HEADER OXIDOREDUCTASE 03-DEC-15 5FPV
TITLE CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH COMPOUND KDOAM20A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: RESIDUES 4-354;
COMPND 5 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,
COMPND 6 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
COMPND 7 EC: 1.14.11.27, 1.14.11.-;
COMPND 8 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS OXIDOREDUCTASE, JMJD2A, KDM4A
EXPDTA X-RAY DIFFRACTION
AUTHOR V.SRIKANNATHASAN,C.GILEADI,F.VON DELFT,C.H.ARROWSMITH,C.BOUNTRA,
AUTHOR 2 A.EDWARDS,U.OPPERMANN
REVDAT 5 10-JAN-24 5FPV 1 REMARK LINK
REVDAT 4 29-JUN-16 5FPV 1 JRNL
REVDAT 3 01-JUN-16 5FPV 1 JRNL
REVDAT 2 25-MAY-16 5FPV 1 JRNL
REVDAT 1 13-JAN-16 5FPV 0
JRNL AUTH C.JOHANSSON,S.VELUPILLAI,A.TUMBER,A.SZYKOWSKA,E.S.HOOKWAY,
JRNL AUTH 2 R.P.NOWAK,C.STRAIN-DAMERELL,C.GILEADI,M.PHILPOTT,
JRNL AUTH 3 N.BURGESS-BROWN,N.WU,J.KOPEC,A.NUZZI,H.STEUBER,U.EGNER,
JRNL AUTH 4 V.BADOCK,S.MUNRO,N.B.LATHANGUE,S.WESTAWAY,J.BROWN,
JRNL AUTH 5 N.ATHANASOU,R.PRINJHA,P.E.BRENNAN,U.OPPERMANN
JRNL TITL STRUCTURAL ANALYSIS OF HUMAN KDM5B GUIDES HISTONE
JRNL TITL 2 DEMETHYLASE INHIBITOR DEVELOPMENT.
JRNL REF NAT.CHEM.BIOL. V. 12 539 2016
JRNL REFN ISSN 1552-4450
JRNL PMID 27214403
JRNL DOI 10.1038/NCHEMBIO.2087
REMARK 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 125508
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 85.3796 - 7.5799 0.97 4068 208 0.1813 0.2062
REMARK 3 2 7.5799 - 6.0169 0.94 3837 184 0.1826 0.2207
REMARK 3 3 6.0169 - 5.2565 0.98 3997 208 0.1768 0.2045
REMARK 3 4 5.2565 - 4.7759 0.99 3987 258 0.1561 0.1768
REMARK 3 5 4.7759 - 4.4336 0.99 3984 222 0.1462 0.1618
REMARK 3 6 4.4336 - 4.1722 0.99 4022 187 0.1583 0.1926
REMARK 3 7 4.1722 - 3.9633 0.99 4011 214 0.1652 0.2103
REMARK 3 8 3.9633 - 3.7907 0.99 4005 191 0.1741 0.2027
REMARK 3 9 3.7907 - 3.6448 0.99 4004 222 0.1826 0.2336
REMARK 3 10 3.6448 - 3.5190 0.99 4019 192 0.1856 0.2017
REMARK 3 11 3.5190 - 3.4090 1.00 4001 218 0.1960 0.2150
REMARK 3 12 3.4090 - 3.3116 0.99 4009 214 0.2103 0.2375
REMARK 3 13 3.3116 - 3.2244 0.94 3818 185 0.2095 0.1928
REMARK 3 14 3.2244 - 3.1457 0.94 3786 206 0.2021 0.2543
REMARK 3 15 3.1457 - 3.0742 0.96 3895 190 0.2032 0.2523
REMARK 3 16 3.0742 - 3.0088 0.98 3916 203 0.2134 0.2562
REMARK 3 17 3.0088 - 2.9486 0.99 3996 200 0.2206 0.2729
REMARK 3 18 2.9486 - 2.8929 0.99 3963 186 0.2211 0.2728
REMARK 3 19 2.8929 - 2.8413 0.99 4039 209 0.2281 0.2458
REMARK 3 20 2.8413 - 2.7931 0.99 3970 207 0.2322 0.2724
REMARK 3 21 2.7931 - 2.7480 0.99 4015 202 0.2392 0.2871
REMARK 3 22 2.7480 - 2.7058 1.00 3976 215 0.2398 0.2967
REMARK 3 23 2.7058 - 2.6660 1.00 3975 210 0.2345 0.2884
REMARK 3 24 2.6660 - 2.6284 1.00 4072 205 0.2442 0.2919
REMARK 3 25 2.6284 - 2.5929 1.00 3978 206 0.2451 0.2838
REMARK 3 26 2.5929 - 2.5592 0.99 4021 202 0.2541 0.3026
REMARK 3 27 2.5592 - 2.5272 0.99 3920 210 0.2651 0.3094
REMARK 3 28 2.5272 - 2.4968 0.99 4035 200 0.2583 0.3323
REMARK 3 29 2.4968 - 2.4677 0.99 3972 233 0.2760 0.3309
REMARK 3 30 2.4677 - 2.4400 0.99 4008 222 0.2635 0.2949
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 22771
REMARK 3 ANGLE : 1.136 30917
REMARK 3 CHIRALITY : 0.042 3195
REMARK 3 PLANARITY : 0.005 3951
REMARK 3 DIHEDRAL : 13.910 8171
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): 67.1046 16.4210 39.3987
REMARK 3 T TENSOR
REMARK 3 T11: 0.2234 T22: 0.2169
REMARK 3 T33: 0.2036 T12: 0.0103
REMARK 3 T13: 0.0108 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.0139 L22: 0.1207
REMARK 3 L33: 0.0722 L12: -0.0142
REMARK 3 L13: 0.0208 L23: -0.0771
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: 0.0112 S13: 0.0003
REMARK 3 S21: -0.0359 S22: -0.0183 S23: -0.0177
REMARK 3 S31: -0.0188 S32: 0.0222 S33: 0.0001
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 5FPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1290065700.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : M
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 438854
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 106.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4URA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 5.9, 0.15M AMMONIUM
REMARK 280 SULFATE, 11% PEG3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 51.75450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
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: E
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: 6
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: F
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: 7
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: G
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: 8
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: H
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 SER A 1
REMARK 465 MET A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 THR A 8
REMARK 465 LEU A 9
REMARK 465 ASN A 10
REMARK 465 PRO A 11
REMARK 465 GLU A 162
REMARK 465 LYS A 163
REMARK 465 GLU A 164
REMARK 465 SER A 165
REMARK 465 GLY A 166
REMARK 465 ILE A 167
REMARK 465 THR A 168
REMARK 465 ILE A 169
REMARK 465 GLU A 357
REMARK 465 SER A 358
REMARK 465 GLU A 359
REMARK 465 LEU A 360
REMARK 465 SER B 1
REMARK 465 MET B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 THR B 8
REMARK 465 GLU B 164
REMARK 465 SER B 165
REMARK 465 GLY B 166
REMARK 465 ILE B 167
REMARK 465 THR B 168
REMARK 465 GLU B 357
REMARK 465 SER B 358
REMARK 465 GLU B 359
REMARK 465 LEU B 360
REMARK 465 SER C 1
REMARK 465 MET C 2
REMARK 465 ALA C 3
REMARK 465 SER C 4
REMARK 465 GLU C 5
REMARK 465 SER C 6
REMARK 465 GLU C 7
REMARK 465 THR C 8
REMARK 465 GLU C 164
REMARK 465 SER C 165
REMARK 465 GLY C 166
REMARK 465 ILE C 167
REMARK 465 THR C 168
REMARK 465 ILE C 169
REMARK 465 GLU C 357
REMARK 465 SER C 358
REMARK 465 GLU C 359
REMARK 465 LEU C 360
REMARK 465 SER D 1
REMARK 465 MET D 2
REMARK 465 ALA D 3
REMARK 465 SER D 4
REMARK 465 GLU D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 THR D 8
REMARK 465 GLU D 164
REMARK 465 SER D 165
REMARK 465 GLY D 166
REMARK 465 ILE D 167
REMARK 465 THR D 168
REMARK 465 ILE D 169
REMARK 465 GLU D 357
REMARK 465 SER D 358
REMARK 465 GLU D 359
REMARK 465 LEU D 360
REMARK 465 SER E 1
REMARK 465 MET E 2
REMARK 465 ALA E 3
REMARK 465 SER E 4
REMARK 465 GLU E 5
REMARK 465 SER E 6
REMARK 465 GLU E 7
REMARK 465 THR E 8
REMARK 465 LYS E 163
REMARK 465 GLU E 164
REMARK 465 SER E 165
REMARK 465 GLY E 166
REMARK 465 ILE E 167
REMARK 465 THR E 168
REMARK 465 ILE E 169
REMARK 465 GLU E 357
REMARK 465 SER E 358
REMARK 465 GLU E 359
REMARK 465 LEU E 360
REMARK 465 SER F 1
REMARK 465 MET F 2
REMARK 465 ALA F 3
REMARK 465 SER F 4
REMARK 465 GLU F 5
REMARK 465 SER F 6
REMARK 465 GLU F 7
REMARK 465 THR F 8
REMARK 465 GLU F 164
REMARK 465 SER F 165
REMARK 465 GLY F 166
REMARK 465 ILE F 167
REMARK 465 THR F 168
REMARK 465 ILE F 169
REMARK 465 GLU F 357
REMARK 465 SER F 358
REMARK 465 GLU F 359
REMARK 465 LEU F 360
REMARK 465 SER G 1
REMARK 465 MET G 2
REMARK 465 ALA G 3
REMARK 465 SER G 4
REMARK 465 GLU G 5
REMARK 465 SER G 6
REMARK 465 GLU G 7
REMARK 465 THR G 8
REMARK 465 SER G 165
REMARK 465 GLY G 166
REMARK 465 ILE G 167
REMARK 465 THR G 168
REMARK 465 ILE G 169
REMARK 465 GLU G 357
REMARK 465 SER G 358
REMARK 465 GLU G 359
REMARK 465 LEU G 360
REMARK 465 SER H 1
REMARK 465 MET H 2
REMARK 465 ALA H 3
REMARK 465 SER H 4
REMARK 465 GLU H 5
REMARK 465 SER H 6
REMARK 465 GLU H 7
REMARK 465 THR H 8
REMARK 465 LYS H 163
REMARK 465 GLU H 164
REMARK 465 SER H 165
REMARK 465 GLY H 166
REMARK 465 ILE H 167
REMARK 465 THR H 168
REMARK 465 ILE H 169
REMARK 465 GLU H 170
REMARK 465 GLU H 357
REMARK 465 SER H 358
REMARK 465 GLU H 359
REMARK 465 LEU H 360
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ASP A 65 CG OD1 OD2
REMARK 470 ARG A 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 ARG A 111 CD NE CZ NH1 NH2
REMARK 470 GLU A 114 CD OE1 OE2
REMARK 470 GLU A 116 CG CD OE1 OE2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 ARG A 155 NE CZ NH1 NH2
REMARK 470 ARG A 222 CD NE CZ NH1 NH2
REMARK 470 LYS A 225 CE NZ
REMARK 470 GLN A 233 CG CD OE1 NE2
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 LYS A 252 NZ
REMARK 470 LYS A 253 CE NZ
REMARK 470 ARG A 295 CZ NH1 NH2
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 ASP A 312 CG OD1 OD2
REMARK 470 LYS A 331 CD CE NZ
REMARK 470 LYS A 356 CG CD CE NZ
REMARK 470 GLU B 23 CG CD OE1 OE2
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 ASP B 65 CG OD1 OD2
REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 111 CD NE CZ NH1 NH2
REMARK 470 GLU B 114 CD OE1 OE2
REMARK 470 GLU B 116 CG CD OE1 OE2
REMARK 470 LYS B 144 CG CD CE NZ
REMARK 470 ARG B 155 NE CZ NH1 NH2
REMARK 470 LYS B 163 CG CD CE NZ
REMARK 470 ARG B 222 CD NE CZ NH1 NH2
REMARK 470 LYS B 225 CE NZ
REMARK 470 GLN B 233 CG CD OE1 NE2
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 LYS B 252 NZ
REMARK 470 LYS B 253 CE NZ
REMARK 470 ARG B 295 CZ NH1 NH2
REMARK 470 ARG B 310 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 311 CG CD CE NZ
REMARK 470 ASP B 312 CG OD1 OD2
REMARK 470 MET B 313 CG SD CE
REMARK 470 LYS B 331 CD CE NZ
REMARK 470 LYS B 356 CG CD CE NZ
REMARK 470 GLU C 23 CG CD OE1 OE2
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 LYS C 55 CG CD CE NZ
REMARK 470 ARG C 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 100 CG CD CE NZ
REMARK 470 ARG C 111 CD NE CZ NH1 NH2
REMARK 470 GLU C 114 CD OE1 OE2
REMARK 470 GLU C 116 CG CD OE1 OE2
REMARK 470 LYS C 144 CG CD CE NZ
REMARK 470 ARG C 155 NE CZ NH1 NH2
REMARK 470 LYS C 163 CG CD CE NZ
REMARK 470 ARG C 222 CD NE CZ NH1 NH2
REMARK 470 LYS C 225 CE NZ
REMARK 470 GLN C 233 CG CD OE1 NE2
REMARK 470 GLU C 236 CG CD OE1 OE2
REMARK 470 LYS C 252 NZ
REMARK 470 LYS C 253 CE NZ
REMARK 470 ARG C 295 CZ NH1 NH2
REMARK 470 LYS C 311 CG CD CE NZ
REMARK 470 ASP C 312 CG OD1 OD2
REMARK 470 LYS C 331 CD CE NZ
REMARK 470 LYS C 356 CG CD CE NZ
REMARK 470 GLU D 23 CG CD OE1 OE2
REMARK 470 LYS D 55 CG CD CE NZ
REMARK 470 ASP D 65 CG OD1 OD2
REMARK 470 ARG D 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 100 CG CD CE NZ
REMARK 470 ARG D 111 CD NE CZ NH1 NH2
REMARK 470 GLU D 114 CD OE1 OE2
REMARK 470 GLU D 116 CG CD OE1 OE2
REMARK 470 LYS D 144 CG CD CE NZ
REMARK 470 ARG D 155 NE CZ NH1 NH2
REMARK 470 ARG D 222 CD NE CZ NH1 NH2
REMARK 470 LYS D 225 CE NZ
REMARK 470 GLN D 233 CG CD OE1 NE2
REMARK 470 GLU D 236 CG CD OE1 OE2
REMARK 470 LYS D 252 NZ
REMARK 470 LYS D 253 CE NZ
REMARK 470 ARG D 295 CZ NH1 NH2
REMARK 470 LYS D 311 CG CD CE NZ
REMARK 470 ASP D 312 CG OD1 OD2
REMARK 470 LYS D 331 CD CE NZ
REMARK 470 LYS D 356 CG CD CE NZ
REMARK 470 GLU E 23 CG CD OE1 OE2
REMARK 470 LYS E 55 CG CD CE NZ
REMARK 470 ASP E 65 CG OD1 OD2
REMARK 470 LYS E 91 CG CD CE NZ
REMARK 470 ARG E 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 100 CG CD CE NZ
REMARK 470 ARG E 111 CD NE CZ NH1 NH2
REMARK 470 GLU E 114 CD OE1 OE2
REMARK 470 GLU E 116 CG CD OE1 OE2
REMARK 470 LYS E 144 CG CD CE NZ
REMARK 470 ARG E 155 NE CZ NH1 NH2
REMARK 470 ARG E 222 CD NE CZ NH1 NH2
REMARK 470 LYS E 225 CE NZ
REMARK 470 GLN E 233 CG CD OE1 NE2
REMARK 470 GLU E 236 CG CD OE1 OE2
REMARK 470 LYS E 252 NZ
REMARK 470 LYS E 253 CE NZ
REMARK 470 ARG E 295 CZ NH1 NH2
REMARK 470 LYS E 311 CG CD CE NZ
REMARK 470 ASP E 312 CG OD1 OD2
REMARK 470 LYS E 331 CD CE NZ
REMARK 470 LYS E 356 CG CD CE NZ
REMARK 470 GLU F 23 CG CD OE1 OE2
REMARK 470 LYS F 55 CG CD CE NZ
REMARK 470 ASP F 65 CG OD1 OD2
REMARK 470 ARG F 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 100 CG CD CE NZ
REMARK 470 ARG F 111 CD NE CZ NH1 NH2
REMARK 470 GLU F 114 CD OE1 OE2
REMARK 470 GLU F 116 CG CD OE1 OE2
REMARK 470 LYS F 144 CG CD CE NZ
REMARK 470 ARG F 155 NE CZ NH1 NH2
REMARK 470 LYS F 163 CG CD CE NZ
REMARK 470 ARG F 222 CD NE CZ NH1 NH2
REMARK 470 LYS F 225 CE NZ
REMARK 470 GLN F 233 CG CD OE1 NE2
REMARK 470 GLU F 236 CG CD OE1 OE2
REMARK 470 LYS F 252 NZ
REMARK 470 LYS F 253 CE NZ
REMARK 470 ARG F 295 CZ NH1 NH2
REMARK 470 LYS F 331 CD CE NZ
REMARK 470 LYS F 356 CG CD CE NZ
REMARK 470 GLU G 23 CG CD OE1 OE2
REMARK 470 LYS G 55 CG CD CE NZ
REMARK 470 ASP G 65 CG OD1 OD2
REMARK 470 LYS G 100 CG CD CE NZ
REMARK 470 ARG G 111 CD NE CZ NH1 NH2
REMARK 470 GLU G 114 CD OE1 OE2
REMARK 470 GLU G 116 CG CD OE1 OE2
REMARK 470 LYS G 144 CG CD CE NZ
REMARK 470 ARG G 155 NE CZ NH1 NH2
REMARK 470 LYS G 163 CG CD CE NZ
REMARK 470 GLU G 164 CG CD OE1 OE2
REMARK 470 ARG G 222 CD NE CZ NH1 NH2
REMARK 470 LYS G 225 CE NZ
REMARK 470 GLN G 233 CG CD OE1 NE2
REMARK 470 GLU G 236 CG CD OE1 OE2
REMARK 470 LYS G 252 NZ
REMARK 470 LYS G 253 CE NZ
REMARK 470 ARG G 295 CZ NH1 NH2
REMARK 470 LYS G 311 CG CD CE NZ
REMARK 470 LYS G 331 CD CE NZ
REMARK 470 LYS G 356 CG CD CE NZ
REMARK 470 GLU H 23 CG CD OE1 OE2
REMARK 470 LYS H 55 CG CD CE NZ
REMARK 470 LYS H 100 CG CD CE NZ
REMARK 470 ARG H 111 CD NE CZ NH1 NH2
REMARK 470 GLU H 114 CD OE1 OE2
REMARK 470 GLU H 116 CG CD OE1 OE2
REMARK 470 LYS H 144 CG CD CE NZ
REMARK 470 ARG H 155 NE CZ NH1 NH2
REMARK 470 ARG H 222 CD NE CZ NH1 NH2
REMARK 470 LYS H 225 CE NZ
REMARK 470 GLN H 233 CG CD OE1 NE2
REMARK 470 GLU H 236 CG CD OE1 OE2
REMARK 470 LYS H 252 NZ
REMARK 470 LYS H 253 CE NZ
REMARK 470 ARG H 295 CZ NH1 NH2
REMARK 470 LYS H 311 CG CD CE NZ
REMARK 470 LYS H 331 CD CE NZ
REMARK 470 LYS H 356 CG CD CE NZ
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 O TYR B 330 O HOH B 2125 1.81
REMARK 500 OG SER F 59 OD1 ASP F 61 1.83
REMARK 500 OD1 ASN E 10 OG SER E 12 1.83
REMARK 500 O HOH D 2061 O HOH D 2062 2.02
REMARK 500 N LYS B 334 O HOH B 2125 2.03
REMARK 500 O HOH D 2029 O HOH D 2062 2.06
REMARK 500 OE1 GLU B 264 O HOH B 2026 2.09
REMARK 500 O HOH C 2008 O HOH C 2013 2.10
REMARK 500 OH TYR A 19 O HOH A 2008 2.10
REMARK 500 O ILE C 15 O HOH C 2004 2.11
REMARK 500 OE2 GLU B 353 NE2 HIS C 145 2.11
REMARK 500 O ASP B 65 O HOH B 2036 2.11
REMARK 500 O HOH D 2042 O HOH D 2044 2.11
REMARK 500 O HOH C 2001 O HOH C 2002 2.12
REMARK 500 O LYS H 91 O HOH H 2035 2.13
REMARK 500 NH1 ARG C 329 O HOH C 2127 2.13
REMARK 500 O HOH E 2025 O HOH E 2031 2.14
REMARK 500 O HOH F 2025 O HOH F 2026 2.14
REMARK 500 O HOH H 2072 O HOH H 2077 2.14
REMARK 500 OE1 GLU B 264 O HOH B 2025 2.15
REMARK 500 O TRP G 54 O HOH G 2012 2.16
REMARK 500 O HOH B 2051 O HOH G 2018 2.16
REMARK 500 O PRO D 50 O HOH D 2016 2.16
REMARK 500 O HOH B 2033 O HOH B 2085 2.18
REMARK 500 OD1 ASP B 64 O HOH B 2029 2.18
REMARK 500 NH2 ARG E 30 OE2 GLU E 353 2.18
REMARK 500 O HOH C 2016 O HOH C 2050 2.18
REMARK 500 OE2 GLU D 205 O HOH D 2097 2.19
REMARK 500 NH1 ARG G 96 O HOH G 2024 2.19
REMARK 500 O LYS E 90 O HOH E 2015 2.19
REMARK 500 O LYS H 90 O HOH H 2029 2.19
REMARK 500 OG1 THR F 262 O HOH F 2058 2.19
REMARK 500 OE2 GLU C 205 O HOH C 2110 2.19
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 HOH D 2102 O HOH F 2068 2645 2.10
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 TYR D 330 CZ TYR D 330 CE2 -0.122
REMARK 500 LYS D 331 CA LYS D 331 CB 0.204
REMARK 500 LYS D 334 CD LYS D 334 CE 0.154
REMARK 500 LYS D 334 CE LYS D 334 NZ 0.333
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 LEU B 75 CA - CB - CG ANGL. DEV. = -14.1 DEGREES
REMARK 500 ASP C 319 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LYS D 334 CD - CE - NZ ANGL. DEV. = 15.3 DEGREES
REMARK 500 PRO E 11 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASP H 312 CB - CG - OD1 ANGL. DEV. = 7.2 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 ALA A 13 53.30 -111.19
REMARK 500 SER A 113 -68.66 -100.15
REMARK 500 ARG A 153 66.08 -152.99
REMARK 500 LYS A 183 4.46 80.93
REMARK 500 ALA A 237 53.74 -149.20
REMARK 500 GLU B 53 -35.19 -38.52
REMARK 500 SER B 113 -68.42 -101.72
REMARK 500 ARG B 153 63.04 -156.74
REMARK 500 LYS B 183 -0.29 75.03
REMARK 500 ALA B 237 59.52 -146.30
REMARK 500 ASP B 312 -124.62 63.13
REMARK 500 MET B 313 164.00 71.80
REMARK 500 GLU B 353 -37.01 -38.94
REMARK 500 SER C 113 -68.22 -99.51
REMARK 500 ARG C 153 62.43 -154.13
REMARK 500 ALA C 237 59.33 -142.82
REMARK 500 LEU C 355 -77.66 -110.90
REMARK 500 SER D 113 -65.47 -101.97
REMARK 500 ARG D 153 67.88 -153.40
REMARK 500 LYS D 183 -1.56 76.20
REMARK 500 ASP D 312 17.86 83.60
REMARK 500 LYS D 334 -38.00 -34.37
REMARK 500 LEU D 355 -62.58 -103.68
REMARK 500 ASN E 10 67.88 29.12
REMARK 500 SER E 113 -69.01 -102.07
REMARK 500 ARG E 153 67.95 -157.45
REMARK 500 LEU E 355 -93.02 -109.71
REMARK 500 ASN F 10 70.34 39.43
REMARK 500 SER F 113 -69.15 -101.30
REMARK 500 ARG F 153 67.40 -156.64
REMARK 500 ALA F 237 59.45 -146.21
REMARK 500 LYS F 311 -176.00 -60.39
REMARK 500 ASP F 312 -7.28 85.43
REMARK 500 LEU F 355 -80.97 -110.81
REMARK 500 SER G 113 -61.69 -108.38
REMARK 500 ARG G 153 67.48 -155.44
REMARK 500 SER H 113 -67.48 -98.71
REMARK 500 ARG H 153 70.38 -152.01
REMARK 500 ALA H 237 58.57 -149.46
REMARK 500 ASP H 312 -28.95 107.99
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 LEU E 9 ASN E 10 -147.46
REMARK 500 LEU F 9 ASN F 10 -149.08
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 B2012 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH F2090 DISTANCE = 7.53 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 189 NE2
REMARK 620 2 GLU A 191 OE2 94.0
REMARK 620 3 HIS A 277 NE2 87.4 88.8
REMARK 620 4 MMK A1358 N 82.8 95.4 169.6
REMARK 620 5 MMK A1358 NAR 99.0 162.6 103.1 75.1
REMARK 620 6 HOH A2094 O 174.9 82.3 96.1 93.9 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 235 SG
REMARK 620 2 HIS A 241 NE2 117.2
REMARK 620 3 CYS A 307 SG 118.0 109.7
REMARK 620 4 CYS A 309 SG 111.7 90.1 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 189 NE2
REMARK 620 2 GLU B 191 OE2 91.7
REMARK 620 3 HIS B 277 NE2 83.5 88.2
REMARK 620 4 MMK B1358 N 88.1 98.1 169.6
REMARK 620 5 MMK B1358 NAR 98.7 163.9 105.1 70.2
REMARK 620 6 HOH B2095 O 175.2 86.7 92.0 96.6 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 235 SG
REMARK 620 2 HIS B 241 NE2 142.1
REMARK 620 3 CYS B 309 SG 111.4 68.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 189 NE2
REMARK 620 2 GLU C 191 OE2 89.3
REMARK 620 3 HIS C 277 NE2 83.9 91.8
REMARK 620 4 MMK C1358 NAR 96.9 164.6 102.9
REMARK 620 5 MMK C1358 N 80.8 90.7 164.4 76.5
REMARK 620 6 HOH C2103 O 176.1 92.5 92.5 82.2 102.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 235 SG
REMARK 620 2 HIS C 241 NE2 113.5
REMARK 620 3 CYS C 307 SG 111.4 115.1
REMARK 620 4 CYS C 309 SG 116.1 94.2 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 189 NE2
REMARK 620 2 GLU D 191 OE2 93.3
REMARK 620 3 HIS D 277 NE2 88.8 93.8
REMARK 620 4 MMK D1358 N 83.7 90.9 171.3
REMARK 620 5 MMK D1358 NAR 98.5 161.6 100.4 76.7
REMARK 620 6 HOH D2089 O 177.0 83.9 90.3 97.4 84.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 235 SG
REMARK 620 2 HIS D 241 NE2 110.4
REMARK 620 3 CYS D 307 SG 115.2 113.8
REMARK 620 4 CYS D 309 SG 116.3 90.5 108.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 189 NE2
REMARK 620 2 GLU E 191 OE2 90.8
REMARK 620 3 HIS E 277 NE2 85.9 87.8
REMARK 620 4 MMK E1358 N 78.6 98.3 163.3
REMARK 620 5 MMK E1358 NAR 98.5 162.5 107.6 69.3
REMARK 620 6 HOH E2057 O 178.4 90.5 95.1 100.3 80.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 235 SG
REMARK 620 2 HIS E 241 NE2 117.1
REMARK 620 3 CYS E 307 SG 111.3 110.2
REMARK 620 4 CYS E 309 SG 112.8 94.4 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN F1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 189 NE2
REMARK 620 2 GLU F 191 OE2 92.1
REMARK 620 3 HIS F 277 NE2 87.4 87.0
REMARK 620 4 MMK F1358 N 82.6 101.6 167.1
REMARK 620 5 MMK F1358 NAR 99.3 165.9 101.7 72.0
REMARK 620 6 HOH F2049 O 177.7 85.9 91.3 98.9 82.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 235 SG
REMARK 620 2 HIS F 241 NE2 119.4
REMARK 620 3 CYS F 307 SG 107.6 107.4
REMARK 620 4 CYS F 309 SG 119.7 94.5 107.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN G1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 189 NE2
REMARK 620 2 GLU G 191 OE2 89.4
REMARK 620 3 HIS G 277 NE2 85.9 89.8
REMARK 620 4 MMK G1358 NAR 101.8 159.4 108.1
REMARK 620 5 MMK G1358 N 81.5 92.5 167.2 72.5
REMARK 620 6 HOH G2044 O 172.0 82.8 92.5 86.2 100.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 235 SG
REMARK 620 2 HIS G 241 NE2 113.3
REMARK 620 3 CYS G 307 SG 114.5 108.4
REMARK 620 4 CYS G 309 SG 112.5 94.3 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN H1357 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 189 NE2
REMARK 620 2 GLU H 191 OE2 94.0
REMARK 620 3 HIS H 277 NE2 89.4 89.4
REMARK 620 4 MMK H1358 NAR 98.4 161.6 104.1
REMARK 620 5 MMK H1358 N 80.8 95.9 169.2 73.0
REMARK 620 6 HOH H2075 O 177.5 83.7 89.5 84.1 100.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H1359 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 235 SG
REMARK 620 2 HIS H 241 NE2 113.7
REMARK 620 3 CYS H 307 SG 112.0 112.3
REMARK 620 4 CYS H 309 SG 112.3 95.4 110.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI H1363 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H2119 O
REMARK 620 2 HOH H2120 O 68.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK A 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK B 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK C 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK D 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK E 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK F 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK G 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI G 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN H 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MMK H 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI H 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI H 1361
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI H 1363
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FPL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JARID1B IN COMPLEX WITH CCT363901
REMARK 900 RELATED ID: 5FPU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JARID1B IN COMPLEX WITH GSKJ1
DBREF 5FPV A 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV B 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV C 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV D 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV E 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV F 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV G 2 360 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FPV H 2 360 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 5FPV SER A 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER B 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER C 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER D 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER E 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER F 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER G 1 UNP O75164 EXPRESSION TAG
SEQADV 5FPV SER H 1 UNP O75164 EXPRESSION TAG
SEQRES 1 A 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 A 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 A 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 A 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 A 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 A 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 A 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 A 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 A 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 A 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 A 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 A 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 A 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 A 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 A 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 A 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 A 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 A 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 A 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 A 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 A 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 A 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 A 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 A 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 A 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 A 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 A 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 A 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 B 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 B 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 B 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 B 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 B 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 B 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 B 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 B 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 B 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 B 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 B 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 B 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 B 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 B 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 B 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 B 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 B 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 B 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 B 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 B 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 B 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 B 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 B 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 B 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 B 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 B 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 B 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 B 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 C 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 C 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 C 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 C 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 C 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 C 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 C 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 C 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 C 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 C 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 C 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 C 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 C 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 C 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 C 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 C 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 C 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 C 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 C 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 C 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 C 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 C 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 C 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 C 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 C 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 C 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 C 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 C 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 D 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 D 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 D 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 D 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 D 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 D 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 D 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 D 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 D 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 D 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 D 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 D 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 D 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 D 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 D 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 D 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 D 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 D 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 D 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 D 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 D 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 D 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 D 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 D 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 D 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 D 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 D 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 D 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 E 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 E 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 E 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 E 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 E 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 E 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 E 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 E 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 E 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 E 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 E 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 E 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 E 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 E 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 E 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 E 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 E 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 E 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 E 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 E 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 E 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 E 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 E 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 E 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 E 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 E 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 E 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 E 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 F 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 F 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 F 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 F 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 F 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 F 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 F 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 F 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 F 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 F 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 F 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 F 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 F 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 F 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 F 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 F 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 F 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 F 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 F 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 F 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 F 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 F 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 F 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 F 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 F 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 F 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 F 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 F 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 G 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 G 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 G 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 G 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 G 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 G 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 G 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 G 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 G 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 G 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 G 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 G 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 G 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 G 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 G 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 G 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 G 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 G 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 G 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 G 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 G 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 G 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 G 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 G 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 G 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 G 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 G 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 G 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 H 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 H 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 H 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 H 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 H 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 H 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 H 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 H 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 H 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 H 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 H 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 H 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 H 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 H 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 H 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 H 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 H 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 H 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 H 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 H 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 H 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 H 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 H 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 H 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 H 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 H 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 H 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 H 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
HET MN A1357 1
HET MMK A1358 22
HET ZN A1359 1
HET NI A1360 1
HET NI A1361 1
HET NI A1362 1
HET MN B1357 1
HET MMK B1358 22
HET ZN B1359 1
HET NI B1360 1
HET NI B1361 1
HET MN C1357 1
HET MMK C1358 22
HET ZN C1359 1
HET NI C1360 1
HET NI C1361 1
HET MN D1357 1
HET MMK D1358 22
HET ZN D1359 1
HET NI D1360 1
HET NI D1361 1
HET NI D1362 1
HET MN E1357 1
HET MMK E1358 22
HET ZN E1359 1
HET MN F1357 1
HET MMK F1358 22
HET ZN F1359 1
HET MN G1357 1
HET MMK G1358 22
HET ZN G1359 1
HET NI G1360 1
HET MN H1357 1
HET MMK H1358 22
HET ZN H1359 1
HET NI H1360 1
HET NI H1361 1
HET NI H1362 1
HET NI H1363 1
HETNAM MN MANGANESE (II) ION
HETNAM MMK 2-{[(2-{[(E)-2-(DIMETHYLAMINO)ETHENYL](ETHYL)AMINO}-2-
HETNAM 2 MMK OXOETHYL)AMINO]METHYL}PYRIDINE-4-CARBOXYLIC ACID
HETNAM ZN ZINC ION
HETNAM NI NICKEL (II) ION
FORMUL 9 MN 8(MN 2+)
FORMUL 10 MMK 8(C15 H22 N4 O3)
FORMUL 11 ZN 8(ZN 2+)
FORMUL 12 NI 15(NI 2+)
FORMUL 48 HOH *891(H2 O)
HELIX 1 1 THR A 21 ARG A 26 1 6
HELIX 2 2 ASN A 27 GLN A 38 1 12
HELIX 3 3 GLY A 39 ALA A 43 5 5
HELIX 4 4 VAL A 95 SER A 104 1 10
HELIX 5 5 GLU A 114 LEU A 126 1 13
HELIX 6 6 THR A 156 VAL A 161 5 6
HELIX 7 7 GLU A 191 LEU A 195 5 5
HELIX 8 8 PRO A 213 GLU A 215 5 3
HELIX 9 9 HIS A 216 PHE A 228 1 13
HELIX 10 10 PHE A 228 CYS A 235 1 8
HELIX 11 11 ALA A 237 LYS A 242 5 6
HELIX 12 12 SER A 247 TYR A 254 1 8
HELIX 13 13 ARG A 296 ALA A 304 1 9
HELIX 14 14 MET A 318 GLN A 326 1 9
HELIX 15 15 ARG A 329 ALA A 335 1 7
HELIX 16 16 THR A 348 LEU A 355 5 8
HELIX 17 17 THR B 21 ARG B 26 1 6
HELIX 18 18 ASN B 27 GLN B 38 1 12
HELIX 19 19 GLY B 39 ALA B 43 5 5
HELIX 20 20 VAL B 95 SER B 104 1 10
HELIX 21 21 GLU B 114 LEU B 126 1 13
HELIX 22 22 THR B 156 GLU B 162 5 7
HELIX 23 23 GLU B 191 LEU B 195 5 5
HELIX 24 24 PRO B 213 GLU B 215 5 3
HELIX 25 25 HIS B 216 PHE B 228 1 13
HELIX 26 26 PHE B 228 CYS B 235 1 8
HELIX 27 27 ALA B 237 LYS B 242 5 6
HELIX 28 28 SER B 247 TYR B 254 1 8
HELIX 29 29 ARG B 296 ALA B 304 1 9
HELIX 30 30 MET B 318 GLN B 326 1 9
HELIX 31 31 ARG B 329 ALA B 335 1 7
HELIX 32 32 THR B 348 LEU B 355 5 8
HELIX 33 33 THR C 21 ARG C 26 1 6
HELIX 34 34 ASN C 27 GLN C 38 1 12
HELIX 35 35 GLY C 39 ALA C 43 5 5
HELIX 36 36 VAL C 95 SER C 104 1 10
HELIX 37 37 GLU C 114 LEU C 126 1 13
HELIX 38 38 THR C 156 GLU C 162 5 7
HELIX 39 39 GLU C 191 LEU C 195 5 5
HELIX 40 40 PRO C 213 GLU C 215 5 3
HELIX 41 41 HIS C 216 PHE C 228 1 13
HELIX 42 42 PHE C 228 CYS C 235 1 8
HELIX 43 43 ALA C 237 LYS C 242 5 6
HELIX 44 44 SER C 247 TYR C 254 1 8
HELIX 45 45 ARG C 296 ALA C 304 1 9
HELIX 46 46 MET C 318 GLN C 326 1 9
HELIX 47 47 ARG C 329 ALA C 335 1 7
HELIX 48 48 THR C 348 LEU C 355 5 8
HELIX 49 49 THR D 21 ARG D 26 1 6
HELIX 50 50 ASN D 27 GLN D 38 1 12
HELIX 51 51 GLY D 39 ALA D 43 5 5
HELIX 52 52 VAL D 95 SER D 104 1 10
HELIX 53 53 GLU D 114 LEU D 126 1 13
HELIX 54 54 THR D 156 GLU D 162 5 7
HELIX 55 55 GLU D 191 LEU D 195 5 5
HELIX 56 56 PRO D 213 GLU D 215 5 3
HELIX 57 57 HIS D 216 PHE D 228 1 13
HELIX 58 58 PHE D 228 CYS D 235 1 8
HELIX 59 59 ALA D 237 LYS D 242 5 6
HELIX 60 60 SER D 247 TYR D 254 1 8
HELIX 61 61 ARG D 296 ALA D 304 1 9
HELIX 62 62 MET D 318 GLN D 326 1 9
HELIX 63 63 ARG D 329 LYS D 334 1 6
HELIX 64 64 THR D 348 LEU D 355 5 8
HELIX 65 65 THR E 21 ARG E 26 1 6
HELIX 66 66 ASN E 27 GLN E 38 1 12
HELIX 67 67 GLY E 39 ALA E 43 5 5
HELIX 68 68 VAL E 95 SER E 104 1 10
HELIX 69 69 GLU E 114 LEU E 126 1 13
HELIX 70 70 THR E 156 GLU E 162 5 7
HELIX 71 71 GLU E 191 LEU E 195 5 5
HELIX 72 72 PRO E 213 GLU E 215 5 3
HELIX 73 73 HIS E 216 PHE E 228 1 13
HELIX 74 74 PHE E 228 CYS E 235 1 8
HELIX 75 75 ALA E 237 LYS E 242 5 6
HELIX 76 76 SER E 247 TYR E 254 1 8
HELIX 77 77 ARG E 296 ALA E 304 1 9
HELIX 78 78 MET E 318 GLN E 326 1 9
HELIX 79 79 ARG E 329 ALA E 335 1 7
HELIX 80 80 THR E 348 LEU E 355 5 8
HELIX 81 81 THR F 21 ARG F 26 1 6
HELIX 82 82 ASN F 27 GLN F 38 1 12
HELIX 83 83 GLY F 39 ALA F 43 5 5
HELIX 84 84 VAL F 95 SER F 104 1 10
HELIX 85 85 GLU F 114 LEU F 126 1 13
HELIX 86 86 THR F 156 GLU F 162 5 7
HELIX 87 87 GLU F 191 LEU F 195 5 5
HELIX 88 88 PRO F 213 GLU F 215 5 3
HELIX 89 89 HIS F 216 PHE F 228 1 13
HELIX 90 90 PHE F 228 CYS F 235 1 8
HELIX 91 91 ALA F 237 LYS F 242 5 6
HELIX 92 92 SER F 247 TYR F 254 1 8
HELIX 93 93 ARG F 296 ALA F 304 1 9
HELIX 94 94 MET F 318 GLN F 326 1 9
HELIX 95 95 ARG F 329 ALA F 335 1 7
HELIX 96 96 THR F 348 LEU F 355 5 8
HELIX 97 97 THR G 21 ARG G 26 1 6
HELIX 98 98 ASN G 27 GLN G 38 1 12
HELIX 99 99 GLY G 39 ALA G 43 5 5
HELIX 100 100 VAL G 95 SER G 104 1 10
HELIX 101 101 GLU G 114 LEU G 126 1 13
HELIX 102 102 THR G 156 LEU G 158 5 3
HELIX 103 103 ASP G 159 GLU G 164 1 6
HELIX 104 104 GLU G 191 LEU G 195 5 5
HELIX 105 105 PRO G 213 GLU G 215 5 3
HELIX 106 106 HIS G 216 PHE G 228 1 13
HELIX 107 107 PHE G 228 CYS G 235 1 8
HELIX 108 108 ALA G 237 LYS G 242 5 6
HELIX 109 109 SER G 247 TYR G 254 1 8
HELIX 110 110 ARG G 296 ALA G 304 1 9
HELIX 111 111 MET G 318 GLN G 326 1 9
HELIX 112 112 ARG G 329 ALA G 335 1 7
HELIX 113 113 THR G 348 LEU G 355 5 8
HELIX 114 114 THR H 21 ARG H 26 1 6
HELIX 115 115 ASN H 27 GLN H 38 1 12
HELIX 116 116 GLY H 39 ALA H 43 5 5
HELIX 117 117 TYR H 60 ASP H 65 5 6
HELIX 118 118 VAL H 95 SER H 104 1 10
HELIX 119 119 GLU H 114 LEU H 126 1 13
HELIX 120 120 ASN H 150 LEU H 154 5 5
HELIX 121 121 THR H 156 VAL H 161 5 6
HELIX 122 122 GLU H 191 LEU H 195 5 5
HELIX 123 123 PRO H 213 GLU H 215 5 3
HELIX 124 124 HIS H 216 PHE H 228 1 13
HELIX 125 125 PHE H 228 CYS H 235 1 8
HELIX 126 126 ALA H 237 LYS H 242 5 6
HELIX 127 127 SER H 247 TYR H 254 1 8
HELIX 128 128 ARG H 296 ALA H 304 1 9
HELIX 129 129 MET H 318 GLN H 326 1 9
HELIX 130 130 ARG H 329 ALA H 335 1 7
HELIX 131 131 THR H 348 LEU H 355 5 8
SHEET 1 AA10 MET A 16 PHE A 18 0
SHEET 2 AA10 LEU A 45 VAL A 48 1 O LEU A 45 N MET A 16
SHEET 3 AA10 PHE A 268 THR A 271 -1 O PHE A 268 N VAL A 48
SHEET 4 AA10 TYR A 196 GLY A 204 -1 O SER A 197 N THR A 271
SHEET 5 AA10 ASN A 285 PHE A 292 -1 O CYS A 286 N HIS A 202
SHEET 6 AA10 TYR A 176 GLY A 180 -1 O TYR A 176 N SER A 289
SHEET 7 AA10 ILE A 132 ASN A 138 -1 O GLY A 134 N PHE A 179
SHEET 8 AA10 ILE A 72 GLN A 79 -1 O ILE A 72 N TYR A 133
SHEET 9 AA10 LEU A 82 GLN A 89 -1 O LEU A 82 N GLN A 79
SHEET 10 AA10 THR A 244 ILE A 246 -1 O LEU A 245 N PHE A 83
SHEET 1 AB 2 VAL A 67 ILE A 68 0
SHEET 2 AB 2 MET A 93 THR A 94 -1 O MET A 93 N ILE A 68
SHEET 1 AC 4 SER A 185 HIS A 189 0
SHEET 2 AC 4 TYR A 276 ASN A 281 -1 O HIS A 277 N HIS A 189
SHEET 3 AC 4 LYS A 207 VAL A 212 -1 O SER A 208 N PHE A 280
SHEET 4 AC 4 ASP A 259 GLN A 263 -1 O ASP A 259 N SER A 211
SHEET 1 BA10 MET B 16 PHE B 18 0
SHEET 2 BA10 LEU B 45 VAL B 48 1 O LEU B 45 N MET B 16
SHEET 3 BA10 PHE B 268 THR B 271 -1 O PHE B 268 N VAL B 48
SHEET 4 BA10 TYR B 196 GLY B 204 -1 O SER B 197 N THR B 271
SHEET 5 BA10 ASN B 285 PHE B 292 -1 O CYS B 286 N HIS B 202
SHEET 6 BA10 TYR B 176 GLY B 180 -1 O TYR B 176 N SER B 289
SHEET 7 BA10 ILE B 132 ASN B 138 -1 O GLY B 134 N PHE B 179
SHEET 8 BA10 ILE B 72 GLN B 79 -1 O ILE B 72 N TYR B 133
SHEET 9 BA10 LEU B 82 GLN B 89 -1 O LEU B 82 N GLN B 79
SHEET 10 BA10 THR B 244 ILE B 246 -1 O LEU B 245 N PHE B 83
SHEET 1 BB 2 VAL B 67 ILE B 68 0
SHEET 2 BB 2 MET B 93 THR B 94 -1 O MET B 93 N ILE B 68
SHEET 1 BC 4 SER B 185 HIS B 189 0
SHEET 2 BC 4 TYR B 276 ASN B 281 -1 O HIS B 277 N HIS B 189
SHEET 3 BC 4 LYS B 207 VAL B 212 -1 O SER B 208 N PHE B 280
SHEET 4 BC 4 ASP B 259 GLN B 263 -1 O ASP B 259 N SER B 211
SHEET 1 CA10 MET C 16 PHE C 18 0
SHEET 2 CA10 LEU C 45 VAL C 48 1 O LEU C 45 N MET C 16
SHEET 3 CA10 PHE C 268 THR C 271 -1 O PHE C 268 N VAL C 48
SHEET 4 CA10 TYR C 196 GLY C 204 -1 O SER C 197 N THR C 271
SHEET 5 CA10 ASN C 285 PHE C 292 -1 O CYS C 286 N HIS C 202
SHEET 6 CA10 TYR C 176 GLY C 180 -1 O TYR C 176 N SER C 289
SHEET 7 CA10 ILE C 132 ASN C 138 -1 O GLY C 134 N PHE C 179
SHEET 8 CA10 ILE C 72 GLN C 79 -1 O ILE C 72 N TYR C 133
SHEET 9 CA10 LEU C 82 GLN C 89 -1 O LEU C 82 N GLN C 79
SHEET 10 CA10 THR C 244 ILE C 246 -1 O LEU C 245 N PHE C 83
SHEET 1 CB 2 VAL C 67 ILE C 68 0
SHEET 2 CB 2 MET C 93 THR C 94 -1 O MET C 93 N ILE C 68
SHEET 1 CC 4 SER C 185 HIS C 189 0
SHEET 2 CC 4 TYR C 276 ASN C 281 -1 O HIS C 277 N HIS C 189
SHEET 3 CC 4 LYS C 207 VAL C 212 -1 O SER C 208 N PHE C 280
SHEET 4 CC 4 ASP C 259 GLN C 263 -1 O ASP C 259 N SER C 211
SHEET 1 DA10 MET D 16 PHE D 18 0
SHEET 2 DA10 LEU D 45 VAL D 48 1 O LEU D 45 N MET D 16
SHEET 3 DA10 PHE D 268 THR D 271 -1 O PHE D 268 N VAL D 48
SHEET 4 DA10 TYR D 196 GLY D 204 -1 O SER D 197 N THR D 271
SHEET 5 DA10 ASN D 285 PHE D 292 -1 O CYS D 286 N HIS D 202
SHEET 6 DA10 TYR D 176 GLY D 180 -1 O TYR D 176 N SER D 289
SHEET 7 DA10 ILE D 132 ASN D 138 -1 O GLY D 134 N PHE D 179
SHEET 8 DA10 ILE D 72 GLN D 79 -1 O ILE D 72 N TYR D 133
SHEET 9 DA10 LEU D 82 GLN D 89 -1 O LEU D 82 N GLN D 79
SHEET 10 DA10 THR D 244 ILE D 246 -1 O LEU D 245 N PHE D 83
SHEET 1 DB 2 VAL D 67 ILE D 68 0
SHEET 2 DB 2 MET D 93 THR D 94 -1 O MET D 93 N ILE D 68
SHEET 1 DC 4 SER D 185 HIS D 189 0
SHEET 2 DC 4 TYR D 276 ASN D 281 -1 O HIS D 277 N HIS D 189
SHEET 3 DC 4 LYS D 207 VAL D 212 -1 O SER D 208 N PHE D 280
SHEET 4 DC 4 ASP D 259 GLN D 263 -1 O ASP D 259 N SER D 211
SHEET 1 EA10 MET E 16 PHE E 18 0
SHEET 2 EA10 LEU E 45 VAL E 48 1 O LEU E 45 N MET E 16
SHEET 3 EA10 PHE E 268 THR E 271 -1 O PHE E 268 N VAL E 48
SHEET 4 EA10 TYR E 196 GLY E 204 -1 O SER E 197 N THR E 271
SHEET 5 EA10 ASN E 285 PHE E 292 -1 O CYS E 286 N HIS E 202
SHEET 6 EA10 TYR E 176 GLY E 180 -1 O TYR E 176 N SER E 289
SHEET 7 EA10 ILE E 132 ASN E 138 -1 O GLY E 134 N PHE E 179
SHEET 8 EA10 ILE E 72 GLN E 79 -1 O ILE E 72 N TYR E 133
SHEET 9 EA10 LEU E 82 GLN E 89 -1 O LEU E 82 N GLN E 79
SHEET 10 EA10 THR E 244 ILE E 246 -1 O LEU E 245 N PHE E 83
SHEET 1 EB 2 VAL E 67 ILE E 68 0
SHEET 2 EB 2 MET E 93 THR E 94 -1 O MET E 93 N ILE E 68
SHEET 1 EC 4 SER E 185 HIS E 189 0
SHEET 2 EC 4 TYR E 276 ASN E 281 -1 O HIS E 277 N HIS E 189
SHEET 3 EC 4 LYS E 207 VAL E 212 -1 O SER E 208 N PHE E 280
SHEET 4 EC 4 ASP E 259 GLN E 263 -1 O ASP E 259 N SER E 211
SHEET 1 FA10 MET F 16 PHE F 18 0
SHEET 2 FA10 LEU F 45 VAL F 48 1 O LEU F 45 N MET F 16
SHEET 3 FA10 PHE F 268 THR F 271 -1 O PHE F 268 N VAL F 48
SHEET 4 FA10 TYR F 196 GLY F 204 -1 O SER F 197 N THR F 271
SHEET 5 FA10 ASN F 285 PHE F 292 -1 O CYS F 286 N HIS F 202
SHEET 6 FA10 TYR F 176 GLY F 180 -1 O TYR F 176 N SER F 289
SHEET 7 FA10 ILE F 132 ASN F 138 -1 O GLY F 134 N PHE F 179
SHEET 8 FA10 ILE F 72 GLN F 79 -1 O ILE F 72 N TYR F 133
SHEET 9 FA10 LEU F 82 GLN F 89 -1 O LEU F 82 N GLN F 79
SHEET 10 FA10 THR F 244 ILE F 246 -1 O LEU F 245 N PHE F 83
SHEET 1 FB 2 VAL F 67 ILE F 68 0
SHEET 2 FB 2 MET F 93 THR F 94 -1 O MET F 93 N ILE F 68
SHEET 1 FC 4 SER F 185 HIS F 189 0
SHEET 2 FC 4 TYR F 276 ASN F 281 -1 O HIS F 277 N HIS F 189
SHEET 3 FC 4 LYS F 207 VAL F 212 -1 O SER F 208 N PHE F 280
SHEET 4 FC 4 ASP F 259 GLN F 263 -1 O ASP F 259 N SER F 211
SHEET 1 GA10 MET G 16 PHE G 18 0
SHEET 2 GA10 LEU G 45 VAL G 48 1 O LEU G 45 N MET G 16
SHEET 3 GA10 PHE G 268 THR G 271 -1 O PHE G 268 N VAL G 48
SHEET 4 GA10 TYR G 196 GLY G 204 -1 O SER G 197 N THR G 271
SHEET 5 GA10 ASN G 285 PHE G 292 -1 O CYS G 286 N HIS G 202
SHEET 6 GA10 TYR G 176 GLY G 180 -1 O TYR G 176 N SER G 289
SHEET 7 GA10 ILE G 132 ASN G 138 -1 O GLY G 134 N PHE G 179
SHEET 8 GA10 ILE G 72 GLN G 79 -1 O ILE G 72 N TYR G 133
SHEET 9 GA10 LEU G 82 GLN G 89 -1 O LEU G 82 N GLN G 79
SHEET 10 GA10 THR G 244 ILE G 246 -1 O LEU G 245 N PHE G 83
SHEET 1 GB 2 VAL G 67 ILE G 68 0
SHEET 2 GB 2 MET G 93 THR G 94 -1 O MET G 93 N ILE G 68
SHEET 1 GC 4 SER G 185 HIS G 189 0
SHEET 2 GC 4 TYR G 276 ASN G 281 -1 O HIS G 277 N HIS G 189
SHEET 3 GC 4 LYS G 207 VAL G 212 -1 O SER G 208 N PHE G 280
SHEET 4 GC 4 ASP G 259 GLN G 263 -1 O ASP G 259 N SER G 211
SHEET 1 HA10 MET H 16 PHE H 18 0
SHEET 2 HA10 LEU H 45 VAL H 48 1 O LEU H 45 N MET H 16
SHEET 3 HA10 PHE H 268 THR H 271 -1 O PHE H 268 N VAL H 48
SHEET 4 HA10 TYR H 196 GLY H 204 -1 O SER H 197 N THR H 271
SHEET 5 HA10 ASN H 285 PHE H 292 -1 O CYS H 286 N HIS H 202
SHEET 6 HA10 TYR H 176 GLY H 180 -1 O TYR H 176 N SER H 289
SHEET 7 HA10 ILE H 132 ASN H 138 -1 O GLY H 134 N PHE H 179
SHEET 8 HA10 ILE H 72 GLN H 79 -1 O ILE H 72 N TYR H 133
SHEET 9 HA10 LEU H 82 GLN H 89 -1 O LEU H 82 N GLN H 79
SHEET 10 HA10 THR H 244 ILE H 246 -1 O LEU H 245 N PHE H 83
SHEET 1 HB 2 VAL H 67 ILE H 68 0
SHEET 2 HB 2 MET H 93 THR H 94 -1 O MET H 93 N ILE H 68
SHEET 1 HC 4 SER H 185 HIS H 189 0
SHEET 2 HC 4 TYR H 276 ASN H 281 -1 O HIS H 277 N HIS H 189
SHEET 3 HC 4 LYS H 207 VAL H 212 -1 O SER H 208 N PHE H 280
SHEET 4 HC 4 ASP H 259 GLN H 263 -1 O ASP H 259 N SER H 211
SSBOND 1 CYS B 307 CYS B 309 1555 1555 3.00
LINK NE2 HIS A 189 MN MN A1357 1555 1555 2.13
LINK OE2 GLU A 191 MN MN A1357 1555 1555 2.06
LINK SG CYS A 235 ZN ZN A1359 1555 1555 2.21
LINK NE2 HIS A 241 ZN ZN A1359 1555 1555 2.11
LINK NE2 HIS A 277 MN MN A1357 1555 1555 2.25
LINK SG CYS A 307 ZN ZN A1359 1555 1555 2.28
LINK SG CYS A 309 ZN ZN A1359 1555 1555 2.41
LINK MN MN A1357 N MMK A1358 1555 1555 2.29
LINK MN MN A1357 NAR MMK A1358 1555 1555 2.20
LINK MN MN A1357 O HOH A2094 1555 1555 1.99
LINK NI NI A1360 NZ LYS H 106 1555 1555 2.54
LINK NE2 HIS B 189 MN MN B1357 1555 1555 2.14
LINK OE2 GLU B 191 MN MN B1357 1555 1555 2.00
LINK SG CYS B 235 ZN ZN B1359 1555 1555 2.07
LINK NE2 HIS B 241 ZN ZN B1359 1555 1555 2.04
LINK NE2 HIS B 277 MN MN B1357 1555 1555 2.26
LINK SG CYS B 309 ZN ZN B1359 1555 1555 2.16
LINK MN MN B1357 N MMK B1358 1555 1555 2.24
LINK MN MN B1357 NAR MMK B1358 1555 1555 2.17
LINK MN MN B1357 O HOH B2095 1555 1555 2.17
LINK NE2 HIS C 189 MN MN C1357 1555 1555 2.19
LINK OE2 GLU C 191 MN MN C1357 1555 1555 2.05
LINK SG CYS C 235 ZN ZN C1359 1555 1555 2.37
LINK NE2 HIS C 241 ZN ZN C1359 1555 1555 2.03
LINK NE2 HIS C 277 MN MN C1357 1555 1555 2.27
LINK SG CYS C 307 ZN ZN C1359 1555 1555 2.24
LINK SG CYS C 309 ZN ZN C1359 1555 1555 2.39
LINK MN MN C1357 NAR MMK C1358 1555 1555 2.04
LINK MN MN C1357 N MMK C1358 1555 1555 2.32
LINK MN MN C1357 O HOH C2103 1555 1555 2.29
LINK NE2 HIS D 189 MN MN D1357 1555 1555 2.10
LINK OE2 GLU D 191 MN MN D1357 1555 1555 2.04
LINK SG CYS D 235 ZN ZN D1359 1555 1555 2.35
LINK NE2 HIS D 241 ZN ZN D1359 1555 1555 2.09
LINK NE2 HIS D 277 MN MN D1357 1555 1555 2.21
LINK SG CYS D 307 ZN ZN D1359 1555 1555 2.29
LINK SG CYS D 309 ZN ZN D1359 1555 1555 2.39
LINK MN MN D1357 N MMK D1358 1555 1555 2.36
LINK MN MN D1357 NAR MMK D1358 1555 1555 2.07
LINK MN MN D1357 O HOH D2089 1555 1555 2.18
LINK NE2 HIS E 189 MN MN E1357 1555 1555 2.23
LINK OE2 GLU E 191 MN MN E1357 1555 1555 2.03
LINK SG CYS E 235 ZN ZN E1359 1555 1555 2.28
LINK NE2 HIS E 241 ZN ZN E1359 1555 1555 2.06
LINK NE2 HIS E 277 MN MN E1357 1555 1555 2.22
LINK SG CYS E 307 ZN ZN E1359 1555 1555 2.25
LINK SG CYS E 309 ZN ZN E1359 1555 1555 2.39
LINK MN MN E1357 N MMK E1358 1555 1555 2.46
LINK MN MN E1357 NAR MMK E1358 1555 1555 2.18
LINK MN MN E1357 O HOH E2057 1555 1555 2.11
LINK NE2 HIS F 189 MN MN F1357 1555 1555 2.13
LINK OE2 GLU F 191 MN MN F1357 1555 1555 2.06
LINK SG CYS F 235 ZN ZN F1359 1555 1555 2.26
LINK NE2 HIS F 241 ZN ZN F1359 1555 1555 2.07
LINK NE2 HIS F 277 MN MN F1357 1555 1555 2.26
LINK SG CYS F 307 ZN ZN F1359 1555 1555 2.14
LINK SG CYS F 309 ZN ZN F1359 1555 1555 2.35
LINK MN MN F1357 N MMK F1358 1555 1555 2.49
LINK MN MN F1357 NAR MMK F1358 1555 1555 2.25
LINK MN MN F1357 O HOH F2049 1555 1555 2.12
LINK NE2 HIS G 189 MN MN G1357 1555 1555 2.12
LINK OE2 GLU G 191 MN MN G1357 1555 1555 2.10
LINK SG CYS G 235 ZN ZN G1359 1555 1555 2.32
LINK NE2 HIS G 241 ZN ZN G1359 1555 1555 2.11
LINK NE2 HIS G 277 MN MN G1357 1555 1555 2.25
LINK SG CYS G 307 ZN ZN G1359 1555 1555 2.21
LINK SG CYS G 309 ZN ZN G1359 1555 1555 2.31
LINK MN MN G1357 NAR MMK G1358 1555 1555 1.95
LINK MN MN G1357 N MMK G1358 1555 1555 2.34
LINK MN MN G1357 O HOH G2044 1555 1555 2.20
LINK NZ LYS H 91 NI NI H1361 1555 1555 1.67
LINK NE2 HIS H 189 MN MN H1357 1555 1555 2.09
LINK OE2 GLU H 191 MN MN H1357 1555 1555 2.09
LINK SG CYS H 235 ZN ZN H1359 1555 1555 2.36
LINK NE2 HIS H 241 ZN ZN H1359 1555 1555 2.06
LINK NE2 HIS H 277 MN MN H1357 1555 1555 2.26
LINK SG CYS H 307 ZN ZN H1359 1555 1555 2.27
LINK SG CYS H 309 ZN ZN H1359 1555 1555 2.30
LINK MN MN H1357 NAR MMK H1358 1555 1555 2.06
LINK MN MN H1357 N MMK H1358 1555 1555 2.31
LINK MN MN H1357 O HOH H2075 1555 1555 2.13
LINK NI NI H1363 O HOH H2119 1555 1555 2.46
LINK NI NI H1363 O HOH H2120 1555 1555 2.57
SITE 1 AC1 5 HIS A 189 GLU A 191 HIS A 277 MMK A1358
SITE 2 AC1 5 HOH A2094
SITE 1 AC2 16 TYR A 133 ASP A 136 TYR A 176 TYR A 178
SITE 2 AC2 16 PHE A 186 HIS A 189 GLU A 191 LYS A 207
SITE 3 AC2 16 TRP A 209 LYS A 242 HIS A 277 SER A 289
SITE 4 AC2 16 THR A 290 ASN A 291 MN A1357 HOH A2094
SITE 1 AC3 4 CYS A 235 HIS A 241 CYS A 307 CYS A 309
SITE 1 AC4 2 GLY A 230 LYS H 106
SITE 1 AC5 1 LYS A 91
SITE 1 AC6 5 HIS B 189 GLU B 191 HIS B 277 MMK B1358
SITE 2 AC6 5 HOH B2095
SITE 1 AC7 16 TYR B 133 TYR B 176 TYR B 178 PHE B 186
SITE 2 AC7 16 HIS B 189 GLU B 191 ASP B 192 LYS B 207
SITE 3 AC7 16 TRP B 209 LYS B 242 HIS B 277 SER B 289
SITE 4 AC7 16 THR B 290 ASN B 291 MN B1357 HOH B2095
SITE 1 AC8 4 CYS B 235 HIS B 241 CYS B 307 CYS B 309
SITE 1 AC9 2 GLY B 230 SER B 231
SITE 1 BC1 5 HIS C 189 GLU C 191 HIS C 277 MMK C1358
SITE 2 BC1 5 HOH C2103
SITE 1 BC2 17 TYR C 133 ASP C 136 TYR C 178 PHE C 186
SITE 2 BC2 17 HIS C 189 GLU C 191 ASP C 192 LYS C 207
SITE 3 BC2 17 TRP C 209 LYS C 242 HIS C 277 SER C 289
SITE 4 BC2 17 THR C 290 ASN C 291 MN C1357 HOH C2076
SITE 5 BC2 17 HOH C2103
SITE 1 BC3 4 CYS C 235 HIS C 241 CYS C 307 CYS C 309
SITE 1 BC4 2 ARG C 96 ASP H 147
SITE 1 BC5 5 HIS D 189 GLU D 191 HIS D 277 MMK D1358
SITE 2 BC5 5 HOH D2089
SITE 1 BC6 14 TYR D 133 TYR D 176 TYR D 178 PHE D 186
SITE 2 BC6 14 HIS D 189 GLU D 191 LYS D 207 TRP D 209
SITE 3 BC6 14 LYS D 242 HIS D 277 SER D 289 MN D1357
SITE 4 BC6 14 HOH D2068 HOH D2089
SITE 1 BC7 4 CYS D 235 HIS D 241 CYS D 307 CYS D 309
SITE 1 BC8 2 GLY D 230 LYS E 106
SITE 1 BC9 5 HIS E 189 GLU E 191 HIS E 277 MMK E1358
SITE 2 BC9 5 HOH E2057
SITE 1 CC1 15 TYR E 133 ASP E 136 TYR E 178 PHE E 186
SITE 2 CC1 15 HIS E 189 GLU E 191 LYS E 207 TRP E 209
SITE 3 CC1 15 LYS E 242 HIS E 277 THR E 290 ASN E 291
SITE 4 CC1 15 MN E1357 HOH E2047 HOH E2057
SITE 1 CC2 4 CYS E 235 HIS E 241 CYS E 307 CYS E 309
SITE 1 CC3 5 HIS F 189 GLU F 191 HIS F 277 MMK F1358
SITE 2 CC3 5 HOH F2049
SITE 1 CC4 16 TYR F 133 ASP F 136 TYR F 176 TYR F 178
SITE 2 CC4 16 PHE F 186 HIS F 189 GLU F 191 LYS F 207
SITE 3 CC4 16 TRP F 209 LYS F 242 HIS F 277 SER F 289
SITE 4 CC4 16 THR F 290 ASN F 291 MN F1357 HOH F2049
SITE 1 CC5 4 CYS F 235 HIS F 241 CYS F 307 CYS F 309
SITE 1 CC6 5 HIS G 189 GLU G 191 HIS G 277 MMK G1358
SITE 2 CC6 5 HOH G2044
SITE 1 CC7 16 TYR G 133 ASP G 136 TYR G 176 TYR G 178
SITE 2 CC7 16 PHE G 186 HIS G 189 GLU G 191 LYS G 207
SITE 3 CC7 16 TRP G 209 LYS G 242 HIS G 277 SER G 289
SITE 4 CC7 16 THR G 290 ASN G 291 MN G1357 HOH G2044
SITE 1 CC8 4 CYS G 235 HIS G 241 CYS G 307 CYS G 309
SITE 1 CC9 2 GLY G 230 SER G 231
SITE 1 DC1 5 HIS H 189 GLU H 191 HIS H 277 MMK H1358
SITE 2 DC1 5 HOH H2075
SITE 1 DC2 13 TYR H 133 TYR H 176 TYR H 178 PHE H 186
SITE 2 DC2 13 HIS H 189 GLU H 191 LYS H 207 TRP H 209
SITE 3 DC2 13 LYS H 242 HIS H 277 SER H 289 MN H1357
SITE 4 DC2 13 HOH H2075
SITE 1 DC3 4 CYS H 235 HIS H 241 CYS H 307 CYS H 309
SITE 1 DC4 2 LYS A 106 GLY H 230
SITE 1 DC5 2 LYS H 90 LYS H 91
SITE 1 DC6 2 HOH H2119 HOH H2120
CRYST1 111.346 103.509 157.103 90.00 106.37 90.00 P 1 21 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008981 0.000000 0.002638 0.00000
SCALE2 0.000000 0.009661 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006634 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
