HEADER UNKNOWN FUNCTION 26-JUL-10 3AL6
TITLE CRYSTAL STRUCTURE OF HUMAN TYW5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: JMJC DOMAIN-CONTAINING PROTEIN C2ORF60;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HTYW5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: C2ORF60;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS TRNA MODIFICATION ENZYME, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KATO,Y.ARAISO,R.ISHITANI,O.NUREKI
REVDAT 3 13-MAR-24 3AL6 1 REMARK SEQADV LINK
REVDAT 2 07-AUG-13 3AL6 1 JRNL VERSN
REVDAT 1 01-DEC-10 3AL6 0
JRNL AUTH M.KATO,Y.ARAISO,A.NOMA,A.NAGAO,T.SUZUKI,R.ISHITANI,O.NUREKI
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL JMJC-DOMAIN-CONTAINING PROTEIN,
JRNL TITL 2 TYW5, INVOLVED IN TRNA MODIFICATION.
JRNL REF NUCLEIC ACIDS RES. V. 39 1576 2011
JRNL REFN ISSN 0305-1048
JRNL PMID 20972222
JRNL DOI 10.1093/NAR/GKQ919
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6_289
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.150
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 36782
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1840
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 49.0249 - 6.5789 0.97 2817 149 0.2414 0.3006
REMARK 3 2 6.5789 - 5.2237 1.00 2766 146 0.2405 0.2991
REMARK 3 3 5.2237 - 4.5640 1.00 2716 143 0.2018 0.2541
REMARK 3 4 4.5640 - 4.1469 1.00 2702 143 0.2094 0.2551
REMARK 3 5 4.1469 - 3.8498 1.00 2686 140 0.2214 0.2966
REMARK 3 6 3.8498 - 3.6229 1.00 2688 142 0.2324 0.2845
REMARK 3 7 3.6229 - 3.4415 1.00 2677 141 0.2234 0.3002
REMARK 3 8 3.4415 - 3.2917 1.00 2667 140 0.2385 0.2806
REMARK 3 9 3.2917 - 3.1650 1.00 2656 140 0.2433 0.3337
REMARK 3 10 3.1650 - 3.0558 1.00 2678 141 0.2718 0.3001
REMARK 3 11 3.0558 - 2.9603 1.00 2641 139 0.2835 0.3523
REMARK 3 12 2.9603 - 2.8757 1.00 2649 139 0.3034 0.3760
REMARK 3 13 2.8757 - 2.8000 0.98 2599 137 0.3344 0.3704
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 69.56
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.93790
REMARK 3 B22 (A**2) : 2.93790
REMARK 3 B33 (A**2) : -5.87570
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 9267
REMARK 3 ANGLE : 1.360 12643
REMARK 3 CHIRALITY : 0.086 1408
REMARK 3 PLANARITY : 0.006 1644
REMARK 3 DIHEDRAL : 20.092 3130
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND RESID 4:311 AND (NAME C OR
REMARK 3 NAME N OR NAME O OR NAME CA)
REMARK 3 SELECTION : CHAIN C AND RESID 6:311 AND (NAME C OR
REMARK 3 NAME N OR NAME O OR NAME CA)
REMARK 3 ATOM PAIRS NUMBER : 1092
REMARK 3 RMSD : 0.673
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN D AND RESID 4:311 AND (NAME C OR
REMARK 3 NAME N OR NAME O OR NAME CA)
REMARK 3 SELECTION : CHAIN A AND RESID 5:311 AND (NAME C OR
REMARK 3 NAME N OR NAME O OR NAME CA)
REMARK 3 ATOM PAIRS NUMBER : 1196
REMARK 3 RMSD : 0.526
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3AL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000029386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.48505
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36950
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 19.00
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 56.4440
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM POTASSIUM THIOCYANATE, 10% (W/V)
REMARK 280 PEG3350, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.97550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 82.93550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 82.93550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.48775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 82.93550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 82.93550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.46325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 82.93550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.93550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.48775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 82.93550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.93550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.46325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 52.97550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 MET A -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 VAL A -7
REMARK 465 LEU A -6
REMARK 465 PHE A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 LEU A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLY A 3
REMARK 465 GLN A 4
REMARK 465 ALA A 63
REMARK 465 ALA A 64
REMARK 465 VAL A 65
REMARK 465 ALA A 66
REMARK 465 PHE A 70
REMARK 465 ILE A 71
REMARK 465 SER A 72
REMARK 465 GLU A 92
REMARK 465 LYS A 312
REMARK 465 ASN A 313
REMARK 465 SER A 314
REMARK 465 GLU A 315
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 LEU B -9
REMARK 465 GLU B -8
REMARK 465 VAL B -7
REMARK 465 LEU B -6
REMARK 465 PHE B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 LEU B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 LYS B 312
REMARK 465 ASN B 313
REMARK 465 SER B 314
REMARK 465 GLU B 315
REMARK 465 MET C -22
REMARK 465 GLY C -21
REMARK 465 SER C -20
REMARK 465 SER C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 SER C -12
REMARK 465 SER C -11
REMARK 465 GLY C -10
REMARK 465 LEU C -9
REMARK 465 GLU C -8
REMARK 465 VAL C -7
REMARK 465 LEU C -6
REMARK 465 PHE C -5
REMARK 465 GLN C -4
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 LEU C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLY C 3
REMARK 465 GLN C 4
REMARK 465 HIS C 5
REMARK 465 VAL C 52
REMARK 465 GLY C 53
REMARK 465 GLY C 54
REMARK 465 LYS C 55
REMARK 465 LYS C 56
REMARK 465 GLU C 57
REMARK 465 ALA C 66
REMARK 465 GLN C 67
REMARK 465 MET C 68
REMARK 465 ASP C 69
REMARK 465 PHE C 70
REMARK 465 ILE C 71
REMARK 465 SER C 72
REMARK 465 LYS C 73
REMARK 465 ASN C 74
REMARK 465 PHE C 75
REMARK 465 VAL C 76
REMARK 465 TYR C 77
REMARK 465 LYS C 93
REMARK 465 HIS C 94
REMARK 465 LYS C 95
REMARK 465 GLU C 96
REMARK 465 PHE C 97
REMARK 465 PHE C 98
REMARK 465 ARG C 115
REMARK 465 LYS C 116
REMARK 465 ASP C 117
REMARK 465 VAL C 118
REMARK 465 ALA C 119
REMARK 465 GLN C 156
REMARK 465 LEU C 157
REMARK 465 LEU C 198
REMARK 465 THR C 263
REMARK 465 LYS C 312
REMARK 465 ASN C 313
REMARK 465 SER C 314
REMARK 465 GLU C 315
REMARK 465 MET D -22
REMARK 465 GLY D -21
REMARK 465 SER D -20
REMARK 465 SER D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 SER D -12
REMARK 465 SER D -11
REMARK 465 GLY D -10
REMARK 465 LEU D -9
REMARK 465 GLU D -8
REMARK 465 VAL D -7
REMARK 465 LEU D -6
REMARK 465 PHE D -5
REMARK 465 GLN D -4
REMARK 465 GLY D -3
REMARK 465 PRO D -2
REMARK 465 LEU D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLY D 3
REMARK 465 LYS D 312
REMARK 465 ASN D 313
REMARK 465 SER D 314
REMARK 465 GLU D 315
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 17 CG CD OE1 OE2
REMARK 470 GLN A 51 CG CD OE1 NE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 GLU A 57 CG CD OE1 OE2
REMARK 470 VAL A 58 CG1 CG2
REMARK 470 LYS A 59 CG CD CE NZ
REMARK 470 MET A 68 CG SD CE
REMARK 470 ASP A 69 CG OD1 OD2
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 PHE A 75 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 80 CG CD1 CD2
REMARK 470 GLN A 84 CG CD OE1 NE2
REMARK 470 GLN A 87 CG CD OE1 NE2
REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 LYS A 93 CG CD CE NZ
REMARK 470 HIS A 94 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 GLU A 96 CG CD OE1 OE2
REMARK 470 PHE A 97 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 101 CG CD OE1 OE2
REMARK 470 ASP A 102 CG OD1 OD2
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 TYR A 105 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 112 CG CD OE1 OE2
REMARK 470 ASP A 113 CG OD1 OD2
REMARK 470 ARG A 115 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 ILE A 121 CG1 CG2 CD1
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 PHE A 125 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 127 CG CD1 CD2
REMARK 470 GLU A 140 CG CD OE1 OE2
REMARK 470 LYS A 174 CG CD CE NZ
REMARK 470 LEU A 188 CG CD1 CD2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 ILE A 200 CG1 CG2 CD1
REMARK 470 ASN A 202 CG OD1 ND2
REMARK 470 ASP A 204 CG OD1 OD2
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 PHE A 211 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 213 CG CD CE NZ
REMARK 470 ARG A 215 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 GLU A 241 CG CD OE1 OE2
REMARK 470 LYS A 251 CG CD CE NZ
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 LYS A 260 CG CD CE NZ
REMARK 470 LYS A 267 CG CD CE NZ
REMARK 470 ARG A 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 284 CG CD CE NZ
REMARK 470 GLU A 291 CG CD OE1 OE2
REMARK 470 GLU A 292 CG CD OE1 OE2
REMARK 470 GLN B 4 CG CD OE1 NE2
REMARK 470 ILE B 71 CG1 CG2 CD1
REMARK 470 SER B 72 OG
REMARK 470 GLU B 92 CG CD OE1 OE2
REMARK 470 LYS B 93 CG CD CE NZ
REMARK 470 LYS B 95 CG CD CE NZ
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 GLU B 112 CG CD OE1 OE2
REMARK 470 ARG B 115 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 116 CG CD CE NZ
REMARK 470 GLU B 136 CG CD OE1 OE2
REMARK 470 GLU B 140 CG CD OE1 OE2
REMARK 470 GLU B 141 CG CD OE1 OE2
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 LYS B 191 CG CD CE NZ
REMARK 470 ARG B 215 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 LYS B 260 CG CD CE NZ
REMARK 470 GLN B 277 CG CD OE1 NE2
REMARK 470 ARG B 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 284 CG CD CE NZ
REMARK 470 LEU B 303 CG CD1 CD2
REMARK 470 LYS B 308 CG CD CE NZ
REMARK 470 ARG C 16 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 GLN C 21 CG CD OE1 NE2
REMARK 470 HIS C 22 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C 26 CG CD OE1 NE2
REMARK 470 SER C 42 OG
REMARK 470 LYS C 43 CG CD CE NZ
REMARK 470 ASP C 47 CG OD1 OD2
REMARK 470 LEU C 49 CG CD1 CD2
REMARK 470 GLN C 51 CG CD OE1 NE2
REMARK 470 VAL C 58 CG1 CG2
REMARK 470 LYS C 59 CG CD CE NZ
REMARK 470 ILE C 60 CG1 CG2 CD1
REMARK 470 HIS C 61 CG ND1 CD2 CE1 NE2
REMARK 470 VAL C 62 CG1 CG2
REMARK 470 ARG C 78 CG CD NE CZ NH1 NH2
REMARK 470 THR C 79 OG1 CG2
REMARK 470 LEU C 80 CG CD1 CD2
REMARK 470 PHE C 82 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN C 84 CG CD OE1 NE2
REMARK 470 LEU C 85 CG CD1 CD2
REMARK 470 VAL C 86 CG1 CG2
REMARK 470 GLN C 87 CG CD OE1 NE2
REMARK 470 ARG C 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 92 CG CD OE1 OE2
REMARK 470 VAL C 99 CG1 CG2
REMARK 470 ASP C 102 CG OD1 OD2
REMARK 470 GLU C 103 CG CD OE1 OE2
REMARK 470 LYS C 104 CG CD CE NZ
REMARK 470 TYR C 105 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR C 106 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 107 CG CD1 CD2
REMARK 470 ARG C 108 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 110 CG CD1 CD2
REMARK 470 GLU C 112 CG CD OE1 OE2
REMARK 470 ASP C 113 CG OD1 OD2
REMARK 470 ARG C 122 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 123 CG CD CE NZ
REMARK 470 GLN C 124 CG CD OE1 NE2
REMARK 470 LYS C 129 CG CD CE NZ
REMARK 470 LYS C 133 CG CD CE NZ
REMARK 470 LYS C 139 CG CD CE NZ
REMARK 470 GLU C 141 CG CD OE1 OE2
REMARK 470 GLN C 142 CG CD OE1 NE2
REMARK 470 PHE C 144 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 155 CG CD1 CD2
REMARK 470 LEU C 167 CG CD1 CD2
REMARK 470 ILE C 169 CG1 CG2 CD1
REMARK 470 LYS C 174 CG CD CE NZ
REMARK 470 LYS C 175 CG CD CE NZ
REMARK 470 ARG C 176 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 177 CG1 CG2
REMARK 470 LEU C 190 CG CD1 CD2
REMARK 470 LYS C 191 CG CD CE NZ
REMARK 470 LYS C 194 CG CD CE NZ
REMARK 470 GLU C 196 CG CD OE1 OE2
REMARK 470 ILE C 200 CG1 CG2 CD1
REMARK 470 ASN C 202 CG OD1 ND2
REMARK 470 ASP C 204 CG OD1 OD2
REMARK 470 LYS C 207 CG CD CE NZ
REMARK 470 PHE C 211 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 213 CG CD CE NZ
REMARK 470 ARG C 215 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 216 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 218 CG CD OE1 OE2
REMARK 470 ASN C 236 CG OD1 ND2
REMARK 470 ILE C 238 CG1 CG2 CD1
REMARK 470 GLU C 240 CG CD OE1 OE2
REMARK 470 GLU C 241 CG CD OE1 OE2
REMARK 470 PHE C 242 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL C 246 CG1 CG2
REMARK 470 LYS C 251 CG CD CE NZ
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 LYS C 260 CG CD CE NZ
REMARK 470 ARG C 274 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 277 CG CD OE1 NE2
REMARK 470 ARG C 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 284 CG CD CE NZ
REMARK 470 GLU C 288 CG CD OE1 OE2
REMARK 470 GLU C 291 CG CD OE1 OE2
REMARK 470 LYS C 308 CG CD CE NZ
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 GLN D 21 CG CD OE1 NE2
REMARK 470 LYS D 28 CG CD CE NZ
REMARK 470 ILE D 71 CG1 CG2 CD1
REMARK 470 LYS D 93 CG CD CE NZ
REMARK 470 LYS D 95 CG CD CE NZ
REMARK 470 GLU D 96 CG CD OE1 OE2
REMARK 470 GLU D 101 CG CD OE1 OE2
REMARK 470 GLU D 112 CG CD OE1 OE2
REMARK 470 ARG D 115 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 116 CG CD CE NZ
REMARK 470 GLU D 136 CG CD OE1 OE2
REMARK 470 GLU D 140 CG CD OE1 OE2
REMARK 470 LYS D 174 CG CD CE NZ
REMARK 470 LYS D 191 CD CE NZ
REMARK 470 LYS D 194 CG CD CE NZ
REMARK 470 ARG D 215 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 222 CG CD OE1 OE2
REMARK 470 GLU D 241 CG CD OE1 OE2
REMARK 470 LYS D 260 CG CD CE NZ
REMARK 470 LYS D 267 CG CD CE NZ
REMARK 470 ARG D 274 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 284 CG CD CE NZ
REMARK 470 GLU D 291 CG CD OE1 OE2
REMARK 470 GLU D 292 CG CD OE1 OE2
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 OH TYR C 24 OD2 ASP C 165 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 39 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO C 9 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500 PRO D 269 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 30 129.87 -175.45
REMARK 500 ARG A 78 -157.19 -143.71
REMARK 500 LYS A 95 -71.43 -58.68
REMARK 500 VAL A 99 -39.54 -137.68
REMARK 500 ASP A 102 47.48 -94.98
REMARK 500 ASP A 120 104.08 -166.48
REMARK 500 TRP A 158 155.20 -39.54
REMARK 500 LYS A 175 118.87 -176.50
REMARK 500 ASP A 184 36.38 -86.36
REMARK 500 ASP A 201 -75.27 -63.05
REMARK 500 ASN A 202 79.59 -111.39
REMARK 500 ASP A 204 86.18 -67.01
REMARK 500 PRO A 230 157.83 -48.57
REMARK 500 LEU A 232 -14.49 90.75
REMARK 500 GLU A 241 -166.31 -115.42
REMARK 500 HIS B 22 -62.70 -101.56
REMARK 500 TRP B 44 61.18 -69.93
REMARK 500 GLN B 51 -71.93 -68.96
REMARK 500 LYS B 73 73.15 42.25
REMARK 500 LYS B 95 -71.70 -61.38
REMARK 500 VAL B 99 -45.56 -146.15
REMARK 500 SER B 109 127.27 -34.37
REMARK 500 LEU B 157 -175.45 -58.60
REMARK 500 LEU B 232 -24.42 81.55
REMARK 500 PRO B 254 122.81 -34.18
REMARK 500 LEU B 283 -9.92 -55.89
REMARK 500 TYR B 310 -178.72 -64.41
REMARK 500 PRO C 9 128.19 -34.89
REMARK 500 PHE C 19 -79.36 -43.71
REMARK 500 LEU C 30 139.12 178.24
REMARK 500 PRO C 39 -14.81 -48.81
REMARK 500 SER C 100 154.87 178.63
REMARK 500 TYR C 106 62.24 -162.79
REMARK 500 LEU C 127 -73.93 -70.78
REMARK 500 ARG C 149 83.14 -158.18
REMARK 500 SER C 151 -165.58 -129.04
REMARK 500 PRO C 153 45.32 -88.37
REMARK 500 THR C 159 87.75 -62.56
REMARK 500 HIS C 160 -158.59 -101.08
REMARK 500 LEU C 167 88.92 -60.76
REMARK 500 LYS C 191 85.11 -156.37
REMARK 500 ASN C 202 71.91 -116.07
REMARK 500 PHE C 211 29.04 -65.45
REMARK 500 CYS C 219 158.85 178.37
REMARK 500 LEU C 232 -14.11 78.85
REMARK 500 VAL C 246 -178.02 -177.65
REMARK 500 ASN C 247 151.60 167.40
REMARK 500 PRO C 269 159.40 -43.65
REMARK 500 ALA C 271 -75.09 -34.02
REMARK 500 ALA C 272 -35.22 -37.44
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 NI A 401 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 160 NE2
REMARK 620 2 ASP A 162 OD1 101.1
REMARK 620 3 HIS A 235 NE2 84.2 82.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 401 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 160 NE2
REMARK 620 2 ASP B 162 OD1 102.1
REMARK 620 3 HIS B 235 NE2 74.5 94.1
REMARK 620 4 AKG B 501 O2 154.8 98.2 89.3
REMARK 620 5 AKG B 501 O5 85.1 168.9 79.5 72.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 401 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 160 NE2
REMARK 620 2 ASP C 162 OD1 152.7
REMARK 620 3 HIS C 235 NE2 56.2 125.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D 401 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 160 NE2
REMARK 620 2 ASP D 162 OD1 110.6
REMARK 620 3 HIS D 235 NE2 81.1 83.0
REMARK 620 4 AKG D 501 O2 166.5 82.9 100.3
REMARK 620 5 AKG D 501 O5 91.0 157.6 94.9 75.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG D 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AL5 RELATED DB: PDB
DBREF 3AL6 A 1 315 UNP A2RUC4 CB060_HUMAN 1 315
DBREF 3AL6 B 1 315 UNP A2RUC4 CB060_HUMAN 1 315
DBREF 3AL6 C 1 315 UNP A2RUC4 CB060_HUMAN 1 315
DBREF 3AL6 D 1 315 UNP A2RUC4 CB060_HUMAN 1 315
SEQADV 3AL6 MET A -22 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY A -21 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER A -20 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER A -19 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A -18 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A -17 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A -16 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A -15 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A -14 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A -13 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER A -12 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER A -11 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY A -10 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU A -9 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLU A -8 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 VAL A -7 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU A -6 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PHE A -5 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLN A -4 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY A -3 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PRO A -2 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU A -1 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS A 0 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 MET B -22 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY B -21 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER B -20 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER B -19 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B -18 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B -17 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B -16 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B -15 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B -14 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B -13 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER B -12 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER B -11 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY B -10 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU B -9 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLU B -8 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 VAL B -7 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU B -6 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PHE B -5 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLN B -4 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY B -3 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PRO B -2 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU B -1 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS B 0 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 MET C -22 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY C -21 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER C -20 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER C -19 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C -18 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C -17 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C -16 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C -15 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C -14 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C -13 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER C -12 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER C -11 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY C -10 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU C -9 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLU C -8 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 VAL C -7 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU C -6 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PHE C -5 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLN C -4 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY C -3 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PRO C -2 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU C -1 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS C 0 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 MET D -22 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY D -21 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER D -20 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER D -19 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D -18 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D -17 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D -16 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D -15 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D -14 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D -13 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER D -12 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 SER D -11 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY D -10 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU D -9 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLU D -8 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 VAL D -7 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU D -6 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PHE D -5 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLN D -4 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 GLY D -3 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 PRO D -2 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 LEU D -1 UNP A2RUC4 EXPRESSION TAG
SEQADV 3AL6 HIS D 0 UNP A2RUC4 EXPRESSION TAG
SEQRES 1 A 338 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 338 LEU GLU VAL LEU PHE GLN GLY PRO LEU HIS MET ALA GLY
SEQRES 3 A 338 GLN HIS LEU PRO VAL PRO ARG LEU GLU GLY VAL SER ARG
SEQRES 4 A 338 GLU GLN PHE MET GLN HIS LEU TYR PRO GLN ARG LYS PRO
SEQRES 5 A 338 LEU VAL LEU GLU GLY ILE ASP LEU GLY PRO CYS THR SER
SEQRES 6 A 338 LYS TRP THR VAL ASP TYR LEU SER GLN VAL GLY GLY LYS
SEQRES 7 A 338 LYS GLU VAL LYS ILE HIS VAL ALA ALA VAL ALA GLN MET
SEQRES 8 A 338 ASP PHE ILE SER LYS ASN PHE VAL TYR ARG THR LEU PRO
SEQRES 9 A 338 PHE ASP GLN LEU VAL GLN ARG ALA ALA GLU GLU LYS HIS
SEQRES 10 A 338 LYS GLU PHE PHE VAL SER GLU ASP GLU LYS TYR TYR LEU
SEQRES 11 A 338 ARG SER LEU GLY GLU ASP PRO ARG LYS ASP VAL ALA ASP
SEQRES 12 A 338 ILE ARG LYS GLN PHE PRO LEU LEU LYS GLY ASP ILE LYS
SEQRES 13 A 338 PHE PRO GLU PHE PHE LYS GLU GLU GLN PHE PHE SER SER
SEQRES 14 A 338 VAL PHE ARG ILE SER SER PRO GLY LEU GLN LEU TRP THR
SEQRES 15 A 338 HIS TYR ASP VAL MET ASP ASN LEU LEU ILE GLN VAL THR
SEQRES 16 A 338 GLY LYS LYS ARG VAL VAL LEU PHE SER PRO ARG ASP ALA
SEQRES 17 A 338 GLN TYR LEU TYR LEU LYS GLY THR LYS SER GLU VAL LEU
SEQRES 18 A 338 ASN ILE ASP ASN PRO ASP LEU ALA LYS TYR PRO LEU PHE
SEQRES 19 A 338 SER LYS ALA ARG ARG TYR GLU CYS SER LEU GLU ALA GLY
SEQRES 20 A 338 ASP VAL LEU PHE ILE PRO ALA LEU TRP PHE HIS ASN VAL
SEQRES 21 A 338 ILE SER GLU GLU PHE GLY VAL GLY VAL ASN ILE PHE TRP
SEQRES 22 A 338 LYS HIS LEU PRO SER GLU CYS TYR ASP LYS THR ASP THR
SEQRES 23 A 338 TYR GLY ASN LYS ASP PRO THR ALA ALA SER ARG ALA ALA
SEQRES 24 A 338 GLN ILE LEU ASP ARG ALA LEU LYS THR LEU ALA GLU LEU
SEQRES 25 A 338 PRO GLU GLU TYR ARG ASP PHE TYR ALA ARG ARG MET VAL
SEQRES 26 A 338 LEU HIS ILE GLN ASP LYS ALA TYR SER LYS ASN SER GLU
SEQRES 1 B 338 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 338 LEU GLU VAL LEU PHE GLN GLY PRO LEU HIS MET ALA GLY
SEQRES 3 B 338 GLN HIS LEU PRO VAL PRO ARG LEU GLU GLY VAL SER ARG
SEQRES 4 B 338 GLU GLN PHE MET GLN HIS LEU TYR PRO GLN ARG LYS PRO
SEQRES 5 B 338 LEU VAL LEU GLU GLY ILE ASP LEU GLY PRO CYS THR SER
SEQRES 6 B 338 LYS TRP THR VAL ASP TYR LEU SER GLN VAL GLY GLY LYS
SEQRES 7 B 338 LYS GLU VAL LYS ILE HIS VAL ALA ALA VAL ALA GLN MET
SEQRES 8 B 338 ASP PHE ILE SER LYS ASN PHE VAL TYR ARG THR LEU PRO
SEQRES 9 B 338 PHE ASP GLN LEU VAL GLN ARG ALA ALA GLU GLU LYS HIS
SEQRES 10 B 338 LYS GLU PHE PHE VAL SER GLU ASP GLU LYS TYR TYR LEU
SEQRES 11 B 338 ARG SER LEU GLY GLU ASP PRO ARG LYS ASP VAL ALA ASP
SEQRES 12 B 338 ILE ARG LYS GLN PHE PRO LEU LEU LYS GLY ASP ILE LYS
SEQRES 13 B 338 PHE PRO GLU PHE PHE LYS GLU GLU GLN PHE PHE SER SER
SEQRES 14 B 338 VAL PHE ARG ILE SER SER PRO GLY LEU GLN LEU TRP THR
SEQRES 15 B 338 HIS TYR ASP VAL MET ASP ASN LEU LEU ILE GLN VAL THR
SEQRES 16 B 338 GLY LYS LYS ARG VAL VAL LEU PHE SER PRO ARG ASP ALA
SEQRES 17 B 338 GLN TYR LEU TYR LEU LYS GLY THR LYS SER GLU VAL LEU
SEQRES 18 B 338 ASN ILE ASP ASN PRO ASP LEU ALA LYS TYR PRO LEU PHE
SEQRES 19 B 338 SER LYS ALA ARG ARG TYR GLU CYS SER LEU GLU ALA GLY
SEQRES 20 B 338 ASP VAL LEU PHE ILE PRO ALA LEU TRP PHE HIS ASN VAL
SEQRES 21 B 338 ILE SER GLU GLU PHE GLY VAL GLY VAL ASN ILE PHE TRP
SEQRES 22 B 338 LYS HIS LEU PRO SER GLU CYS TYR ASP LYS THR ASP THR
SEQRES 23 B 338 TYR GLY ASN LYS ASP PRO THR ALA ALA SER ARG ALA ALA
SEQRES 24 B 338 GLN ILE LEU ASP ARG ALA LEU LYS THR LEU ALA GLU LEU
SEQRES 25 B 338 PRO GLU GLU TYR ARG ASP PHE TYR ALA ARG ARG MET VAL
SEQRES 26 B 338 LEU HIS ILE GLN ASP LYS ALA TYR SER LYS ASN SER GLU
SEQRES 1 C 338 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 338 LEU GLU VAL LEU PHE GLN GLY PRO LEU HIS MET ALA GLY
SEQRES 3 C 338 GLN HIS LEU PRO VAL PRO ARG LEU GLU GLY VAL SER ARG
SEQRES 4 C 338 GLU GLN PHE MET GLN HIS LEU TYR PRO GLN ARG LYS PRO
SEQRES 5 C 338 LEU VAL LEU GLU GLY ILE ASP LEU GLY PRO CYS THR SER
SEQRES 6 C 338 LYS TRP THR VAL ASP TYR LEU SER GLN VAL GLY GLY LYS
SEQRES 7 C 338 LYS GLU VAL LYS ILE HIS VAL ALA ALA VAL ALA GLN MET
SEQRES 8 C 338 ASP PHE ILE SER LYS ASN PHE VAL TYR ARG THR LEU PRO
SEQRES 9 C 338 PHE ASP GLN LEU VAL GLN ARG ALA ALA GLU GLU LYS HIS
SEQRES 10 C 338 LYS GLU PHE PHE VAL SER GLU ASP GLU LYS TYR TYR LEU
SEQRES 11 C 338 ARG SER LEU GLY GLU ASP PRO ARG LYS ASP VAL ALA ASP
SEQRES 12 C 338 ILE ARG LYS GLN PHE PRO LEU LEU LYS GLY ASP ILE LYS
SEQRES 13 C 338 PHE PRO GLU PHE PHE LYS GLU GLU GLN PHE PHE SER SER
SEQRES 14 C 338 VAL PHE ARG ILE SER SER PRO GLY LEU GLN LEU TRP THR
SEQRES 15 C 338 HIS TYR ASP VAL MET ASP ASN LEU LEU ILE GLN VAL THR
SEQRES 16 C 338 GLY LYS LYS ARG VAL VAL LEU PHE SER PRO ARG ASP ALA
SEQRES 17 C 338 GLN TYR LEU TYR LEU LYS GLY THR LYS SER GLU VAL LEU
SEQRES 18 C 338 ASN ILE ASP ASN PRO ASP LEU ALA LYS TYR PRO LEU PHE
SEQRES 19 C 338 SER LYS ALA ARG ARG TYR GLU CYS SER LEU GLU ALA GLY
SEQRES 20 C 338 ASP VAL LEU PHE ILE PRO ALA LEU TRP PHE HIS ASN VAL
SEQRES 21 C 338 ILE SER GLU GLU PHE GLY VAL GLY VAL ASN ILE PHE TRP
SEQRES 22 C 338 LYS HIS LEU PRO SER GLU CYS TYR ASP LYS THR ASP THR
SEQRES 23 C 338 TYR GLY ASN LYS ASP PRO THR ALA ALA SER ARG ALA ALA
SEQRES 24 C 338 GLN ILE LEU ASP ARG ALA LEU LYS THR LEU ALA GLU LEU
SEQRES 25 C 338 PRO GLU GLU TYR ARG ASP PHE TYR ALA ARG ARG MET VAL
SEQRES 26 C 338 LEU HIS ILE GLN ASP LYS ALA TYR SER LYS ASN SER GLU
SEQRES 1 D 338 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 338 LEU GLU VAL LEU PHE GLN GLY PRO LEU HIS MET ALA GLY
SEQRES 3 D 338 GLN HIS LEU PRO VAL PRO ARG LEU GLU GLY VAL SER ARG
SEQRES 4 D 338 GLU GLN PHE MET GLN HIS LEU TYR PRO GLN ARG LYS PRO
SEQRES 5 D 338 LEU VAL LEU GLU GLY ILE ASP LEU GLY PRO CYS THR SER
SEQRES 6 D 338 LYS TRP THR VAL ASP TYR LEU SER GLN VAL GLY GLY LYS
SEQRES 7 D 338 LYS GLU VAL LYS ILE HIS VAL ALA ALA VAL ALA GLN MET
SEQRES 8 D 338 ASP PHE ILE SER LYS ASN PHE VAL TYR ARG THR LEU PRO
SEQRES 9 D 338 PHE ASP GLN LEU VAL GLN ARG ALA ALA GLU GLU LYS HIS
SEQRES 10 D 338 LYS GLU PHE PHE VAL SER GLU ASP GLU LYS TYR TYR LEU
SEQRES 11 D 338 ARG SER LEU GLY GLU ASP PRO ARG LYS ASP VAL ALA ASP
SEQRES 12 D 338 ILE ARG LYS GLN PHE PRO LEU LEU LYS GLY ASP ILE LYS
SEQRES 13 D 338 PHE PRO GLU PHE PHE LYS GLU GLU GLN PHE PHE SER SER
SEQRES 14 D 338 VAL PHE ARG ILE SER SER PRO GLY LEU GLN LEU TRP THR
SEQRES 15 D 338 HIS TYR ASP VAL MET ASP ASN LEU LEU ILE GLN VAL THR
SEQRES 16 D 338 GLY LYS LYS ARG VAL VAL LEU PHE SER PRO ARG ASP ALA
SEQRES 17 D 338 GLN TYR LEU TYR LEU LYS GLY THR LYS SER GLU VAL LEU
SEQRES 18 D 338 ASN ILE ASP ASN PRO ASP LEU ALA LYS TYR PRO LEU PHE
SEQRES 19 D 338 SER LYS ALA ARG ARG TYR GLU CYS SER LEU GLU ALA GLY
SEQRES 20 D 338 ASP VAL LEU PHE ILE PRO ALA LEU TRP PHE HIS ASN VAL
SEQRES 21 D 338 ILE SER GLU GLU PHE GLY VAL GLY VAL ASN ILE PHE TRP
SEQRES 22 D 338 LYS HIS LEU PRO SER GLU CYS TYR ASP LYS THR ASP THR
SEQRES 23 D 338 TYR GLY ASN LYS ASP PRO THR ALA ALA SER ARG ALA ALA
SEQRES 24 D 338 GLN ILE LEU ASP ARG ALA LEU LYS THR LEU ALA GLU LEU
SEQRES 25 D 338 PRO GLU GLU TYR ARG ASP PHE TYR ALA ARG ARG MET VAL
SEQRES 26 D 338 LEU HIS ILE GLN ASP LYS ALA TYR SER LYS ASN SER GLU
HET NI A 401 1
HET NI B 401 1
HET AKG B 501 10
HET NI C 401 1
HET NI D 401 1
HET AKG D 501 10
HETNAM NI NICKEL (II) ION
HETNAM AKG 2-OXOGLUTARIC ACID
FORMUL 5 NI 4(NI 2+)
FORMUL 7 AKG 2(C5 H6 O5)
HELIX 1 1 SER A 15 LEU A 23 1 9
HELIX 2 2 TYR A 24 ARG A 27 5 4
HELIX 3 3 PRO A 39 TRP A 44 1 6
HELIX 4 4 THR A 45 GLY A 54 1 10
HELIX 5 5 PHE A 82 GLU A 91 1 10
HELIX 6 6 ASP A 120 PHE A 125 1 6
HELIX 7 7 PHE A 125 GLY A 130 1 6
HELIX 8 8 PRO A 182 LEU A 188 5 7
HELIX 9 9 TYR A 208 ALA A 214 5 7
HELIX 10 10 PRO A 254 TYR A 258 5 5
HELIX 11 11 PRO A 269 ALA A 287 1 19
HELIX 12 12 PRO A 290 TYR A 310 1 21
HELIX 13 13 SER B 15 HIS B 22 1 8
HELIX 14 14 LEU B 23 ARG B 27 5 5
HELIX 15 15 PRO B 39 TRP B 44 1 6
HELIX 16 16 THR B 45 GLY B 54 1 10
HELIX 17 17 PHE B 82 ALA B 90 1 9
HELIX 18 18 ASP B 120 PHE B 125 1 6
HELIX 19 19 PHE B 125 GLY B 130 1 6
HELIX 20 20 LYS B 139 GLU B 141 5 3
HELIX 21 21 PRO B 182 LEU B 188 5 7
HELIX 22 22 PRO B 209 ALA B 214 5 6
HELIX 23 23 PRO B 254 TYR B 258 5 5
HELIX 24 24 PRO B 269 LEU B 286 1 18
HELIX 25 25 ALA B 287 LEU B 289 5 3
HELIX 26 26 PRO B 290 ALA B 309 1 20
HELIX 27 27 SER C 15 LEU C 23 1 9
HELIX 28 28 PRO C 39 TRP C 44 1 6
HELIX 29 29 THR C 45 GLN C 51 1 7
HELIX 30 30 PRO C 81 GLU C 92 1 12
HELIX 31 31 ASP C 120 PHE C 125 1 6
HELIX 32 32 LYS C 139 GLU C 141 5 3
HELIX 33 33 PRO C 182 LEU C 188 5 7
HELIX 34 34 PRO C 254 TYR C 258 5 5
HELIX 35 35 PRO C 269 LEU C 286 1 18
HELIX 36 36 ALA C 287 LEU C 289 5 3
HELIX 37 37 PRO C 290 ALA C 309 1 20
HELIX 38 38 SER D 15 HIS D 22 1 8
HELIX 39 39 LEU D 23 ARG D 27 5 5
HELIX 40 40 PRO D 39 TRP D 44 1 6
HELIX 41 41 THR D 45 GLY D 54 1 10
HELIX 42 42 PHE D 82 GLU D 91 1 10
HELIX 43 43 ASP D 120 PHE D 125 1 6
HELIX 44 44 PHE D 125 GLY D 130 1 6
HELIX 45 45 LYS D 139 GLU D 141 5 3
HELIX 46 46 SER D 181 LEU D 188 5 8
HELIX 47 47 PRO D 209 ALA D 214 5 6
HELIX 48 48 PRO D 254 TYR D 258 5 5
HELIX 49 49 PRO D 269 GLU D 288 1 20
HELIX 50 50 PRO D 290 ALA D 309 1 20
SHEET 1 A 5 LEU A 6 PRO A 7 0
SHEET 2 A 5 ARG A 216 SER A 220 1 O GLU A 218 N LEU A 6
SHEET 3 A 5 ARG A 176 PHE A 180 -1 N LEU A 179 O TYR A 217
SHEET 4 A 5 PHE A 234 ILE A 238 -1 O ASN A 236 N VAL A 178
SHEET 5 A 5 GLN A 156 HIS A 160 -1 N HIS A 160 O HIS A 235
SHEET 1 B 9 ARG A 10 GLU A 12 0
SHEET 2 B 9 LEU A 30 GLU A 33 1 O GLU A 33 N LEU A 11
SHEET 3 B 9 VAL A 226 ILE A 229 -1 O VAL A 226 N LEU A 32
SHEET 4 B 9 ASP A 165 GLN A 170 -1 N LEU A 168 O LEU A 227
SHEET 5 B 9 GLY A 243 TRP A 250 -1 O VAL A 246 N ILE A 169
SHEET 6 B 9 PHE A 143 SER A 151 -1 N VAL A 147 O ASN A 247
SHEET 7 B 9 TYR A 106 ARG A 108 -1 N LEU A 107 O ILE A 150
SHEET 8 B 9 GLU A 57 VAL A 62 -1 N HIS A 61 O TYR A 106
SHEET 9 B 9 VAL A 76 PRO A 81 -1 O LEU A 80 N VAL A 58
SHEET 1 C 2 LEU A 190 LYS A 191 0
SHEET 2 C 2 LYS A 194 SER A 195 -1 O LYS A 194 N LYS A 191
SHEET 1 D 6 HIS B 5 PRO B 7 0
SHEET 2 D 6 ARG B 216 LEU B 221 1 O ARG B 216 N LEU B 6
SHEET 3 D 6 ASP B 165 PHE B 180 -1 N LYS B 175 O LEU B 221
SHEET 4 D 6 VAL B 226 ILE B 229 -1 O ILE B 229 N ASN B 166
SHEET 5 D 6 LEU B 30 GLU B 33 -1 N LEU B 30 O PHE B 228
SHEET 6 D 6 ARG B 10 GLU B 12 1 N LEU B 11 O VAL B 31
SHEET 1 E 8 HIS B 5 PRO B 7 0
SHEET 2 E 8 ARG B 216 LEU B 221 1 O ARG B 216 N LEU B 6
SHEET 3 E 8 ASP B 165 PHE B 180 -1 N LYS B 175 O LEU B 221
SHEET 4 E 8 PHE B 234 TRP B 250 -1 O VAL B 246 N ILE B 169
SHEET 5 E 8 PHE B 143 SER B 151 -1 N ARG B 149 O GLY B 245
SHEET 6 E 8 LYS B 104 ARG B 108 -1 N LEU B 107 O ILE B 150
SHEET 7 E 8 GLU B 57 ALA B 63 -1 N ALA B 63 O LYS B 104
SHEET 8 E 8 PHE B 75 PRO B 81 -1 O LEU B 80 N VAL B 58
SHEET 1 F 2 LEU B 190 LYS B 191 0
SHEET 2 F 2 LYS B 194 SER B 195 -1 O LYS B 194 N LYS B 191
SHEET 1 G 4 ARG C 10 GLU C 12 0
SHEET 2 G 4 LEU C 30 GLU C 33 1 O VAL C 31 N LEU C 11
SHEET 3 G 4 VAL C 226 ILE C 229 -1 O VAL C 226 N LEU C 32
SHEET 4 G 4 ASN C 166 ILE C 169 -1 N LEU C 168 O LEU C 227
SHEET 1 H 3 LEU C 107 ARG C 108 0
SHEET 2 H 3 ARG C 149 ILE C 150 -1 O ILE C 150 N LEU C 107
SHEET 3 H 3 VAL C 244 GLY C 245 -1 O GLY C 245 N ARG C 149
SHEET 1 I 2 PHE C 143 SER C 146 0
SHEET 2 I 2 ILE C 248 TRP C 250 -1 O PHE C 249 N SER C 145
SHEET 1 J 3 ARG C 216 TYR C 217 0
SHEET 2 J 3 LYS C 175 PHE C 180 -1 N LEU C 179 O TYR C 217
SHEET 3 J 3 SER C 220 LEU C 221 -1 O LEU C 221 N LYS C 175
SHEET 1 K 3 ARG C 216 TYR C 217 0
SHEET 2 K 3 LYS C 175 PHE C 180 -1 N LEU C 179 O TYR C 217
SHEET 3 K 3 PHE C 234 VAL C 237 -1 O ASN C 236 N VAL C 178
SHEET 1 L 2 LEU C 190 LYS C 191 0
SHEET 2 L 2 LYS C 194 SER C 195 -1 O LYS C 194 N LYS C 191
SHEET 1 M 5 HIS D 5 PRO D 7 0
SHEET 2 M 5 ARG D 216 LEU D 221 1 O GLU D 218 N LEU D 6
SHEET 3 M 5 LYS D 175 PHE D 180 -1 N LYS D 175 O LEU D 221
SHEET 4 M 5 PHE D 234 SER D 239 -1 O PHE D 234 N PHE D 180
SHEET 5 M 5 GLN D 156 HIS D 160 -1 N HIS D 160 O HIS D 235
SHEET 1 N 9 ARG D 10 GLU D 12 0
SHEET 2 N 9 LEU D 30 GLU D 33 1 O GLU D 33 N LEU D 11
SHEET 3 N 9 VAL D 226 ILE D 229 -1 O VAL D 226 N LEU D 32
SHEET 4 N 9 ASP D 165 GLN D 170 -1 N ASN D 166 O ILE D 229
SHEET 5 N 9 GLY D 243 TRP D 250 -1 O TRP D 250 N ASP D 165
SHEET 6 N 9 PHE D 143 SER D 151 -1 N SER D 145 O PHE D 249
SHEET 7 N 9 LYS D 104 ARG D 108 -1 N LEU D 107 O ILE D 150
SHEET 8 N 9 GLU D 57 ALA D 63 -1 N ALA D 63 O LYS D 104
SHEET 9 N 9 PHE D 75 PRO D 81 -1 O VAL D 76 N VAL D 62
SHEET 1 O 2 LEU D 190 LYS D 191 0
SHEET 2 O 2 LYS D 194 SER D 195 -1 O LYS D 194 N LYS D 191
LINK NE2 HIS A 160 NI NI A 401 1555 1555 2.54
LINK OD1 ASP A 162 NI NI A 401 1555 1555 2.50
LINK NE2 HIS A 235 NI NI A 401 1555 1555 2.44
LINK NE2 HIS B 160 NI NI B 401 1555 1555 2.02
LINK OD1 ASP B 162 NI NI B 401 1555 1555 2.19
LINK NE2 HIS B 235 NI NI B 401 1555 1555 2.59
LINK NI NI B 401 O2 AKG B 501 1555 1555 2.00
LINK NI NI B 401 O5 AKG B 501 1555 1555 2.56
LINK NE2 HIS C 160 NI NI C 401 1555 1555 2.57
LINK OD1 ASP C 162 NI NI C 401 1555 1555 2.51
LINK NE2 HIS C 235 NI NI C 401 1555 1555 2.69
LINK NE2 HIS D 160 NI NI D 401 1555 1555 2.11
LINK OD1 ASP D 162 NI NI D 401 1555 1555 2.39
LINK NE2 HIS D 235 NI NI D 401 1555 1555 2.24
LINK NI NI D 401 O2 AKG D 501 1555 1555 2.25
LINK NI NI D 401 O5 AKG D 501 1555 1555 2.48
SITE 1 AC1 3 HIS A 160 ASP A 162 HIS A 235
SITE 1 AC2 4 HIS B 160 ASP B 162 HIS B 235 AKG B 501
SITE 1 AC3 11 TYR B 106 ARG B 149 LEU B 157 HIS B 160
SITE 2 AC3 11 ASP B 162 ASN B 166 LYS B 175 HIS B 235
SITE 3 AC3 11 VAL B 237 ASN B 247 NI B 401
SITE 1 AC4 3 HIS C 160 ASP C 162 HIS C 235
SITE 1 AC5 4 HIS D 160 ASP D 162 HIS D 235 AKG D 501
SITE 1 AC6 13 TYR D 106 ARG D 149 LEU D 157 HIS D 160
SITE 2 AC6 13 ASP D 162 ASN D 166 LEU D 168 LYS D 175
SITE 3 AC6 13 HIS D 235 VAL D 237 ASN D 247 PHE D 249
SITE 4 AC6 13 NI D 401
CRYST1 165.871 165.871 105.951 90.00 90.00 90.00 P 41 21 2 32
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 0.006029 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009438 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
