C 114 5 4
HELIX 12 12 PRO C 142 LEU C 144 5 3
HELIX 13 13 HIS C 152 GLY C 173 1 22
HELIX 14 14 ASN D 54 CYS D 68 1 15
HELIX 15 15 PHE D 111 SER D 114 5 4
HELIX 16 16 PRO D 142 LEU D 144 5 3
HELIX 17 17 HIS D 152 GLY D 173 1 22
SHEET 1 AA 2 LYS A 44 ASP A 45 0
SHEET 2 AA 2 TYR A 79 LYS A 80 -1 O LYS A 80 N LYS A 44
SHEET 1 AB14 TRP A 73 LEU A 76 0
SHEET 2 AB14 PHE A 121 ASN A 128 -1 O MET A 125 N LEU A 76
SHEET 3 AB14 ARG A 133 GLY A 140 -1 O ARG A 133 N ASN A 128
SHEET 4 AB14 VAL A 193 GLU A 204 -1 O VAL A 194 N PHE A 138
SHEET 5 AB14 LYS A 207 SER A 216 -1 O LYS A 207 N GLU A 204
SHEET 6 AB14 LEU A 222 LYS A 232 -1 N TYR A 223 O VAL A 214
SHEET 7 AB14 VAL A 175 TYR A 184 -1 O MET A 176 N ILE A 231
SHEET 8 AB14 VAL B 175 TYR B 184 -1 O ALA B 178 N TYR A 184
SHEET 9 AB14 LEU B 222 LYS B 232 -1 O GLU B 225 N ASN B 183
SHEET 10 AB14 LYS B 207 SER B 216 -1 O PHE B 208 N PHE B 230
SHEET 11 AB14 VAL B 193 GLU B 204 -1 O MET B 195 N GLN B 215
SHEET 12 AB14 ARG B 133 GLY B 140 -1 O MET B 134 N SER B 198
SHEET 13 AB14 PHE B 121 ASN B 128 -1 O GLU B 122 N GLN B 139
SHEET 14 AB14 LYS B 74 LEU B 76 -1 O LYS B 74 N TYR B 127
SHEET 1 BA 2 LYS B 44 ASP B 45 0
SHEET 2 BA 2 TYR B 79 LYS B 80 -1 O LYS B 80 N LYS B 44
SHEET 1 CA 2 LYS C 44 ASP C 45 0
SHEET 2 CA 2 TYR C 79 LYS C 80 -1 O LYS C 80 N LYS C 44
SHEET 1 CB14 LYS C 74 LEU C 76 0
SHEET 2 CB14 PHE C 121 ASN C 128 -1 O MET C 125 N LEU C 76
SHEET 3 CB14 ARG C 133 GLY C 140 -1 O ARG C 133 N ASN C 128
SHEET 4 CB14 VAL C 193 GLU C 204 -1 O VAL C 194 N PHE C 138
SHEET 5 CB14 LYS C 207 SER C 216 -1 O LYS C 207 N GLU C 204
SHEET 6 CB14 LEU C 222 ILE C 231 -1 N TYR C 223 O VAL C 214
SHEET 7 CB14 MET C 176 TYR C 184 -1 O MET C 176 N ILE C 231
SHEET 8 CB14 VAL D 175 TYR D 184 -1 O ALA D 178 N TYR C 184
SHEET 9 CB14 LEU D 222 LYS D 232 -1 O GLU D 225 N ASN D 183
SHEET 10 CB14 LYS D 207 SER D 216 -1 O PHE D 208 N PHE D 230
SHEET 11 CB14 VAL D 193 GLU D 204 -1 O MET D 195 N GLN D 215
SHEET 12 CB14 ARG D 133 GLY D 140 -1 O MET D 134 N SER D 198
SHEET 13 CB14 PHE D 121 ASN D 128 -1 O GLU D 122 N GLN D 139
SHEET 14 CB14 LYS D 74 LEU D 76 -1 O LYS D 74 N TYR D 127
CRYST1 50.539 58.211 69.681 89.96 71.14 64.60 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019787 -0.009395 -0.008385 0.00000
SCALE2 0.000000 0.019017 0.003110 0.00000
SCALE3 0.000000 0.000000 0.015367 0.00000
MTRIX1 1 -0.181000 -0.938300 0.294500 5.00900 1
MTRIX2 1 -0.935600 0.072060 -0.345600 6.25800 1
MTRIX3 1 0.303100 -0.338100 -0.891000 5.96600 1
MTRIX1 2 -0.613800 -0.734200 -0.290200 62.40000 1
MTRIX2 2 0.642600 -0.678200 0.356600 -58.26000 1
MTRIX3 2 -0.458600 0.032330 0.888000 -8.17800 1
MTRIX1 3 -0.633500 0.773700 0.005155 45.27000 1
MTRIX2 3 0.773700 0.633500 -0.002555 -53.63000 1
MTRIX3 3 -0.005242 0.002370 -1.000000 52.11000 1
(ATOM LINES ARE NOT SHOWN.)
END
