HEADER TRANSFERASE 01-AUG-19 6KMS
TITLE CRYSTAL STRUCTURE OF HUMAN N6AMT1-TRM112 IN COMPLEX WITH SAM (SPACE
TITLE 2 GROUP I422)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLTRANSFERASE N6AMT1;
COMPND 3 CHAIN: C, D;
COMPND 4 SYNONYM: HEMK METHYLTRANSFERASE FAMILY MEMBER 2,M.HSAHEMK2P,
COMPND 5 METHYLARSONITE METHYLTRANSFERASE N6AMT1,N(6)-ADENINE-SPECIFIC DNA
COMPND 6 METHYLTRANSFERASE 1,PROTEIN N(5)-GLUTAMINE METHYLTRANSFERASE;
COMPND 7 EC: 2.1.1.-,2.1.1.72;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MULTIFUNCTIONAL METHYLTRANSFERASE SUBUNIT TRM112-LIKE
COMPND 11 PROTEIN;
COMPND 12 CHAIN: A, B;
COMPND 13 SYNONYM: TRNA METHYLTRANSFERASE 112 HOMOLOG;
COMPND 14 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: N6AMT1, C21ORF127, HEMK2, PRED28;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TRMT112, AD-001, HSPC152, HSPC170;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS METHYLTRANSFERASE, COMPLEX, PROTEIN TRANSLATION, POLYPEPTIDE RELEASE
KEYWDS 2 FACTOR ERF1, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.J.LI,Y.SHI,T.L.ZHANG,J.YE,J.P.DING
REVDAT 2 06-NOV-19 6KMS 1 JRNL
REVDAT 1 18-SEP-19 6KMS 0
JRNL AUTH W.LI,Y.SHI,T.ZHANG,J.YE,J.DING
JRNL TITL STRUCTURAL INSIGHT INTO HUMAN N6AMT1-TRM112 COMPLEX
JRNL TITL 2 FUNCTIONING AS A PROTEIN METHYLTRANSFERASE.
JRNL REF CELL DISCOV V. 5 51 2019
JRNL REFN ESSN 2056-5968
JRNL PMID 31636962
JRNL DOI 10.1038/S41421-019-0121-Y
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 39482
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1978
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 39.3860 - 7.6947 1.00 2864 143 0.1653 0.2019
REMARK 3 2 7.6947 - 6.1149 1.00 2742 141 0.2123 0.2490
REMARK 3 3 6.1149 - 5.3441 1.00 2713 138 0.2245 0.2948
REMARK 3 4 5.3441 - 4.8564 1.00 2704 130 0.2120 0.2509
REMARK 3 5 4.8564 - 4.5089 1.00 2673 151 0.2076 0.2260
REMARK 3 6 4.5089 - 4.2434 1.00 2648 143 0.2170 0.2229
REMARK 3 7 4.2434 - 4.0311 1.00 2683 128 0.2430 0.3205
REMARK 3 8 4.0311 - 3.8558 1.00 2640 145 0.2646 0.2902
REMARK 3 9 3.8558 - 3.7074 1.00 2660 146 0.2669 0.2602
REMARK 3 10 3.7074 - 3.5796 1.00 2642 133 0.2836 0.3451
REMARK 3 11 3.5796 - 3.4677 1.00 2614 163 0.2954 0.3416
REMARK 3 12 3.4677 - 3.3687 1.00 2622 156 0.3072 0.3621
REMARK 3 13 3.3687 - 3.2800 1.00 2647 142 0.3477 0.3854
REMARK 3 14 3.2800 - 3.2000 1.00 2652 119 0.3611 0.3588
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 83.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.66
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 : 0.012 5209
REMARK 3 ANGLE : 1.374 7094
REMARK 3 CHIRALITY : 0.072 827
REMARK 3 PLANARITY : 0.009 922
REMARK 3 DIHEDRAL : 21.871 3114
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 A AND (RESID 0 THROUGH 43 OR
REMARK 3 (RESID 44 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 45
REMARK 3 THROUGH 67 OR (RESID 68 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 69 THROUGH 75 OR (RESID 76 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 77 THROUGH 88 OR
REMARK 3 (RESID 89 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 90
REMARK 3 THROUGH 120))
REMARK 3 SELECTION : (CHAIN B AND RESID 0 THROUGH 120)
REMARK 3 ATOM PAIRS NUMBER : 953
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN C AND (RESID 6 THROUGH 15 OR
REMARK 3 (RESID 16 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 17
REMARK 3 THROUGH 114 OR (RESID 115 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 116 THROUGH 145 OR (RESID 146
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 147 THROUGH 167
REMARK 3 OR (RESID 168 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 169 THROUGH 174 OR (RESID 175 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 176 THROUGH 183 OR (RESID 184
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 185 THROUGH 186
REMARK 3 OR (RESID 187 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 188 THROUGH 190 OR (RESID 191 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 192 THROUGH 198 OR (RESID 199
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 200 THROUGH 202
REMARK 3 OR (RESID 203 THROUGH 204 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 205 THROUGH 212 OR (RESID 213
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 214))
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 1670
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6KMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1300013184.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39672
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 28.80
REMARK 200 R MERGE (I) : 0.23400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 28.10
REMARK 200 R MERGE FOR SHELL (I) : 2.20300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 83.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH4)2SO4, 0.1M MES, PH 6.5, 10%
REMARK 280 1,4-DIOXANE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 97.67700
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 123.27550
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 97.67700
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 123.27550
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 97.67700
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 123.27550
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 97.67700
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 123.27550
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 97.67700
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 123.27550
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 97.67700
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 123.27550
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 97.67700
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 123.27550
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 97.67700
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 97.67700
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 123.27550
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: 2450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MSE C -13
REMARK 465 GLY C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 SER C -3
REMARK 465 GLN C -2
REMARK 465 ASP C -1
REMARK 465 PRO C 0
REMARK 465 MSE C 1
REMARK 465 ALA C 2
REMARK 465 GLY C 3
REMARK 465 GLU C 4
REMARK 465 GLU A 121
REMARK 465 GLU A 122
REMARK 465 THR A 123
REMARK 465 GLU A 124
REMARK 465 SER A 125
REMARK 465 SER B 125
REMARK 465 MSE D -13
REMARK 465 GLY D -12
REMARK 465 SER D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 SER D -3
REMARK 465 GLN D -2
REMARK 465 ASP D -1
REMARK 465 PRO D 0
REMARK 465 MSE D 1
REMARK 465 ALA D 2
REMARK 465 GLY D 3
REMARK 465 GLU D 4
REMARK 465 ASN D 5
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 ARG C 166 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 44 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 68 CG CD CE NZ
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 LEU B 89 CG CD1 CD2
REMARK 470 ARG D 16 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 115 CG CD CE NZ
REMARK 470 ARG D 146 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 166 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 168 CG CD1 CD2
REMARK 470 LYS D 175 CG CD CE NZ
REMARK 470 LYS D 184 CG CD CE NZ
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 LEU D 191 CG CD1 CD2
REMARK 470 ARG D 199 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 203 CG CD OE1 NE2
REMARK 470 GLU D 204 CG CD OE1 OE2
REMARK 470 LYS D 213 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE C 6 -70.11 -128.92
REMARK 500 HIS C 11 46.74 -145.92
REMARK 500 PRO C 69 7.40 -67.93
REMARK 500 LEU C 104 -96.70 59.14
REMARK 500 GLU C 114 27.88 49.80
REMARK 500 ASN C 178 68.14 72.04
REMARK 500 SER C 198 155.79 178.58
REMARK 500 ALA C 201 138.01 -172.58
REMARK 500 GLN A 65 79.15 -112.81
REMARK 500 HIS D 11 46.16 -146.25
REMARK 500 ASP D 21 30.85 -93.88
REMARK 500 PRO D 69 14.38 -66.79
REMARK 500 CYS D 75 144.41 177.33
REMARK 500 LEU D 104 -98.70 61.82
REMARK 500 SER D 135 165.25 -49.32
REMARK 500 ARG D 166 30.42 -83.64
REMARK 500 ASN D 178 63.26 71.38
REMARK 500 SER D 198 165.62 174.75
REMARK 500 ALA D 201 145.05 -174.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM D 301
DBREF 6KMS C 1 214 UNP Q9Y5N5 N6MT1_HUMAN 1 214
DBREF 6KMS A 1 125 UNP Q9UI30 TR112_HUMAN 1 125
DBREF 6KMS B 1 125 UNP Q9UI30 TR112_HUMAN 1 125
DBREF 6KMS D 1 214 UNP Q9Y5N5 N6MT1_HUMAN 1 214
SEQADV 6KMS MSE C -13 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS GLY C -12 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS SER C -11 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS SER C -10 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS C -9 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS C -8 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS C -7 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS C -6 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS C -5 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS C -4 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS SER C -3 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS GLN C -2 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS ASP C -1 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS PRO C 0 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS MSE A 0 UNP Q9UI30 INITIATING METHIONINE
SEQADV 6KMS MSE B 0 UNP Q9UI30 INITIATING METHIONINE
SEQADV 6KMS MSE D -13 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS GLY D -12 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS SER D -11 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS SER D -10 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS D -9 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS D -8 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS D -7 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS D -6 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS D -5 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS HIS D -4 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS SER D -3 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS GLN D -2 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS ASP D -1 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6KMS PRO D 0 UNP Q9Y5N5 EXPRESSION TAG
SEQRES 1 C 228 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 C 228 PRO MSE ALA GLY GLU ASN PHE ALA THR PRO PHE HIS GLY
SEQRES 3 C 228 HIS VAL GLY ARG GLY ALA PHE SER ASP VAL TYR GLU PRO
SEQRES 4 C 228 ALA GLU ASP THR PHE LEU LEU LEU ASP ALA LEU GLU ALA
SEQRES 5 C 228 ALA ALA ALA GLU LEU ALA GLY VAL GLU ILE CYS LEU GLU
SEQRES 6 C 228 VAL GLY SER GLY SER GLY VAL VAL SER ALA PHE LEU ALA
SEQRES 7 C 228 SER MSE ILE GLY PRO GLN ALA LEU TYR MSE CYS THR ASP
SEQRES 8 C 228 ILE ASN PRO GLU ALA ALA ALA CYS THR LEU GLU THR ALA
SEQRES 9 C 228 ARG CYS ASN LYS VAL HIS ILE GLN PRO VAL ILE THR ASP
SEQRES 10 C 228 LEU VAL LYS GLY LEU LEU PRO ARG LEU THR GLU LYS VAL
SEQRES 11 C 228 ASP LEU LEU VAL PHE ASN PRO PRO TYR VAL VAL THR PRO
SEQRES 12 C 228 PRO GLN GLU VAL GLY SER HIS GLY ILE GLU ALA ALA TRP
SEQRES 13 C 228 ALA GLY GLY ARG ASN GLY ARG GLU VAL MSE ASP ARG PHE
SEQRES 14 C 228 PHE PRO LEU VAL PRO ASP LEU LEU SER PRO ARG GLY LEU
SEQRES 15 C 228 PHE TYR LEU VAL THR ILE LYS GLU ASN ASN PRO GLU GLU
SEQRES 16 C 228 ILE LEU LYS ILE MSE LYS THR LYS GLY LEU GLN GLY THR
SEQRES 17 C 228 THR ALA LEU SER ARG GLN ALA GLY GLN GLU THR LEU SER
SEQRES 18 C 228 VAL LEU LYS PHE THR LYS SER
SEQRES 1 A 126 MSE MSE LYS LEU LEU THR HIS ASN LEU LEU SER SER HIS
SEQRES 2 A 126 VAL ARG GLY VAL GLY SER ARG GLY PHE PRO LEU ARG LEU
SEQRES 3 A 126 GLN ALA THR GLU VAL ARG ILE CYS PRO VAL GLU PHE ASN
SEQRES 4 A 126 PRO ASN PHE VAL ALA ARG MSE ILE PRO LYS VAL GLU TRP
SEQRES 5 A 126 SER ALA PHE LEU GLU ALA ALA ASP ASN LEU ARG LEU ILE
SEQRES 6 A 126 GLN VAL PRO LYS GLY PRO VAL GLU GLY TYR GLU GLU ASN
SEQRES 7 A 126 GLU GLU PHE LEU ARG THR MSE HIS HIS LEU LEU LEU GLU
SEQRES 8 A 126 VAL GLU VAL ILE GLU GLY THR LEU GLN CYS PRO GLU SER
SEQRES 9 A 126 GLY ARG MSE PHE PRO ILE SER ARG GLY ILE PRO ASN MSE
SEQRES 10 A 126 LEU LEU SER GLU GLU GLU THR GLU SER
SEQRES 1 B 126 MSE MSE LYS LEU LEU THR HIS ASN LEU LEU SER SER HIS
SEQRES 2 B 126 VAL ARG GLY VAL GLY SER ARG GLY PHE PRO LEU ARG LEU
SEQRES 3 B 126 GLN ALA THR GLU VAL ARG ILE CYS PRO VAL GLU PHE ASN
SEQRES 4 B 126 PRO ASN PHE VAL ALA ARG MSE ILE PRO LYS VAL GLU TRP
SEQRES 5 B 126 SER ALA PHE LEU GLU ALA ALA ASP ASN LEU ARG LEU ILE
SEQRES 6 B 126 GLN VAL PRO LYS GLY PRO VAL GLU GLY TYR GLU GLU ASN
SEQRES 7 B 126 GLU GLU PHE LEU ARG THR MSE HIS HIS LEU LEU LEU GLU
SEQRES 8 B 126 VAL GLU VAL ILE GLU GLY THR LEU GLN CYS PRO GLU SER
SEQRES 9 B 126 GLY ARG MSE PHE PRO ILE SER ARG GLY ILE PRO ASN MSE
SEQRES 10 B 126 LEU LEU SER GLU GLU GLU THR GLU SER
SEQRES 1 D 228 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 D 228 PRO MSE ALA GLY GLU ASN PHE ALA THR PRO PHE HIS GLY
SEQRES 3 D 228 HIS VAL GLY ARG GLY ALA PHE SER ASP VAL TYR GLU PRO
SEQRES 4 D 228 ALA GLU ASP THR PHE LEU LEU LEU ASP ALA LEU GLU ALA
SEQRES 5 D 228 ALA ALA ALA GLU LEU ALA GLY VAL GLU ILE CYS LEU GLU
SEQRES 6 D 228 VAL GLY SER GLY SER GLY VAL VAL SER ALA PHE LEU ALA
SEQRES 7 D 228 SER MSE ILE GLY PRO GLN ALA LEU TYR MSE CYS THR ASP
SEQRES 8 D 228 ILE ASN PRO GLU ALA ALA ALA CYS THR LEU GLU THR ALA
SEQRES 9 D 228 ARG CYS ASN LYS VAL HIS ILE GLN PRO VAL ILE THR ASP
SEQRES 10 D 228 LEU VAL LYS GLY LEU LEU PRO ARG LEU THR GLU LYS VAL
SEQRES 11 D 228 ASP LEU LEU VAL PHE ASN PRO PRO TYR VAL VAL THR PRO
SEQRES 12 D 228 PRO GLN GLU VAL GLY SER HIS GLY ILE GLU ALA ALA TRP
SEQRES 13 D 228 ALA GLY GLY ARG ASN GLY ARG GLU VAL MSE ASP ARG PHE
SEQRES 14 D 228 PHE PRO LEU VAL PRO ASP LEU LEU SER PRO ARG GLY LEU
SEQRES 15 D 228 PHE TYR LEU VAL THR ILE LYS GLU ASN ASN PRO GLU GLU
SEQRES 16 D 228 ILE LEU LYS ILE MSE LYS THR LYS GLY LEU GLN GLY THR
SEQRES 17 D 228 THR ALA LEU SER ARG GLN ALA GLY GLN GLU THR LEU SER
SEQRES 18 D 228 VAL LEU LYS PHE THR LYS SER
MODRES 6KMS MSE C 66 MET MODIFIED RESIDUE
MODRES 6KMS MSE C 74 MET MODIFIED RESIDUE
MODRES 6KMS MSE C 152 MET MODIFIED RESIDUE
MODRES 6KMS MSE C 186 MET MODIFIED RESIDUE
MODRES 6KMS MSE A 1 MET MODIFIED RESIDUE
MODRES 6KMS MSE A 45 MET MODIFIED RESIDUE
MODRES 6KMS MSE A 84 MET MODIFIED RESIDUE
MODRES 6KMS MSE A 106 MET MODIFIED RESIDUE
MODRES 6KMS MSE A 116 MET MODIFIED RESIDUE
MODRES 6KMS MSE B 1 MET MODIFIED RESIDUE
MODRES 6KMS MSE B 45 MET MODIFIED RESIDUE
MODRES 6KMS MSE B 84 MET MODIFIED RESIDUE
MODRES 6KMS MSE B 106 MET MODIFIED RESIDUE
MODRES 6KMS MSE B 116 MET MODIFIED RESIDUE
MODRES 6KMS MSE D 66 MET MODIFIED RESIDUE
MODRES 6KMS MSE D 74 MET MODIFIED RESIDUE
MODRES 6KMS MSE D 152 MET MODIFIED RESIDUE
MODRES 6KMS MSE D 186 MET MODIFIED RESIDUE
HET MSE C 66 8
HET MSE C 74 8
HET MSE C 152 8
HET MSE C 186 8
HET MSE A 0 8
HET MSE A 1 8
HET MSE A 45 8
HET MSE A 84 8
HET MSE A 106 8
HET MSE A 116 8
HET MSE B 0 8
HET MSE B 1 8
HET MSE B 45 8
HET MSE B 84 8
HET MSE B 106 8
HET MSE B 116 8
HET MSE D 66 8
HET MSE D 74 8
HET MSE D 152 8
HET MSE D 186 8
HET SAM C 301 27
HET SAM D 301 27
HETNAM MSE SELENOMETHIONINE
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 5 SAM 2(C15 H22 N6 O5 S)
HELIX 1 AA1 ARG C 16 SER C 20 5 5
HELIX 2 AA2 ALA C 26 ALA C 39 1 14
HELIX 3 AA3 ALA C 41 VAL C 46 5 6
HELIX 4 AA4 GLY C 57 GLY C 68 1 12
HELIX 5 AA5 ASN C 79 ASN C 93 1 15
HELIX 6 AA6 PRO C 129 VAL C 133 5 5
HELIX 7 AA7 ILE C 138 ALA C 143 1 6
HELIX 8 AA8 GLY C 145 GLY C 148 5 4
HELIX 9 AA9 ARG C 149 PHE C 156 1 8
HELIX 10 AB1 LEU C 158 LEU C 162 1 5
HELIX 11 AB2 ILE C 174 ASN C 177 5 4
HELIX 12 AB3 ASN C 178 THR C 188 1 11
HELIX 13 AB4 LEU A 3 ASN A 7 1 5
HELIX 14 AB5 VAL A 16 PHE A 21 5 6
HELIX 15 AB6 ASN A 38 ILE A 46 1 9
HELIX 16 AB7 GLU A 50 LEU A 61 1 12
HELIX 17 AB8 ASN A 77 GLU A 90 1 14
HELIX 18 AB9 LYS B 2 ASN B 7 1 6
HELIX 19 AC1 VAL B 16 GLY B 20 5 5
HELIX 20 AC2 ASN B 38 ILE B 46 1 9
HELIX 21 AC3 GLU B 50 LEU B 61 1 12
HELIX 22 AC4 ASN B 77 GLU B 90 1 14
HELIX 23 AC5 ALA D 26 ALA D 39 1 14
HELIX 24 AC6 GLY D 57 GLY D 68 1 12
HELIX 25 AC7 ASN D 79 ASN D 93 1 15
HELIX 26 AC8 GLY D 137 ALA D 141 5 5
HELIX 27 AC9 GLY D 145 GLY D 148 5 4
HELIX 28 AD1 ARG D 149 PHE D 156 1 8
HELIX 29 AD2 PRO D 157 LEU D 162 1 6
HELIX 30 AD3 ASN D 178 LYS D 189 1 12
SHEET 1 AA1 7 ILE C 97 ILE C 101 0
SHEET 2 AA1 7 LEU C 72 ASP C 77 1 N TYR C 73 O GLN C 98
SHEET 3 AA1 7 ILE C 48 VAL C 52 1 N CYS C 49 O MSE C 74
SHEET 4 AA1 7 VAL C 116 PHE C 121 1 O VAL C 120 N LEU C 50
SHEET 5 AA1 7 LEU C 163 THR C 173 1 O LEU C 168 N ASP C 117
SHEET 6 AA1 7 GLU C 204 LYS C 213 -1 O LEU C 209 N LEU C 171
SHEET 7 AA1 7 LEU C 191 THR C 194 -1 N THR C 194 O LYS C 210
SHEET 1 AA2 7 ILE C 97 ILE C 101 0
SHEET 2 AA2 7 LEU C 72 ASP C 77 1 N TYR C 73 O GLN C 98
SHEET 3 AA2 7 ILE C 48 VAL C 52 1 N CYS C 49 O MSE C 74
SHEET 4 AA2 7 VAL C 116 PHE C 121 1 O VAL C 120 N LEU C 50
SHEET 5 AA2 7 LEU C 163 THR C 173 1 O LEU C 168 N ASP C 117
SHEET 6 AA2 7 GLU C 204 LYS C 213 -1 O LEU C 209 N LEU C 171
SHEET 7 AA2 7 ARG C 199 ALA C 201 -1 N ALA C 201 O GLU C 204
SHEET 1 AA3 3 MSE A 1 LYS A 2 0
SHEET 2 AA3 3 VAL A 91 GLN A 99 -1 O VAL A 93 N MSE A 1
SHEET 3 AA3 3 ARG A 24 ILE A 32 -1 N GLU A 29 O ILE A 94
SHEET 1 AA4 4 MSE A 1 LYS A 2 0
SHEET 2 AA4 4 VAL A 91 GLN A 99 -1 O VAL A 93 N MSE A 1
SHEET 3 AA4 4 MSE A 106 SER A 110 -1 O PHE A 107 N LEU A 98
SHEET 4 AA4 4 ILE A 113 PRO A 114 -1 O ILE A 113 N SER A 110
SHEET 1 AA5 4 ARG B 24 ILE B 32 0
SHEET 2 AA5 4 VAL B 91 GLN B 99 -1 O GLN B 99 N ARG B 24
SHEET 3 AA5 4 MSE B 106 SER B 110 -1 O PHE B 107 N LEU B 98
SHEET 4 AA5 4 ILE B 113 PRO B 114 -1 O ILE B 113 N SER B 110
SHEET 1 AA6 6 ILE D 97 VAL D 100 0
SHEET 2 AA6 6 LEU D 72 THR D 76 1 N TYR D 73 O GLN D 98
SHEET 3 AA6 6 ILE D 48 LEU D 50 1 N CYS D 49 O LEU D 72
SHEET 4 AA6 6 VAL D 116 PHE D 121 1 O VAL D 120 N LEU D 50
SHEET 5 AA6 6 LEU D 163 THR D 173 1 O SER D 164 N VAL D 116
SHEET 6 AA6 6 SER D 207 VAL D 208 -1 O SER D 207 N THR D 173
SHEET 1 AA7 6 ILE D 97 VAL D 100 0
SHEET 2 AA7 6 LEU D 72 THR D 76 1 N TYR D 73 O GLN D 98
SHEET 3 AA7 6 ILE D 48 LEU D 50 1 N CYS D 49 O LEU D 72
SHEET 4 AA7 6 VAL D 116 PHE D 121 1 O VAL D 120 N LEU D 50
SHEET 5 AA7 6 LEU D 163 THR D 173 1 O SER D 164 N VAL D 116
SHEET 6 AA7 6 PHE D 211 THR D 212 -1 O PHE D 211 N PHE D 169
LINK C SER C 65 N MSE C 66 1555 1555 1.32
LINK C MSE C 66 N ILE C 67 1555 1555 1.33
LINK C TYR C 73 N MSE C 74 1555 1555 1.32
LINK C MSE C 74 N CYS C 75 1555 1555 1.32
LINK C VAL C 151 N MSE C 152 1555 1555 1.34
LINK C MSE C 152 N ASP C 153 1555 1555 1.34
LINK C ILE C 185 N MSE C 186 1555 1555 1.33
LINK C MSE C 186 N LYS C 187 1555 1555 1.34
LINK C MSE A 0 N MSE A 1 1555 1555 1.35
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C ARG A 44 N MSE A 45 1555 1555 1.34
LINK C MSE A 45 N ILE A 46 1555 1555 1.34
LINK C THR A 83 N MSE A 84 1555 1555 1.33
LINK C MSE A 84 N HIS A 85 1555 1555 1.34
LINK C ARG A 105 N MSE A 106 1555 1555 1.32
LINK C MSE A 106 N PHE A 107 1555 1555 1.32
LINK C ASN A 115 N MSE A 116 1555 1555 1.32
LINK C MSE A 116 N LEU A 117 1555 1555 1.33
LINK C MSE B 0 N MSE B 1 1555 1555 1.35
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C ARG B 44 N MSE B 45 1555 1555 1.33
LINK C MSE B 45 N ILE B 46 1555 1555 1.33
LINK C THR B 83 N MSE B 84 1555 1555 1.33
LINK C MSE B 84 N HIS B 85 1555 1555 1.33
LINK C ARG B 105 N MSE B 106 1555 1555 1.32
LINK C MSE B 106 N PHE B 107 1555 1555 1.33
LINK C ASN B 115 N MSE B 116 1555 1555 1.33
LINK C MSE B 116 N LEU B 117 1555 1555 1.33
LINK C SER D 65 N MSE D 66 1555 1555 1.32
LINK C MSE D 66 N ILE D 67 1555 1555 1.34
LINK C TYR D 73 N MSE D 74 1555 1555 1.33
LINK C MSE D 74 N CYS D 75 1555 1555 1.34
LINK C VAL D 151 N MSE D 152 1555 1555 1.32
LINK C MSE D 152 N ASP D 153 1555 1555 1.34
LINK C ILE D 185 N MSE D 186 1555 1555 1.33
LINK C MSE D 186 N LYS D 187 1555 1555 1.34
CISPEP 1 LEU C 109 PRO C 110 0 6.45
CISPEP 2 PHE A 21 PRO A 22 0 -1.91
CISPEP 3 PHE B 21 PRO B 22 0 -0.94
CISPEP 4 LEU D 109 PRO D 110 0 3.79
SITE 1 AC1 15 TYR C 23 THR C 29 GLU C 51 GLY C 53
SITE 2 AC1 15 SER C 54 GLY C 55 SER C 56 ASP C 77
SITE 3 AC1 15 ILE C 78 ASP C 103 LEU C 104 ASN C 122
SITE 4 AC1 15 PRO C 124 ALA C 140 ALA C 141
SITE 1 AC2 13 TYR D 23 THR D 29 GLU D 51 GLY D 53
SITE 2 AC2 13 GLY D 55 VAL D 59 ASP D 77 ILE D 78
SITE 3 AC2 13 LEU D 104 ASN D 122 ALA D 140 ALA D 141
SITE 4 AC2 13 ARG D 154
CRYST1 195.354 195.354 246.551 90.00 90.00 90.00 I 4 2 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 0.005119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004056 0.00000
(ATOM LINES ARE NOT SHOWN.)
END