HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 07-OCT-10 3P51
TITLE THREE-DIMENSIONAL STRUCTURE OF PROTEIN Q2Y8N9_NITMU FROM NITROSOSPIRA
TITLE 2 MULTIFORMIS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET NMR118
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NITROSOSPIRA MULTIFORMIS;
SOURCE 3 ORGANISM_TAXID: 323848;
SOURCE 4 STRAIN: ATCC 25196 / NCIMB 11849;
SOURCE 5 GENE: NMUL_A1581;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) + MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET 21-23C
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUZIN,Y.CHEN,J.SEETHARAMAN,S.SAHDEV,R.XIAO,C.CICCOSANTI,D.LEE,
AUTHOR 2 J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,J.F.HUNT,L.TONG,
AUTHOR 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 2 22-FEB-12 3P51 1 VERSN KEYWDS
REVDAT 1 27-OCT-10 3P51 0
JRNL AUTH A.KUZIN,Y.CHEN,J.SEETHARAMAN,S.SAHDEV,R.XIAO,C.CICCOSANTI,
JRNL AUTH 2 D.LEE,J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,
JRNL AUTH 3 J.F.HUNT,L.TONG
JRNL TITL NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET NMR118
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 13511
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1229
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 44.83
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.29500
REMARK 3 B22 (A**2) : 5.29500
REMARK 3 B33 (A**2) : -10.58900
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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): 24.9863 18.7290 63.3293
REMARK 3 T TENSOR
REMARK 3 T11: 0.3621 T22: 0.2632
REMARK 3 T33: 0.2332 T12: -0.0536
REMARK 3 T13: 0.0444 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 1.3958 L22: 0.5803
REMARK 3 L33: 0.6956 L12: -0.4318
REMARK 3 L13: -0.3832 L23: 0.6197
REMARK 3 S TENSOR
REMARK 3 S11: -0.1437 S12: 0.1651 S13: -0.0943
REMARK 3 S21: -0.0179 S22: -0.0021 S23: 0.0505
REMARK 3 S31: 0.2048 S32: 0.0199 S33: 0.1340
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 3P51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23884
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 10.700
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.33000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX.AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,
REMARK 280 0.02% NAN3, 10MM TRIS-HCL (PH 7.5), RESERVOIR SOLUTION: LICL
REMARK 280 4.42M, BIS-TRIS PROPANE 0.1M, MACROBATCH UNDER OIL, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.08533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 72.17067
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.08533
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.17067
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.08533
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 72.17067
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.08533
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 72.17067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 40.20450
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 69.63624
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 144.34133
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 40.20450
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 69.63624
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 144.34133
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 298 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 242 LIES ON A SPECIAL POSITION.
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 A 1
REMARK 465 SER A 147
REMARK 465 GLU A 148
REMARK 465 TRP A 149
REMARK 465 ILE A 150
REMARK 465 ASP A 151
REMARK 465 GLN A 152
REMARK 465 LEU A 153
REMARK 465 GLU A 154
REMARK 465 HIS A 155
REMARK 465 HIS A 156
REMARK 465 HIS A 157
REMARK 465 HIS A 158
REMARK 465 HIS A 159
REMARK 465 HIS A 160
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 GLU A 57 -23.41 -147.36
REMARK 500 THR A 105 -169.29 -109.61
REMARK 500 PHE A 140 77.90 -116.28
REMARK 500 ARG A 145 58.92 -94.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NMR118 RELATED DB: TARGETDB
DBREF 3P51 A 1 152 UNP Q2Y8N9 Q2Y8N9_NITMU 1 152
SEQADV 3P51 LEU A 153 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 GLU A 154 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 HIS A 155 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 HIS A 156 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 HIS A 157 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 HIS A 158 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 HIS A 159 UNP Q2Y8N9 EXPRESSION TAG
SEQADV 3P51 HIS A 160 UNP Q2Y8N9 EXPRESSION TAG
SEQRES 1 A 160 MSE PRO LYS VAL TYR ASN SER ILE VAL VAL ASP ALA PRO
SEQRES 2 A 160 VAL GLU ARG VAL TRP SER ARG ILE ARG ASN PHE HIS ASP
SEQRES 3 A 160 PHE SER TRP ALA PRO SER LEU ILE LYS SER CYS LYS LYS
SEQRES 4 A 160 VAL GLY GLY GLY GLY GLY TYR SER VAL GLY ALA ARG ARG
SEQRES 5 A 160 LEU LEU ASN GLY GLU PHE LEU ASP THR LEU ILE ALA TYR
SEQRES 6 A 160 SER GLU ILE GLU ARG ARG ILE MSE TYR SER MSE ASP GLU
SEQRES 7 A 160 GLY PRO SER PRO VAL SER SER GLY GLU ILE TYR ASN TYR
SEQRES 8 A 160 VAL GLY ASN LEU HIS LEU LEU PRO VAL THR ILE ASP ASP
SEQRES 9 A 160 THR THR PHE VAL GLU TRP SER GLY SER TRP GLU SER ALA
SEQRES 10 A 160 SER THR GLU ALA VAL GLU TYR MSE ASN THR VAL TYR ARG
SEQRES 11 A 160 SER LEU LEU ALA ASP LEU ALA ALA GLU PHE THR SER GLU
SEQRES 12 A 160 SER ARG ARG SER GLU TRP ILE ASP GLN LEU GLU HIS HIS
SEQRES 13 A 160 HIS HIS HIS HIS
MODRES 3P51 MSE A 73 MET SELENOMETHIONINE
MODRES 3P51 MSE A 76 MET SELENOMETHIONINE
MODRES 3P51 MSE A 125 MET SELENOMETHIONINE
HET MSE A 73 8
HET MSE A 76 8
HET MSE A 125 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 HOH *142(H2 O)
HELIX 1 1 PRO A 13 ARG A 22 1 10
HELIX 2 2 GLU A 120 PHE A 140 1 21
SHEET 1 A 7 LYS A 3 VAL A 10 0
SHEET 2 A 7 THR A 105 SER A 116 -1 O THR A 106 N VAL A 10
SHEET 3 A 7 ILE A 88 VAL A 100 -1 N LEU A 98 O PHE A 107
SHEET 4 A 7 ARG A 71 GLU A 78 -1 N TYR A 74 O GLY A 93
SHEET 5 A 7 PHE A 58 SER A 66 -1 N ALA A 64 O MSE A 73
SHEET 6 A 7 ARG A 51 LEU A 54 -1 N LEU A 54 O PHE A 58
SHEET 7 A 7 CYS A 37 VAL A 40 -1 N LYS A 38 O LEU A 53
LINK C ILE A 72 N MSE A 73 1555 1555 1.33
LINK C MSE A 73 N TYR A 74 1555 1555 1.32
LINK C SER A 75 N MSE A 76 1555 1555 1.33
LINK C MSE A 76 N ASP A 77 1555 1555 1.33
LINK C TYR A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N ASN A 126 1555 1555 1.33
CISPEP 1 SER A 81 PRO A 82 0 7.54
CRYST1 80.409 80.409 108.256 90.00 90.00 120.00 P 64 2 2 12
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 0.012436 0.007180 0.000000 0.00000
SCALE2 0.000000 0.014360 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009237 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
