HEADER PROTEIN BINDING 10-DEC-09 3L0M
TITLE CRYSTAL STRUCTURE OF RAB1-ACTIVATION DOMAIN AND P4M DOMAIN OF
TITLE 2 SIDM/DRRA FROM LEGIONELLA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DRRA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RAB1-ACTIVATION DOMAIN, P4M DOMAIN;
COMPND 5 SYNONYM: SIDM;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA;
SOURCE 3 ORGANISM_TAXID: 446;
SOURCE 4 GENE: SIDM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2
KEYWDS GEF/GDF OF RAB1, A NEW NOVEL PHOSPHATIDYLINOSITOL 4-PHOSPHATE-BINDING
KEYWDS 2 DOMAIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHU,F.SHAO
REVDAT 2 24-NOV-10 3L0M 1 JRNL
REVDAT 1 22-DEC-09 3L0M 0
JRNL AUTH Y.ZHU,L.HU,Y.ZHOU,Q.YAO,L.LIU,F.SHAO
JRNL TITL STRUCTURAL MECHANISM OF HOST RAB1 ACTIVATION BY THE
JRNL TITL 2 BIFUNCTIONAL LEGIONELLA TYPE IV EFFECTOR SIDM/DRRA
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 4699 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20176951
JRNL DOI 10.1073/PNAS.0914231107
REMARK 2
REMARK 2 RESOLUTION. 3.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 27365
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2728
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5109
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 145.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -27.90100
REMARK 3 B22 (A**2) : -27.90100
REMARK 3 B33 (A**2) : 55.80200
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.33
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.72
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 106.39
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : SO4_XPLOR.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3L0M COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97907
REMARK 200 MONOCHROMATOR : NULL
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27431
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.449
REMARK 200 RESOLUTION RANGE LOW (A) : 144.337
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 82.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6M POTASSIUM SODIUM TARTRATE, 0.1M
REMARK 280 CHES, 0.1M LI2SO4, 0.1M SODIUM ACETATE, PH 9.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 51.14000
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 25.57000
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 76.71000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 GLY A 312
REMARK 465 ARG A 641
REMARK 465 GLN A 642
REMARK 465 THR A 643
REMARK 465 ILE A 644
REMARK 465 LYS A 645
REMARK 465 ILE A 646
REMARK 465 LYS A 647
REMARK 465 GLY B 312
REMARK 465 ASN B 551
REMARK 465 PHE B 552
REMARK 465 LYS B 553
REMARK 465 GLN B 639
REMARK 465 GLU B 640
REMARK 465 ARG B 641
REMARK 465 GLN B 642
REMARK 465 THR B 643
REMARK 465 ILE B 644
REMARK 465 LYS B 645
REMARK 465 ILE B 646
REMARK 465 LYS B 647
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 594 CG CD OE1 OE2
REMARK 470 SER B 320 OG
REMARK 470 GLU B 594 CG CD OE1 OE2
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 ASN B 437 CB - CA - C ANGL. DEV. = 12.0 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 SER A 316 -10.60 93.47
REMARK 500 PRO A 318 169.36 -47.94
REMARK 500 ARG A 339 -14.44 -48.90
REMARK 500 SER A 366 -8.68 -52.19
REMARK 500 SER A 394 -9.80 -59.81
REMARK 500 SER A 426 38.12 -148.83
REMARK 500 THR A 427 -67.65 -124.66
REMARK 500 LYS A 447 -56.83 -123.84
REMARK 500 PRO A 481 8.90 -64.84
REMARK 500 TRP A 486 -121.84 47.97
REMARK 500 ASN A 508 58.36 18.63
REMARK 500 LYS A 533 -33.90 -34.88
REMARK 500 ASP A 538 -138.07 -145.75
REMARK 500 GLU A 539 -73.81 -59.90
REMARK 500 GLU A 542 -154.25 -78.21
REMARK 500 HIS A 543 -150.94 -175.09
REMARK 500 ARG A 544 -15.95 179.78
REMARK 500 TYR A 545 58.01 -150.03
REMARK 500 GLU A 550 -162.46 -54.70
REMARK 500 ASN A 551 -19.04 73.45
REMARK 500 LYS A 556 154.69 -41.93
REMARK 500 GLU A 557 -99.03 -27.17
REMARK 500 LYS A 558 -46.29 -6.46
REMARK 500 GLN A 560 -77.21 -128.73
REMARK 500 GLN A 561 16.01 -69.26
REMARK 500 LEU A 610 -74.23 -42.53
REMARK 500 THR A 619 174.77 -56.56
REMARK 500 LYS A 637 36.24 -74.26
REMARK 500 SER A 638 -25.30 -140.87
REMARK 500 SER B 316 -20.30 84.94
REMARK 500 LEU B 335 -7.18 -57.64
REMARK 500 LYS B 362 63.73 -102.50
REMARK 500 ASN B 383 57.31 34.31
REMARK 500 PRO B 400 10.06 -64.57
REMARK 500 SER B 426 60.43 -155.72
REMARK 500 THR B 427 -50.82 -140.43
REMARK 500 LYS B 447 -61.81 -156.70
REMARK 500 LYS B 461 134.08 -170.36
REMARK 500 PRO B 481 29.74 -65.82
REMARK 500 THR B 482 16.37 -152.63
REMARK 500 TRP B 486 -98.36 68.05
REMARK 500 ASN B 508 58.61 19.71
REMARK 500 SER B 520 30.88 -81.22
REMARK 500 ASN B 525 73.50 -102.99
REMARK 500 LYS B 533 -31.70 -31.64
REMARK 500 ASP B 538 -131.46 -140.40
REMARK 500 GLU B 542 -147.45 -77.51
REMARK 500 HIS B 543 -146.02 -179.99
REMARK 500 ARG B 544 -19.43 174.07
REMARK 500 TYR B 545 48.24 -145.60
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L0I RELATED DB: PDB
DBREF 3L0M A 317 647 UNP Q29ST3 Q29ST3_LEGPN 317 647
DBREF 3L0M B 317 647 UNP Q29ST3 Q29ST3_LEGPN 317 647
SEQADV 3L0M GLY A 312 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M PRO A 313 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M LEU A 314 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M GLY A 315 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M SER A 316 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M GLY B 312 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M PRO B 313 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M LEU B 314 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M GLY B 315 UNP Q29ST3 EXPRESSION TAG
SEQADV 3L0M SER B 316 UNP Q29ST3 EXPRESSION TAG
SEQRES 1 A 336 GLY PRO LEU GLY SER MSE PRO TYR SER ASP ALA LYS ALA
SEQRES 2 A 336 MSE LEU ASP GLU VAL ALA LYS ILE ARG GLU LEU GLY VAL
SEQRES 3 A 336 GLN ARG VAL THR ARG ILE GLU ASN LEU GLU ASN ALA LYS
SEQRES 4 A 336 LYS LEU TRP ASP ASN ALA ASN SER MSE LEU GLU LYS GLY
SEQRES 5 A 336 ASN ILE SER GLY TYR LEU LYS ALA ALA ASN GLU LEU HIS
SEQRES 6 A 336 LYS PHE MSE LYS GLU LYS ASN LEU LYS GLU ASP ASP LEU
SEQRES 7 A 336 ARG PRO GLU LEU SER ASP LYS THR ILE SER PRO LYS GLY
SEQRES 8 A 336 TYR ALA ILE LEU GLN SER LEU TRP GLY ALA ALA SER ASP
SEQRES 9 A 336 TYR SER ARG ALA ALA ALA THR LEU THR GLU SER THR VAL
SEQRES 10 A 336 GLU PRO GLY LEU VAL SER ALA VAL ASN LYS MSE SER ALA
SEQRES 11 A 336 PHE PHE MSE ASP CYS LYS LEU SER PRO ASN GLU ARG ALA
SEQRES 12 A 336 THR PRO ASP PRO ASP PHE LYS VAL GLY LYS SER LYS ILE
SEQRES 13 A 336 LEU VAL GLY ILE MSE GLN PHE ILE LYS ASP VAL ALA ASP
SEQRES 14 A 336 PRO THR SER LYS ILE TRP MSE HIS ASN THR LYS ALA LEU
SEQRES 15 A 336 MSE ASN HIS LYS ILE ALA ALA ILE GLN LYS LEU GLU ARG
SEQRES 16 A 336 SER ASN ASN VAL ASN ASP GLU THR LEU GLU SER VAL LEU
SEQRES 17 A 336 SER SER LYS GLY GLU ASN LEU SER GLU TYR LEU SER TYR
SEQRES 18 A 336 LYS TYR ALA THR LYS ASP GLU GLY ARG GLU HIS ARG TYR
SEQRES 19 A 336 THR ALA SER THR GLU ASN PHE LYS ASN VAL LYS GLU LYS
SEQRES 20 A 336 TYR GLN GLN MSE ARG GLY ASP ALA LEU LYS THR GLU ILE
SEQRES 21 A 336 LEU ALA ASP PHE LYS ASP LYS LEU ALA GLU ALA THR ASP
SEQRES 22 A 336 GLU GLN SER LEU LYS GLN ILE VAL ALA GLU LEU LYS SER
SEQRES 23 A 336 LYS ASP GLU TYR ARG ILE LEU ALA LYS GLY GLN GLY LEU
SEQRES 24 A 336 THR THR GLN LEU LEU GLY LEU LYS THR SER SER VAL SER
SEQRES 25 A 336 SER PHE GLU LYS MSE VAL GLU GLU THR ARG GLU SER ILE
SEQRES 26 A 336 LYS SER GLN GLU ARG GLN THR ILE LYS ILE LYS
SEQRES 1 B 336 GLY PRO LEU GLY SER MSE PRO TYR SER ASP ALA LYS ALA
SEQRES 2 B 336 MSE LEU ASP GLU VAL ALA LYS ILE ARG GLU LEU GLY VAL
SEQRES 3 B 336 GLN ARG VAL THR ARG ILE GLU ASN LEU GLU ASN ALA LYS
SEQRES 4 B 336 LYS LEU TRP ASP ASN ALA ASN SER MSE LEU GLU LYS GLY
SEQRES 5 B 336 ASN ILE SER GLY TYR LEU LYS ALA ALA ASN GLU LEU HIS
SEQRES 6 B 336 LYS PHE MSE LYS GLU LYS ASN LEU LYS GLU ASP ASP LEU
SEQRES 7 B 336 ARG PRO GLU LEU SER ASP LYS THR ILE SER PRO LYS GLY
SEQRES 8 B 336 TYR ALA ILE LEU GLN SER LEU TRP GLY ALA ALA SER ASP
SEQRES 9 B 336 TYR SER ARG ALA ALA ALA THR LEU THR GLU SER THR VAL
SEQRES 10 B 336 GLU PRO GLY LEU VAL SER ALA VAL ASN LYS MSE SER ALA
SEQRES 11 B 336 PHE PHE MSE ASP CYS LYS LEU SER PRO ASN GLU ARG ALA
SEQRES 12 B 336 THR PRO ASP PRO ASP PHE LYS VAL GLY LYS SER LYS ILE
SEQRES 13 B 336 LEU VAL GLY ILE MSE GLN PHE ILE LYS ASP VAL ALA ASP
SEQRES 14 B 336 PRO THR SER LYS ILE TRP MSE HIS ASN THR LYS ALA LEU
SEQRES 15 B 336 MSE ASN HIS LYS ILE ALA ALA ILE GLN LYS LEU GLU ARG
SEQRES 16 B 336 SER ASN ASN VAL ASN ASP GLU THR LEU GLU SER VAL LEU
SEQRES 17 B 336 SER SER LYS GLY GLU ASN LEU SER GLU TYR LEU SER TYR
SEQRES 18 B 336 LYS TYR ALA THR LYS ASP GLU GLY ARG GLU HIS ARG TYR
SEQRES 19 B 336 THR ALA SER THR GLU ASN PHE LYS ASN VAL LYS GLU LYS
SEQRES 20 B 336 TYR GLN GLN MSE ARG GLY ASP ALA LEU LYS THR GLU ILE
SEQRES 21 B 336 LEU ALA ASP PHE LYS ASP LYS LEU ALA GLU ALA THR ASP
SEQRES 22 B 336 GLU GLN SER LEU LYS GLN ILE VAL ALA GLU LEU LYS SER
SEQRES 23 B 336 LYS ASP GLU TYR ARG ILE LEU ALA LYS GLY GLN GLY LEU
SEQRES 24 B 336 THR THR GLN LEU LEU GLY LEU LYS THR SER SER VAL SER
SEQRES 25 B 336 SER PHE GLU LYS MSE VAL GLU GLU THR ARG GLU SER ILE
SEQRES 26 B 336 LYS SER GLN GLU ARG GLN THR ILE LYS ILE LYS
MODRES 3L0M MSE A 317 MET SELENOMETHIONINE
MODRES 3L0M MSE A 325 MET SELENOMETHIONINE
MODRES 3L0M MSE A 359 MET SELENOMETHIONINE
MODRES 3L0M MSE A 379 MET SELENOMETHIONINE
MODRES 3L0M MSE A 439 MET SELENOMETHIONINE
MODRES 3L0M MSE A 444 MET SELENOMETHIONINE
MODRES 3L0M MSE A 472 MET SELENOMETHIONINE
MODRES 3L0M MSE A 487 MET SELENOMETHIONINE
MODRES 3L0M MSE A 494 MET SELENOMETHIONINE
MODRES 3L0M MSE A 562 MET SELENOMETHIONINE
MODRES 3L0M MSE A 628 MET SELENOMETHIONINE
MODRES 3L0M MSE B 317 MET SELENOMETHIONINE
MODRES 3L0M MSE B 325 MET SELENOMETHIONINE
MODRES 3L0M MSE B 359 MET SELENOMETHIONINE
MODRES 3L0M MSE B 379 MET SELENOMETHIONINE
MODRES 3L0M MSE B 439 MET SELENOMETHIONINE
MODRES 3L0M MSE B 444 MET SELENOMETHIONINE
MODRES 3L0M MSE B 472 MET SELENOMETHIONINE
MODRES 3L0M MSE B 487 MET SELENOMETHIONINE
MODRES 3L0M MSE B 494 MET SELENOMETHIONINE
MODRES 3L0M MSE B 562 MET SELENOMETHIONINE
MODRES 3L0M MSE B 628 MET SELENOMETHIONINE
HET MSE A 317 8
HET MSE A 325 8
HET MSE A 359 8
HET MSE A 379 8
HET MSE A 439 8
HET MSE A 444 8
HET MSE A 472 8
HET MSE A 487 8
HET MSE A 494 8
HET MSE A 562 8
HET MSE A 628 8
HET MSE B 317 8
HET MSE B 325 8
HET MSE B 359 8
HET MSE B 379 8
HET MSE B 439 8
HET MSE B 444 8
HET MSE B 472 8
HET MSE B 487 8
HET MSE B 494 8
HET MSE B 562 8
HET MSE B 628 8
HET SO4 A 1 5
HET SO4 B 2 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
HELIX 1 1 PRO A 318 LYS A 362 1 45
HELIX 2 2 ASN A 364 LYS A 382 1 19
HELIX 3 3 LYS A 385 ARG A 390 1 6
HELIX 4 4 PRO A 391 SER A 394 5 4
HELIX 5 5 SER A 399 ALA A 421 1 23
HELIX 6 6 THR A 427 CYS A 446 1 20
HELIX 7 7 GLY A 463 ALA A 479 1 17
HELIX 8 8 THR A 490 SER A 507 1 18
HELIX 9 9 ASN A 511 SER A 521 1 11
HELIX 10 10 ASN A 525 LEU A 530 1 6
HELIX 11 11 GLY A 564 LEU A 579 1 16
HELIX 12 12 ALA A 580 ALA A 582 5 3
HELIX 13 13 ASP A 584 SER A 597 1 14
HELIX 14 14 ASP A 599 LYS A 606 1 8
HELIX 15 15 GLY A 609 LEU A 614 1 6
HELIX 16 16 THR A 619 SER A 635 1 17
HELIX 17 17 PRO B 318 LYS B 362 1 45
HELIX 18 18 ASN B 364 LYS B 382 1 19
HELIX 19 19 LYS B 385 ARG B 390 1 6
HELIX 20 20 PRO B 391 SER B 394 5 4
HELIX 21 21 LYS B 401 ALA B 421 1 21
HELIX 22 22 VAL B 428 CYS B 446 1 19
HELIX 23 23 GLY B 463 ALA B 479 1 17
HELIX 24 24 THR B 490 SER B 507 1 18
HELIX 25 25 ASN B 511 SER B 520 1 10
HELIX 26 26 ASN B 525 LEU B 530 1 6
HELIX 27 27 ARG B 563 LEU B 579 1 17
HELIX 28 28 ALA B 580 ALA B 582 5 3
HELIX 29 29 ASP B 584 SER B 597 1 14
HELIX 30 30 GLY B 609 LEU B 614 1 6
HELIX 31 31 THR B 619 LYS B 637 1 19
SHEET 1 A 2 LYS A 484 ILE A 485 0
SHEET 2 A 2 HIS A 488 ASN A 489 -1 O HIS A 488 N ILE A 485
SHEET 1 B 2 LYS B 484 ILE B 485 0
SHEET 2 B 2 HIS B 488 ASN B 489 -1 O HIS B 488 N ILE B 485
LINK C MSE A 317 N PRO A 318 1555 1555 1.35
LINK C MSE A 325 N LEU A 326 1555 1555 1.33
LINK C MSE A 359 N LEU A 360 1555 1555 1.33
LINK C MSE A 379 N LYS A 380 1555 1555 1.33
LINK C MSE A 439 N SER A 440 1555 1555 1.33
LINK C MSE A 444 N ASP A 445 1555 1555 1.33
LINK C MSE A 472 N GLN A 473 1555 1555 1.32
LINK C MSE A 487 N HIS A 488 1555 1555 1.32
LINK C MSE A 494 N ASN A 495 1555 1555 1.33
LINK C MSE A 562 N ARG A 563 1555 1555 1.33
LINK C MSE A 628 N VAL A 629 1555 1555 1.32
LINK C MSE B 317 N PRO B 318 1555 1555 1.34
LINK C MSE B 325 N LEU B 326 1555 1555 1.33
LINK C MSE B 359 N LEU B 360 1555 1555 1.33
LINK C MSE B 379 N LYS B 380 1555 1555 1.33
LINK C MSE B 439 N SER B 440 1555 1555 1.33
LINK C MSE B 444 N ASP B 445 1555 1555 1.33
LINK C MSE B 472 N GLN B 473 1555 1555 1.33
LINK C MSE B 487 N HIS B 488 1555 1555 1.33
LINK C MSE B 494 N ASN B 495 1555 1555 1.33
LINK C MSE B 562 N ARG B 563 1555 1555 1.33
LINK C MSE B 628 N VAL B 629 1555 1555 1.33
LINK C SER A 316 N MSE A 317 1555 1555 1.33
LINK C ALA A 324 N MSE A 325 1555 1555 1.33
LINK C SER A 358 N MSE A 359 1555 1555 1.34
LINK C PHE A 378 N MSE A 379 1555 1555 1.33
LINK C LYS A 438 N MSE A 439 1555 1555 1.33
LINK C PHE A 443 N MSE A 444 1555 1555 1.32
LINK C ILE A 471 N MSE A 472 1555 1555 1.33
LINK C TRP A 486 N MSE A 487 1555 1555 1.33
LINK C LEU A 493 N MSE A 494 1555 1555 1.33
LINK C GLN A 561 N MSE A 562 1555 1555 1.34
LINK C LYS A 627 N MSE A 628 1555 1555 1.33
LINK C SER B 316 N MSE B 317 1555 1555 1.33
LINK C ALA B 324 N MSE B 325 1555 1555 1.33
LINK C SER B 358 N MSE B 359 1555 1555 1.33
LINK C PHE B 378 N MSE B 379 1555 1555 1.33
LINK C LYS B 438 N MSE B 439 1555 1555 1.33
LINK C PHE B 443 N MSE B 444 1555 1555 1.32
LINK C ILE B 471 N MSE B 472 1555 1555 1.32
LINK C TRP B 486 N MSE B 487 1555 1555 1.33
LINK C LEU B 493 N MSE B 494 1555 1555 1.33
LINK C GLN B 561 N MSE B 562 1555 1555 1.33
LINK C LYS B 627 N MSE B 628 1555 1555 1.33
SITE 1 AC1 7 TYR A 532 ARG A 541 LYS A 568 GLN A 608
SITE 2 AC1 7 THR A 619 SER A 620 SER A 621
SITE 1 AC2 6 TYR B 532 ARG B 541 LYS B 568 THR B 619
SITE 2 AC2 6 SER B 620 SER B 621
CRYST1 144.337 144.337 102.280 90.00 90.00 90.00 P 41 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 0.006928 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009777 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
