HEADER TRANSFERASE 18-JUN-14 4QNX
TITLE CRYSTAL STRUCTURE OF APO-CMOB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA (MO5U34)-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B1871, CMOB, JW1860, YECP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: LIC PET30A
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, NEW YORK STRUCTURAL GENOMICS
KEYWDS 2 RESEARCH CONSORTIUM, NYSGRC, ROSSMANN FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KIM,R.TORO,R.BHOSLE,S.C.ALMO,NEW YORK STRUCTURAL GENOMICS RESEARCH
AUTHOR 2 CONSORTIUM (NYSGRC)
REVDAT 4 28-FEB-24 4QNX 1 REMARK
REVDAT 3 10-JUN-15 4QNX 1 JRNL
REVDAT 2 22-APR-15 4QNX 1 JRNL
REVDAT 1 17-SEP-14 4QNX 0
JRNL AUTH J.KIM,H.XIAO,J.KOH,Y.WANG,J.B.BONANNO,K.THOMAS,P.C.BABBITT,
JRNL AUTH 2 S.BROWN,Y.S.LEE,S.C.ALMO
JRNL TITL DETERMINANTS OF THE CMOB CARBOXYMETHYL TRANSFERASE UTILIZED
JRNL TITL 2 FOR SELECTIVE TRNA WOBBLE MODIFICATION.
JRNL REF NUCLEIC ACIDS RES. V. 43 4602 2015
JRNL REFN ISSN 0305-1048
JRNL PMID 25855808
JRNL DOI 10.1093/NAR/GKV206
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 30170
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1530
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 47.5451 - 5.8220 0.97 2612 143 0.1874 0.2236
REMARK 3 2 5.8220 - 4.6223 0.97 2574 145 0.1755 0.2019
REMARK 3 3 4.6223 - 4.0384 0.96 2553 142 0.1685 0.2360
REMARK 3 4 4.0384 - 3.6693 0.98 2589 135 0.1887 0.2417
REMARK 3 5 3.6693 - 3.4064 0.99 2626 137 0.1932 0.2571
REMARK 3 6 3.4064 - 3.2056 1.00 2649 128 0.2174 0.3026
REMARK 3 7 3.2056 - 3.0451 1.00 2624 136 0.2488 0.2978
REMARK 3 8 3.0451 - 2.9125 1.00 2627 154 0.2403 0.2969
REMARK 3 9 2.9125 - 2.8004 1.00 2626 122 0.2396 0.3331
REMARK 3 10 2.8004 - 2.7038 1.00 2630 148 0.2833 0.3190
REMARK 3 11 2.7038 - 2.6190 0.96 2530 140 0.3026 0.3501
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.009 5373
REMARK 3 ANGLE : 1.188 7321
REMARK 3 CHIRALITY : 0.049 791
REMARK 3 PLANARITY : 0.006 926
REMARK 3 DIHEDRAL : 14.896 1943
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QNX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : DOUBLE SILICON(111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30190
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.83700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26M AMMONIUM SULFATE, AND 100MM
REMARK 280 HEPES/NAOH PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 37.94250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.81700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 37.94250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 92.81700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 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 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 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 1
REMARK 465 GLN A 35
REMARK 465 HIS A 36
REMARK 465 MET B 1
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 GLN A 34 CG CD OE1 NE2
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 69 CG CD OE1 OE2
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLN B 35 CG CD OE1 NE2
REMARK 470 GLU B 51 CG CD OE1 OE2
REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 62 -163.16 -160.74
REMARK 500 PRO A 70 155.05 -42.50
REMARK 500 ALA A 189 -2.51 -141.23
REMARK 500 TYR A 250 -82.45 -106.71
REMARK 500 ASP A 274 140.09 -176.84
REMARK 500 SER A 293 -159.91 -143.99
REMARK 500 ASP A 302 87.28 -163.11
REMARK 500 GLN B 35 2.60 -152.74
REMARK 500 SER B 62 -164.33 -161.21
REMARK 500 PRO B 70 154.47 -44.02
REMARK 500 ALA B 189 -3.05 -143.07
REMARK 500 TYR B 250 -81.90 -106.13
REMARK 500 ASP B 274 141.76 -176.02
REMARK 500 SER B 293 -158.03 -145.66
REMARK 500 ASP B 302 87.11 -164.84
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-012596 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4QNV RELATED DB: PDB
REMARK 900 RELATED ID: 4QNU RELATED DB: PDB
DBREF 4QNX A 1 323 UNP P76291 CMOB_ECOLI 1 323
DBREF 4QNX B 1 323 UNP P76291 CMOB_ECOLI 1 323
SEQRES 1 A 323 MET ILE ASP PHE GLY ASN PHE TYR SER LEU ILE ALA LYS
SEQRES 2 A 323 ASN HIS LEU SER HIS TRP LEU GLU THR LEU PRO ALA GLN
SEQRES 3 A 323 ILE ALA ASN TRP GLN ARG GLU GLN GLN HIS GLY LEU PHE
SEQRES 4 A 323 LYS GLN TRP SER ASN ALA VAL GLU PHE LEU PRO GLU ILE
SEQRES 5 A 323 LYS PRO TYR ARG LEU ASP LEU LEU HIS SER VAL THR ALA
SEQRES 6 A 323 GLU SER GLU GLU PRO LEU SER ALA GLY GLN ILE LYS ARG
SEQRES 7 A 323 ILE GLU THR LEU MET ARG ASN LEU MET PRO TRP ARG LYS
SEQRES 8 A 323 GLY PRO PHE SER LEU TYR GLY VAL ASN ILE ASP THR GLU
SEQRES 9 A 323 TRP ARG SER ASP TRP LYS TRP ASP ARG VAL LEU PRO HIS
SEQRES 10 A 323 LEU SER ASP LEU THR GLY ARG THR ILE LEU ASP VAL GLY
SEQRES 11 A 323 CYS GLY SER GLY TYR HIS MET TRP ARG MET ILE GLY ALA
SEQRES 12 A 323 GLY ALA HIS LEU ALA VAL GLY ILE ASP PRO THR GLN LEU
SEQRES 13 A 323 PHE LEU CYS GLN PHE GLU ALA VAL ARG LYS LEU LEU GLY
SEQRES 14 A 323 ASN ASP GLN ARG ALA HIS LEU LEU PRO LEU GLY ILE GLU
SEQRES 15 A 323 GLN LEU PRO ALA LEU LYS ALA PHE ASP THR VAL PHE SER
SEQRES 16 A 323 MET GLY VAL LEU TYR HIS ARG ARG SER PRO LEU GLU HIS
SEQRES 17 A 323 LEU TRP GLN LEU LYS ASP GLN LEU VAL ASN GLU GLY GLU
SEQRES 18 A 323 LEU VAL LEU GLU THR LEU VAL ILE ASP GLY ASP GLU ASN
SEQRES 19 A 323 THR VAL LEU VAL PRO GLY ASP ARG TYR ALA GLN MET ARG
SEQRES 20 A 323 ASN VAL TYR PHE ILE PRO SER ALA LEU ALA LEU LYS ASN
SEQRES 21 A 323 TRP LEU LYS LYS CYS GLY PHE VAL ASP ILE ARG ILE ALA
SEQRES 22 A 323 ASP VAL SER VAL THR THR THR GLU GLU GLN ARG ARG THR
SEQRES 23 A 323 GLU TRP MET VAL THR GLU SER LEU ALA ASP PHE LEU ASP
SEQRES 24 A 323 PRO HIS ASP PRO GLY LYS THR VAL GLU GLY TYR PRO ALA
SEQRES 25 A 323 PRO LYS ARG ALA VAL LEU ILE ALA ARG LYS PRO
SEQRES 1 B 323 MET ILE ASP PHE GLY ASN PHE TYR SER LEU ILE ALA LYS
SEQRES 2 B 323 ASN HIS LEU SER HIS TRP LEU GLU THR LEU PRO ALA GLN
SEQRES 3 B 323 ILE ALA ASN TRP GLN ARG GLU GLN GLN HIS GLY LEU PHE
SEQRES 4 B 323 LYS GLN TRP SER ASN ALA VAL GLU PHE LEU PRO GLU ILE
SEQRES 5 B 323 LYS PRO TYR ARG LEU ASP LEU LEU HIS SER VAL THR ALA
SEQRES 6 B 323 GLU SER GLU GLU PRO LEU SER ALA GLY GLN ILE LYS ARG
SEQRES 7 B 323 ILE GLU THR LEU MET ARG ASN LEU MET PRO TRP ARG LYS
SEQRES 8 B 323 GLY PRO PHE SER LEU TYR GLY VAL ASN ILE ASP THR GLU
SEQRES 9 B 323 TRP ARG SER ASP TRP LYS TRP ASP ARG VAL LEU PRO HIS
SEQRES 10 B 323 LEU SER ASP LEU THR GLY ARG THR ILE LEU ASP VAL GLY
SEQRES 11 B 323 CYS GLY SER GLY TYR HIS MET TRP ARG MET ILE GLY ALA
SEQRES 12 B 323 GLY ALA HIS LEU ALA VAL GLY ILE ASP PRO THR GLN LEU
SEQRES 13 B 323 PHE LEU CYS GLN PHE GLU ALA VAL ARG LYS LEU LEU GLY
SEQRES 14 B 323 ASN ASP GLN ARG ALA HIS LEU LEU PRO LEU GLY ILE GLU
SEQRES 15 B 323 GLN LEU PRO ALA LEU LYS ALA PHE ASP THR VAL PHE SER
SEQRES 16 B 323 MET GLY VAL LEU TYR HIS ARG ARG SER PRO LEU GLU HIS
SEQRES 17 B 323 LEU TRP GLN LEU LYS ASP GLN LEU VAL ASN GLU GLY GLU
SEQRES 18 B 323 LEU VAL LEU GLU THR LEU VAL ILE ASP GLY ASP GLU ASN
SEQRES 19 B 323 THR VAL LEU VAL PRO GLY ASP ARG TYR ALA GLN MET ARG
SEQRES 20 B 323 ASN VAL TYR PHE ILE PRO SER ALA LEU ALA LEU LYS ASN
SEQRES 21 B 323 TRP LEU LYS LYS CYS GLY PHE VAL ASP ILE ARG ILE ALA
SEQRES 22 B 323 ASP VAL SER VAL THR THR THR GLU GLU GLN ARG ARG THR
SEQRES 23 B 323 GLU TRP MET VAL THR GLU SER LEU ALA ASP PHE LEU ASP
SEQRES 24 B 323 PRO HIS ASP PRO GLY LYS THR VAL GLU GLY TYR PRO ALA
SEQRES 25 B 323 PRO LYS ARG ALA VAL LEU ILE ALA ARG LYS PRO
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET SO4 A 406 5
HET SO4 A 407 5
HET SO4 B 401 5
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET SO4 B 405 5
HET SO4 B 406 5
HET SO4 B 407 5
HET SO4 B 408 5
HET SO4 B 409 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 16(O4 S 2-)
FORMUL 19 HOH *88(H2 O)
HELIX 1 1 PHE A 4 ALA A 12 1 9
HELIX 2 2 LEU A 16 GLU A 21 5 6
HELIX 3 3 THR A 22 GLN A 34 1 13
HELIX 4 4 LEU A 38 LEU A 49 1 12
HELIX 5 5 SER A 72 ASN A 85 1 14
HELIX 6 6 SER A 107 LEU A 115 1 9
HELIX 7 7 PRO A 116 LEU A 118 5 3
HELIX 8 8 GLY A 134 ALA A 143 1 10
HELIX 9 9 THR A 154 LEU A 168 1 15
HELIX 10 10 GLY A 180 LEU A 184 5 5
HELIX 11 11 VAL A 198 ARG A 202 5 5
HELIX 12 12 SER A 204 ASP A 214 1 11
HELIX 13 13 SER A 254 CYS A 265 1 12
HELIX 14 14 SER A 293 PHE A 297 1 5
HELIX 15 15 PHE B 4 LYS B 13 1 10
HELIX 16 16 LEU B 16 GLU B 21 5 6
HELIX 17 17 THR B 22 GLN B 34 1 13
HELIX 18 18 GLY B 37 PHE B 48 1 12
HELIX 19 19 SER B 72 ASN B 85 1 14
HELIX 20 20 SER B 107 LEU B 115 1 9
HELIX 21 21 PRO B 116 LEU B 118 5 3
HELIX 22 22 GLY B 134 GLY B 144 1 11
HELIX 23 23 THR B 154 LEU B 168 1 15
HELIX 24 24 GLY B 180 LEU B 184 5 5
HELIX 25 25 VAL B 198 ARG B 202 5 5
HELIX 26 26 SER B 204 ASP B 214 1 11
HELIX 27 27 SER B 254 CYS B 265 1 12
HELIX 28 28 SER B 293 PHE B 297 1 5
SHEET 1 A 4 ARG A 56 ASP A 58 0
SHEET 2 A 4 THR A 64 GLU A 66 -1 O GLU A 66 N ARG A 56
SHEET 3 A 4 PHE A 94 LEU A 96 1 O SER A 95 N ALA A 65
SHEET 4 A 4 VAL A 99 ILE A 101 -1 O VAL A 99 N LEU A 96
SHEET 1 B 2 LYS A 91 GLY A 92 0
SHEET 2 B 2 TRP A 105 ARG A 106 1 O TRP A 105 N GLY A 92
SHEET 1 C 7 ALA A 174 LEU A 177 0
SHEET 2 C 7 LEU A 147 ILE A 151 1 N GLY A 150 O HIS A 175
SHEET 3 C 7 THR A 125 VAL A 129 1 N ASP A 128 O VAL A 149
SHEET 4 C 7 PHE A 190 MET A 196 1 O PHE A 194 N LEU A 127
SHEET 5 C 7 LEU A 216 LEU A 227 1 O GLU A 221 N ASP A 191
SHEET 6 C 7 LYS A 314 ARG A 321 -1 O LEU A 318 N LEU A 224
SHEET 7 C 7 VAL A 268 VAL A 277 -1 N ARG A 271 O ILE A 319
SHEET 1 D 2 VAL A 236 LEU A 237 0
SHEET 2 D 2 ILE A 252 PRO A 253 -1 O ILE A 252 N LEU A 237
SHEET 1 E 2 LEU A 298 ASP A 299 0
SHEET 2 E 2 ASP A 302 THR A 306 -1 O LYS A 305 N ASP A 299
SHEET 1 F 4 ARG B 56 ASP B 58 0
SHEET 2 F 4 THR B 64 GLU B 66 -1 O THR B 64 N ASP B 58
SHEET 3 F 4 PHE B 94 LEU B 96 1 O SER B 95 N ALA B 65
SHEET 4 F 4 VAL B 99 ILE B 101 -1 O VAL B 99 N LEU B 96
SHEET 1 G 2 LYS B 91 GLY B 92 0
SHEET 2 G 2 TRP B 105 ARG B 106 1 O TRP B 105 N GLY B 92
SHEET 1 H 7 ALA B 174 LEU B 177 0
SHEET 2 H 7 LEU B 147 ILE B 151 1 N GLY B 150 O HIS B 175
SHEET 3 H 7 THR B 125 VAL B 129 1 N ILE B 126 O VAL B 149
SHEET 4 H 7 PHE B 190 MET B 196 1 O PHE B 194 N LEU B 127
SHEET 5 H 7 LEU B 216 LEU B 227 1 O VAL B 223 N VAL B 193
SHEET 6 H 7 LYS B 314 ARG B 321 -1 O LEU B 318 N LEU B 224
SHEET 7 H 7 VAL B 268 VAL B 277 -1 N ARG B 271 O ILE B 319
SHEET 1 I 2 VAL B 236 LEU B 237 0
SHEET 2 I 2 ILE B 252 PRO B 253 -1 O ILE B 252 N LEU B 237
SHEET 1 J 2 LEU B 298 ASP B 299 0
SHEET 2 J 2 ASP B 302 THR B 306 -1 O LYS B 305 N ASP B 299
CISPEP 1 MET A 87 PRO A 88 0 -1.15
CISPEP 2 GLY A 92 PRO A 93 0 10.44
CISPEP 3 MET B 87 PRO B 88 0 -0.10
CISPEP 4 GLY B 92 PRO B 93 0 10.22
SITE 1 AC1 5 LYS A 91 TRP A 105 GLY A 197 TYR A 200
SITE 2 AC1 5 ARG A 315
SITE 1 AC2 8 ILE A 181 GLU A 182 ARG A 202 SER A 204
SITE 2 AC2 8 HIS A 208 GLN A 211 SO4 A 404 HOH A 508
SITE 1 AC3 3 GLN A 26 GLN A 183 HOH A 527
SITE 1 AC4 5 HIS A 201 ARG A 202 ARG A 203 SO4 A 402
SITE 2 AC4 5 HOH A 508
SITE 1 AC5 1 ASP A 120
SITE 1 AC6 2 SER A 72 GLN A 75
SITE 1 AC7 3 LYS A 188 ASN A 218 LYS A 322
SITE 1 AC8 5 ILE B 181 GLU B 182 ARG B 202 HIS B 208
SITE 2 AC8 5 SO4 B 409
SITE 1 AC9 5 LYS B 91 TRP B 105 GLY B 197 TYR B 200
SITE 2 AC9 5 ARG B 315
SITE 1 BC1 2 GLN B 26 GLN B 183
SITE 1 BC2 3 SER B 72 GLY B 74 GLN B 75
SITE 1 BC3 1 ASP B 120
SITE 1 BC4 2 PRO B 50 ARG B 78
SITE 1 BC5 1 ARG B 242
SITE 1 BC6 3 LYS B 188 ASN B 218 LYS B 322
SITE 1 BC7 4 HIS B 201 ARG B 202 ARG B 203 SO4 B 401
CRYST1 75.885 185.634 75.445 90.00 101.88 90.00 C 1 2 1 8
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 0.013178 0.000000 0.002773 0.00000
SCALE2 0.000000 0.005387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013545 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
