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HEADER HYDROLASE 23-DEC-08 3FNB
TITLE CRYSTAL STRUCTURE OF ACYLAMINOACYL PEPTIDASE SMU_737 FROM
TITLE 2 STREPTOCOCCUS MUTANS UA159
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINOACYL PEPTIDASE SMU_737;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS UA159;
SOURCE 3 ORGANISM_TAXID: 210007;
SOURCE 4 STRAIN: UA159;
SOURCE 5 GENE: SMU_737;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA-BETA-ALPHA SANDWICH, HELIX BUNDLE, STRUCTURAL
KEYWDS 2 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,C.HATZOS,G.COBB,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 06-JAN-09 3FNB 0
JRNL AUTH Y.KIM,C.HATZOS,G.COBB,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF ACYLAMINOACYL-PEPTIDASE
JRNL TITL 2 SMU_737 FROM STREPTOCOCCUS MUTANS UA159
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 40513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2060
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 43.6262 - 5.2203 0.98 2807 162 0.1704 0.2163
REMARK 3 2 5.2203 - 4.1445 0.99 2812 140 0.1325 0.1556
REMARK 3 3 4.1445 - 3.6209 0.99 2772 146 0.1425 0.1934
REMARK 3 4 3.6209 - 3.2900 0.99 2729 162 0.1577 0.2308
REMARK 3 5 3.2900 - 3.0542 0.99 2783 141 0.1795 0.2341
REMARK 3 6 3.0542 - 2.8742 0.99 2728 154 0.1822 0.2356
REMARK 3 7 2.8742 - 2.7303 0.98 2745 152 0.1814 0.2460
REMARK 3 8 2.7303 - 2.6114 0.98 2728 128 0.1984 0.2786
REMARK 3 9 2.6114 - 2.5109 0.98 2727 145 0.2079 0.2840
REMARK 3 10 2.5109 - 2.4243 0.97 2691 141 0.2232 0.2833
REMARK 3 11 2.4243 - 2.3485 0.93 2541 147 0.2311 0.2583
REMARK 3 12 2.3485 - 2.2814 0.87 2383 134 0.2159 0.2752
REMARK 3 13 2.2814 - 2.2213 0.79 2172 121 0.2170 0.2620
REMARK 3 14 2.2213 - 2.1671 0.75 2054 106 0.2219 0.3016
REMARK 3 15 2.1671 - 2.1178 0.63 1781 81 0.2333 0.2908
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 : 0.32
REMARK 3 B_SOL : 50.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.60090
REMARK 3 B22 (A**2) : 10.86280
REMARK 3 B33 (A**2) : -7.26200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15330
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 : 0.012 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 20.730 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6597 26.1957 83.4774
REMARK 3 T TENSOR
REMARK 3 T11: 0.2206 T22: 0.2280
REMARK 3 T33: 0.2802 T12: -0.0200
REMARK 3 T13: 0.0009 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 1.6144 L22: 0.8045
REMARK 3 L33: 1.9566 L12: -0.3106
REMARK 3 L13: -0.3113 L23: 0.6001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0198 S12: 0.2350 S13: 0.2460
REMARK 3 S21: 0.0078 S22: 0.0970 S23: -0.1982
REMARK 3 S31: -0.0335 S32: 0.0924 S33: -0.1162
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5863 26.2067 64.8861
REMARK 3 T TENSOR
REMARK 3 T11: 0.2495 T22: 0.2630
REMARK 3 T33: 0.2217 T12: 0.0491
REMARK 3 T13: 0.0078 T23: 0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 1.8873 L22: 1.1843
REMARK 3 L33: 1.5994 L12: 0.2189
REMARK 3 L13: -0.8503 L23: -0.0577
REMARK 3 S TENSOR
REMARK 3 S11: 0.2098 S12: 0.3326 S13: 0.2981
REMARK 3 S21: -0.2680 S22: 0.0337 S23: 0.1438
REMARK 3 S31: -0.1242 S32: -0.1927 S33: -0.2430
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 3FNB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40750
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 43.617
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, DM, SHELXD, RESOLVE, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DI-AMMONIUM HYDROGEN CITRATE,
REMARK 280 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.23400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.9 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 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 GLU A 3
REMARK 465 ASN A 4
REMARK 465 ASN A 5
REMARK 465 THR A 6
REMARK 465 ILE A 7
REMARK 465 THR A 271
REMARK 465 ALA A 272
REMARK 465 LEU A 273
REMARK 465 LYS A 274
REMARK 465 ALA A 275
REMARK 465 PRO A 276
REMARK 465 LYS A 277
REMARK 465 THR A 278
REMARK 465 ILE A 279
REMARK 465 LEU A 280
REMARK 465 LYS A 281
REMARK 465 TRP A 282
REMARK 465 GLY A 283
REMARK 465 SER A 284
REMARK 465 LYS A 285
REMARK 465 LEU A 286
REMARK 465 VAL A 287
REMARK 465 THR A 288
REMARK 465 LYS A 400
REMARK 465 LYS A 401
REMARK 465 ASP A 402
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 GLU B 3
REMARK 465 ASN B 4
REMARK 465 ASN B 5
REMARK 465 THR B 6
REMARK 465 ILE B 7
REMARK 465 LEU B 8
REMARK 465 LYS B 9
REMARK 465 ARG B 10
REMARK 465 THR B 271
REMARK 465 ALA B 272
REMARK 465 LEU B 273
REMARK 465 LYS B 274
REMARK 465 ALA B 275
REMARK 465 PRO B 276
REMARK 465 LYS B 277
REMARK 465 THR B 278
REMARK 465 ILE B 279
REMARK 465 LEU B 280
REMARK 465 LYS B 281
REMARK 465 TRP B 282
REMARK 465 GLY B 283
REMARK 465 SER B 284
REMARK 465 LYS B 285
REMARK 465 LEU B 286
REMARK 465 VAL B 287
REMARK 465 THR B 288
REMARK 465 SER B 289
REMARK 465 LYS B 401
REMARK 465 ASP B 402
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 LYS A 16 -44.59 -144.34
REMARK 500 LYS A 78 2.09 -65.98
REMARK 500 VAL A 79 -5.54 -141.46
REMARK 500 PRO A 131 42.45 -84.40
REMARK 500 SER A 233 -126.39 59.32
REMARK 500 PHE A 269 54.42 -119.45
REMARK 500 ASN A 382 69.50 -160.24
REMARK 500 ASP B 12 51.09 -148.10
REMARK 500 LYS B 16 -39.91 -141.47
REMARK 500 LYS B 78 1.10 -54.69
REMARK 500 PRO B 131 32.18 -79.26
REMARK 500 SER B 233 -122.36 57.99
REMARK 500 PHE B 269 46.73 -101.06
REMARK 500 ASP B 362 96.16 -67.54
REMARK 500 CYS B 378 17.85 58.71
REMARK 500 ASN B 382 69.09 -157.61
REMARK 500 PHE B 398 -67.94 -99.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 441 DISTANCE = 5.91 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 403
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 404
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 403
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 404
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC61094 RELATED DB: TARGETDB
DBREF 3FNB A 1 402 UNP Q8DUZ1 Q8DUZ1_STRMU 1 402
DBREF 3FNB B 1 402 UNP Q8DUZ1 Q8DUZ1_STRMU 1 402
SEQADV 3FNB SER A -2 UNP Q8DUZ1 EXPRESSION TAG
SEQADV 3FNB ASN A -1 UNP Q8DUZ1 EXPRESSION TAG
SEQADV 3FNB ALA A 0 UNP Q8DUZ1 EXPRESSION TAG
SEQADV 3FNB SER B -2 UNP Q8DUZ1 EXPRESSION TAG
SEQADV 3FNB ASN B -1 UNP Q8DUZ1 EXPRESSION TAG
SEQADV 3FNB ALA B 0 UNP Q8DUZ1 EXPRESSION TAG
SEQRES 1 A 405 SER ASN ALA MSE LYS GLU ASN ASN THR ILE LEU LYS ARG
SEQRES 2 A 405 GLN ASP TYR LYS ILE LYS PHE ASN ASN LYS ASP MSE ASP
SEQRES 3 A 405 PHE CYS PHE ASN TRP MSE LEU GLY ILE GLY GLN ILE ILE
SEQRES 4 A 405 GLY MSE SER ALA GLY GLU LEU PHE TYR ILE ALA SER GLY
SEQRES 5 A 405 ILE ARG ASP GLY ASN PRO THR ASP TRP CYS LYS ARG PHE
SEQRES 6 A 405 ASN GLU HIS ALA ASP TYR LEU GLU ASP GLU VAL GLU ARG
SEQRES 7 A 405 VAL LYS LYS VAL GLY TYR ARG ASP LEU ILE SER HIS LEU
SEQRES 8 A 405 TYR PHE SER ALA CYS PHE SER ILE ARG ALA ALA LEU GLN
SEQRES 9 A 405 PHE THR ASP PRO LYS ASP SER GLU PHE MSE GLU ASN PHE
SEQRES 10 A 405 ARG ARG MSE GLU LYS LEU PHE MSE LEU ALA VAL ASP ASN
SEQRES 11 A 405 SER LYS ILE PRO LEU LYS SER ILE GLU VAL PRO PHE GLU
SEQRES 12 A 405 GLY GLU LEU LEU PRO GLY TYR ALA ILE ILE SER GLU ASP
SEQRES 13 A 405 LYS ALA GLN ASP THR LEU ILE VAL VAL GLY GLY GLY ASP
SEQRES 14 A 405 THR SER ARG GLU ASP LEU PHE TYR MSE LEU GLY TYR SER
SEQRES 15 A 405 GLY TRP GLU HIS ASP TYR ASN VAL LEU MSE VAL ASP LEU
SEQRES 16 A 405 PRO GLY GLN GLY LYS ASN PRO ASN GLN GLY LEU HIS PHE
SEQRES 17 A 405 GLU VAL ASP ALA ARG ALA ALA ILE SER ALA ILE LEU ASP
SEQRES 18 A 405 TRP TYR GLN ALA PRO THR GLU LYS ILE ALA ILE ALA GLY
SEQRES 19 A 405 PHE SER GLY GLY GLY TYR PHE THR ALA GLN ALA VAL GLU
SEQRES 20 A 405 LYS ASP LYS ARG ILE LYS ALA TRP ILE ALA SER THR PRO
SEQRES 21 A 405 ILE TYR ASP VAL ALA GLU VAL PHE ARG ILE SER PHE SER
SEQRES 22 A 405 THR ALA LEU LYS ALA PRO LYS THR ILE LEU LYS TRP GLY
SEQRES 23 A 405 SER LYS LEU VAL THR SER VAL ASN LYS VAL ALA GLU VAL
SEQRES 24 A 405 ASN LEU ASN LYS TYR ALA TRP GLN PHE GLY GLN VAL ASP
SEQRES 25 A 405 PHE ILE THR SER VAL ASN GLU VAL LEU GLU GLN ALA GLN
SEQRES 26 A 405 ILE VAL ASP TYR ASN LYS ILE ASP VAL PRO SER LEU PHE
SEQRES 27 A 405 LEU VAL GLY ALA GLY GLU ASP SER GLU LEU MSE ARG GLN
SEQRES 28 A 405 SER GLN VAL LEU TYR ASP ASN PHE LYS GLN ARG GLY ILE
SEQRES 29 A 405 ASP VAL THR LEU ARG LYS PHE SER SER GLU SER GLY ALA
SEQRES 30 A 405 ASP ALA HIS CYS GLN VAL ASN ASN PHE ARG LEU MSE HIS
SEQRES 31 A 405 TYR GLN VAL PHE GLU TRP LEU ASN HIS ILE PHE LYS LYS
SEQRES 32 A 405 LYS ASP
SEQRES 1 B 405 SER ASN ALA MSE LYS GLU ASN ASN THR ILE LEU LYS ARG
SEQRES 2 B 405 GLN ASP TYR LYS ILE LYS PHE ASN ASN LYS ASP MSE ASP
SEQRES 3 B 405 PHE CYS PHE ASN TRP MSE LEU GLY ILE GLY GLN ILE ILE
SEQRES 4 B 405 GLY MSE SER ALA GLY GLU LEU PHE TYR ILE ALA SER GLY
SEQRES 5 B 405 ILE ARG ASP GLY ASN PRO THR ASP TRP CYS LYS ARG PHE
SEQRES 6 B 405 ASN GLU HIS ALA ASP TYR LEU GLU ASP GLU VAL GLU ARG
SEQRES 7 B 405 VAL LYS LYS VAL GLY TYR ARG ASP LEU ILE SER HIS LEU
SEQRES 8 B 405 TYR PHE SER ALA CYS PHE SER ILE ARG ALA ALA LEU GLN
SEQRES 9 B 405 PHE THR ASP PRO LYS ASP SER GLU PHE MSE GLU ASN PHE
SEQRES 10 B 405 ARG ARG MSE GLU LYS LEU PHE MSE LEU ALA VAL ASP ASN
SEQRES 11 B 405 SER LYS ILE PRO LEU LYS SER ILE GLU VAL PRO PHE GLU
SEQRES 12 B 405 GLY GLU LEU LEU PRO GLY TYR ALA ILE ILE SER GLU ASP
SEQRES 13 B 405 LYS ALA GLN ASP THR LEU ILE VAL VAL GLY GLY GLY ASP
SEQRES 14 B 405 THR SER ARG GLU ASP LEU PHE TYR MSE LEU GLY TYR SER
SEQRES 15 B 405 GLY TRP GLU HIS ASP TYR ASN VAL LEU MSE VAL ASP LEU
SEQRES 16 B 405 PRO GLY GLN GLY LYS ASN PRO ASN GLN GLY LEU HIS PHE
SEQRES 17 B 405 GLU VAL ASP ALA ARG ALA ALA ILE SER ALA ILE LEU ASP
SEQRES 18 B 405 TRP TYR GLN ALA PRO THR GLU LYS ILE ALA ILE ALA GLY
SEQRES 19 B 405 PHE SER GLY GLY GLY TYR PHE THR ALA GLN ALA VAL GLU
SEQRES 20 B 405 LYS ASP LYS ARG ILE LYS ALA TRP ILE ALA SER THR PRO
SEQRES 21 B 405 ILE TYR ASP VAL ALA GLU VAL PHE ARG ILE SER PHE SER
SEQRES 22 B 405 THR ALA LEU LYS ALA PRO LYS THR ILE LEU LYS TRP GLY
SEQRES 23 B 405 SER LYS LEU VAL THR SER VAL ASN LYS VAL ALA GLU VAL
SEQRES 24 B 405 ASN LEU ASN LYS TYR ALA TRP GLN PHE GLY GLN VAL ASP
SEQRES 25 B 405 PHE ILE THR SER VAL ASN GLU VAL LEU GLU GLN ALA GLN
SEQRES 26 B 405 ILE VAL ASP TYR ASN LYS ILE ASP VAL PRO SER LEU PHE
SEQRES 27 B 405 LEU VAL GLY ALA GLY GLU ASP SER GLU LEU MSE ARG GLN
SEQRES 28 B 405 SER GLN VAL LEU TYR ASP ASN PHE LYS GLN ARG GLY ILE
SEQRES 29 B 405 ASP VAL THR LEU ARG LYS PHE SER SER GLU SER GLY ALA
SEQRES 30 B 405 ASP ALA HIS CYS GLN VAL ASN ASN PHE ARG LEU MSE HIS
SEQRES 31 B 405 TYR GLN VAL PHE GLU TRP LEU ASN HIS ILE PHE LYS LYS
SEQRES 32 B 405 LYS ASP
MODRES 3FNB MSE A 22 MET SELENOMETHIONINE
MODRES 3FNB MSE A 29 MET SELENOMETHIONINE
MODRES 3FNB MSE A 38 MET SELENOMETHIONINE
MODRES 3FNB MSE A 111 MET SELENOMETHIONINE
MODRES 3FNB MSE A 117 MET SELENOMETHIONINE
MODRES 3FNB MSE A 122 MET SELENOMETHIONINE
MODRES 3FNB MSE A 175 MET SELENOMETHIONINE
MODRES 3FNB MSE A 189 MET SELENOMETHIONINE
MODRES 3FNB MSE A 346 MET SELENOMETHIONINE
MODRES 3FNB MSE A 386 MET SELENOMETHIONINE
MODRES 3FNB MSE B 22 MET SELENOMETHIONINE
MODRES 3FNB MSE B 29 MET SELENOMETHIONINE
MODRES 3FNB MSE B 38 MET SELENOMETHIONINE
MODRES 3FNB MSE B 111 MET SELENOMETHIONINE
MODRES 3FNB MSE B 117 MET SELENOMETHIONINE
MODRES 3FNB MSE B 122 MET SELENOMETHIONINE
MODRES 3FNB MSE B 175 MET SELENOMETHIONINE
MODRES 3FNB MSE B 189 MET SELENOMETHIONINE
MODRES 3FNB MSE B 346 MET SELENOMETHIONINE
MODRES 3FNB MSE B 386 MET SELENOMETHIONINE
HET MSE A 22 8
HET MSE A 29 8
HET MSE A 38 8
HET MSE A 111 8
HET MSE A 117 8
HET MSE A 122 8
HET MSE A 175 8
HET MSE A 189 8
HET MSE A 346 8
HET MSE A 386 8
HET MSE B 22 8
HET MSE B 29 8
HET MSE B 38 8
HET MSE B 111 8
HET MSE B 117 8
HET MSE B 122 8
HET MSE B 175 8
HET MSE B 189 8
HET MSE B 346 8
HET MSE B 386 8
HET MG A 501 1
HET BME A 403 4
HET PGE A 404 10
HET EDO A 405 4
HET MG B 501 1
HET BME B 403 4
HET PGE B 404 10
HET EDO B 405 4
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 MG 2(MG 2+)
FORMUL 4 BME 2(C2 H6 O S)
FORMUL 5 PGE 2(C6 H14 O4)
FORMUL 6 EDO 2(C2 H6 O2)
FORMUL 11 HOH *251(H2 O)
HELIX 1 1 ASN A 19 ILE A 36 1 18
HELIX 2 2 SER A 39 SER A 48 1 10
HELIX 3 3 ASN A 54 LYS A 78 1 25
HELIX 4 4 TYR A 81 PHE A 102 1 22
HELIX 5 5 SER A 108 ASN A 127 1 20
HELIX 6 6 SER A 168 LEU A 176 1 9
HELIX 7 7 LEU A 176 HIS A 183 1 8
HELIX 8 8 LYS A 197 GLY A 202 5 6
HELIX 9 9 ALA A 209 TYR A 220 1 12
HELIX 10 10 GLY A 234 GLU A 244 1 11
HELIX 11 11 ASP A 260 PHE A 269 1 10
HELIX 12 12 ASN A 291 GLY A 306 1 16
HELIX 13 13 ASP A 309 ALA A 321 1 13
HELIX 14 14 ASP A 325 ILE A 329 5 5
HELIX 15 15 ASP A 342 ARG A 359 1 18
HELIX 16 16 ALA A 376 ASN A 381 5 6
HELIX 17 17 ASN A 382 LYS A 399 1 18
HELIX 18 18 ASN B 19 GLN B 34 1 16
HELIX 19 19 SER B 39 SER B 48 1 10
HELIX 20 20 ASN B 54 LYS B 78 1 25
HELIX 21 21 TYR B 81 PHE B 102 1 22
HELIX 22 22 SER B 108 ASN B 127 1 20
HELIX 23 23 SER B 168 LEU B 176 1 9
HELIX 24 24 LEU B 176 HIS B 183 1 8
HELIX 25 25 LYS B 197 GLY B 202 5 6
HELIX 26 26 ALA B 209 TYR B 220 1 12
HELIX 27 27 GLY B 234 ASP B 246 1 13
HELIX 28 28 ASP B 260 PHE B 269 1 10
HELIX 29 29 ASN B 291 GLY B 306 1 16
HELIX 30 30 ASP B 309 ALA B 321 1 13
HELIX 31 31 ASP B 325 ILE B 329 5 5
HELIX 32 32 ASP B 342 ARG B 359 1 18
HELIX 33 33 ALA B 376 ASN B 381 5 6
HELIX 34 34 ASN B 382 LYS B 399 1 18
SHEET 1 A 8 LYS A 133 PHE A 139 0
SHEET 2 A 8 GLU A 142 ILE A 149 -1 O ALA A 148 N LYS A 133
SHEET 3 A 8 ASN A 186 VAL A 190 -1 O MSE A 189 N TYR A 147
SHEET 4 A 8 THR A 158 VAL A 162 1 N LEU A 159 O ASN A 186
SHEET 5 A 8 ILE A 227 PHE A 232 1 O ALA A 230 N VAL A 162
SHEET 6 A 8 ALA A 251 SER A 255 1 O SER A 255 N GLY A 231
SHEET 7 A 8 SER A 333 GLY A 338 1 O LEU A 334 N TRP A 252
SHEET 8 A 8 VAL A 363 PHE A 368 1 O ARG A 366 N PHE A 335
SHEET 1 B 8 LYS B 133 PHE B 139 0
SHEET 2 B 8 GLU B 142 ILE B 149 -1 O LEU B 144 N VAL B 137
SHEET 3 B 8 ASN B 186 VAL B 190 -1 O VAL B 187 N ILE B 149
SHEET 4 B 8 THR B 158 VAL B 162 1 N VAL B 161 O LEU B 188
SHEET 5 B 8 ILE B 227 PHE B 232 1 O ALA B 228 N THR B 158
SHEET 6 B 8 ALA B 251 SER B 255 1 O SER B 255 N GLY B 231
SHEET 7 B 8 SER B 333 GLY B 338 1 O LEU B 336 N ALA B 254
SHEET 8 B 8 VAL B 363 PHE B 368 1 O THR B 364 N PHE B 335
LINK C ASP A 21 N MSE A 22 1555 1555 1.32
LINK C MSE A 22 N ASP A 23 1555 1555 1.34
LINK C TRP A 28 N MSE A 29 1555 1555 1.33
LINK C MSE A 29 N LEU A 30 1555 1555 1.33
LINK C GLY A 37 N MSE A 38 1555 1555 1.33
LINK C MSE A 38 N SER A 39 1555 1555 1.33
LINK C PHE A 110 N MSE A 111 1555 1555 1.33
LINK C MSE A 111 N GLU A 112 1555 1555 1.33
LINK C ARG A 116 N MSE A 117 1555 1555 1.34
LINK C MSE A 117 N GLU A 118 1555 1555 1.33
LINK C PHE A 121 N MSE A 122 1555 1555 1.33
LINK C MSE A 122 N LEU A 123 1555 1555 1.33
LINK C TYR A 174 N MSE A 175 1555 1555 1.31
LINK C MSE A 175 N LEU A 176 1555 1555 1.31
LINK C LEU A 188 N MSE A 189 1555 1555 1.33
LINK C MSE A 189 N VAL A 190 1555 1555 1.32
LINK C LEU A 345 N MSE A 346 1555 1555 1.33
LINK C MSE A 346 N ARG A 347 1555 1555 1.33
LINK C LEU A 385 N MSE A 386 1555 1555 1.33
LINK C MSE A 386 N HIS A 387 1555 1555 1.33
LINK C ASP B 21 N MSE B 22 1555 1555 1.32
LINK C MSE B 22 N ASP B 23 1555 1555 1.33
LINK C TRP B 28 N MSE B 29 1555 1555 1.33
LINK C MSE B 29 N LEU B 30 1555 1555 1.33
LINK C GLY B 37 N MSE B 38 1555 1555 1.32
LINK C MSE B 38 N SER B 39 1555 1555 1.33
LINK C PHE B 110 N MSE B 111 1555 1555 1.33
LINK C MSE B 111 N GLU B 112 1555 1555 1.33
LINK C ARG B 116 N MSE B 117 1555 1555 1.33
LINK C MSE B 117 N GLU B 118 1555 1555 1.34
LINK C PHE B 121 N MSE B 122 1555 1555 1.33
LINK C MSE B 122 N LEU B 123 1555 1555 1.32
LINK C TYR B 174 N MSE B 175 1555 1555 1.33
LINK C MSE B 175 N LEU B 176 1555 1555 1.33
LINK C LEU B 188 N MSE B 189 1555 1555 1.33
LINK C MSE B 189 N VAL B 190 1555 1555 1.32
LINK C LEU B 345 N MSE B 346 1555 1555 1.32
LINK C MSE B 346 N ARG B 347 1555 1555 1.32
LINK C LEU B 385 N MSE B 386 1555 1555 1.33
LINK C MSE B 386 N HIS B 387 1555 1555 1.33
CISPEP 1 SER A 255 THR A 256 0 -6.34
CISPEP 2 SER B 255 THR B 256 0 -6.41
SITE 1 AC1 5 ARG A 366 LYS A 367 PHE A 368 SER A 369
SITE 2 AC1 5 HOH B 522
SITE 1 AC2 5 ASP A 166 MSE A 175 HIS A 377 CYS A 378
SITE 2 AC2 5 HOH A 500
SITE 1 AC3 2 PHE A 238 HOH A 538
SITE 1 AC4 5 TYR A 45 ILE A 46 SER A 48 GLY A 49
SITE 2 AC4 5 ARG A 61
SITE 1 AC5 5 TYR A 68 HOH A 510 ARG B 366 LYS B 367
SITE 2 AC5 5 SER B 369
SITE 1 AC6 2 HIS B 377 CYS B 378
SITE 1 AC7 3 GLU B 206 PHE B 238 EDO B 405
SITE 1 AC8 2 PGE B 404 HOH B 489
CRYST1 68.832 56.468 99.901 90.00 93.86 90.00 P 1 21 1 4
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 0.014528 0.000000 0.000979 0.00000
SCALE2 0.000000 0.017709 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010033 0.00000
TER 3056 LYS A 399
TER 6092 LYS B 400
MASTER 378 0 28 34 16 0 12 6 6379 2 236 64
END |