4UPD-pdb | HEADER HYDROLASE 16-JUN-14 4UPD
TITLE OPEN CONFORMATION OF O. PICEAE STEROL ESTERASE MUTANT I544W
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROL ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 13-549;
COMPND 5 EC: 3.1.1.13;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: N-ACETYLGLUCOSAMINE GLYCOSYLATIONS IN POSITIONS 362
COMPND 9 AND 380
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPHIOSTOMA PICEAE;
SOURCE 3 ORGANISM_TAXID: 61273;
SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: KM71;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PPIC9
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,M.J.GONZALEZ,
AUTHOR 2 J.A.HERMOSO
REVDAT 1 24-SEP-14 4UPD 0
JRNL AUTH J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,
JRNL AUTH 2 M.J.MARTINEZ,J.A.HERMOSO
JRNL TITL CRYSTAL STRUCTURES OF OPHIOSTOMA PICEAE STEROL ESTERASE:
JRNL TITL 2 STRUCTURAL INSIGHTS INTO ACTIVATION MECHANISM AND PRODUCT
JRNL TITL 3 RELEASE.
JRNL REF J.STRUCT.BIOL. V. 187 215 2014
JRNL REFN ISSN 1047-8477
JRNL PMID 25108239
JRNL DOI 10.1016/J.JSB.2014.07.007
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.400
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.287
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.79
REMARK 3 NUMBER OF REFLECTIONS : 49284
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1988
REMARK 3 R VALUE (WORKING SET) : 0.1962
REMARK 3 FREE R VALUE : 0.2477
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2400
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 58.3040 - 6.1694 1.00 2840 137 0.1995 0.2055
REMARK 3 2 6.1694 - 4.8976 1.00 2782 163 0.1970 0.2437
REMARK 3 3 4.8976 - 4.2787 1.00 2766 139 0.1697 0.1954
REMARK 3 4 4.2787 - 3.8876 1.00 2760 145 0.1762 0.2555
REMARK 3 5 3.8876 - 3.6090 1.00 2776 134 0.1868 0.2489
REMARK 3 6 3.6090 - 3.3963 1.00 2731 153 0.1894 0.2363
REMARK 3 7 3.3963 - 3.2262 1.00 2771 126 0.1918 0.2657
REMARK 3 8 3.2262 - 3.0858 1.00 2785 136 0.2023 0.2445
REMARK 3 9 3.0858 - 2.9670 1.00 2741 150 0.2065 0.2984
REMARK 3 10 2.9670 - 2.8646 1.00 2789 113 0.1956 0.2778
REMARK 3 11 2.8646 - 2.7750 1.00 2697 163 0.2030 0.2808
REMARK 3 12 2.7750 - 2.6957 1.00 2770 141 0.2073 0.2677
REMARK 3 13 2.6957 - 2.6247 1.00 2725 133 0.2143 0.2667
REMARK 3 14 2.6247 - 2.5607 1.00 2778 138 0.2269 0.3030
REMARK 3 15 2.5607 - 2.5025 1.00 2714 145 0.2355 0.3191
REMARK 3 16 2.5025 - 2.4492 1.00 2789 129 0.2383 0.2822
REMARK 3 17 2.4492 - 2.4002 0.97 2670 155 0.2516 0.2935
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) : 0.30
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.13
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 : 0.010 8586
REMARK 3 ANGLE : 1.480 11691
REMARK 3 CHIRALITY : 0.064 1303
REMARK 3 PLANARITY : 0.010 1503
REMARK 3 DIHEDRAL : 15.219 3060
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 1-12 IN CHAIN A AND 1-13
REMARK 3 IN CHAIN B ARE DISORDERED.
REMARK 4
REMARK 4 4UPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUN-14.
REMARK 100 THE PDBE ID CODE IS EBI-60914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49299
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 58.29
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.9
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.8
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.8
REMARK 200 R MERGE FOR SHELL (I) : 0.97
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4BE9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM NITRATE, 0.1 M
REMARK 280 BIS-TRIS PROPANE PH 7.5, 20% PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 82.43000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 82.43000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.07000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 82.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.53500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 82.43000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 70.60500
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 82.43000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.43000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 47.07000
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 82.43000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 70.60500
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 82.43000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 23.53500
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: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.3 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 GLU A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 TYR A 9
REMARK 465 VAL A 10
REMARK 465 GLU A 11
REMARK 465 GLU B 5
REMARK 465 ALA B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 TYR B 9
REMARK 465 VAL B 10
REMARK 465 GLU B 11
REMARK 465 PHE B 12
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CB CYS A 279 SG CYS A 288 1.78
REMARK 500 OD1 ASP A 293 O HOH A 2190 1.91
REMARK 500 O GLY A 306 OG SER A 309 1.91
REMARK 500 ND2 ASN A 362 O5 NAG A 1552 2.02
REMARK 500 CG ASN A 380 C1 NAG A 1553 2.17
REMARK 500 ND2 ASN A 380 O5 NAG A 1553 1.91
REMARK 500 OD2 ASP A 396 OG1 THR A 398 2.03
REMARK 500 O VAL B 15 N GLY B 26 1.89
REMARK 500 O GLY B 31 C PRO B 116 2.17
REMARK 500 O GLY B 31 O PRO B 116 1.30
REMARK 500 CG ASP B 64 OG1 THR B 66 1.81
REMARK 500 OD1 ASP B 64 OG1 THR B 66 1.09
REMARK 500 OD2 ASP B 64 OG1 THR B 66 2.12
REMARK 500 SG CYS B 72 CB CYS B 108 1.97
REMARK 500 OG1 THR B 110 O HOH B 2001 1.96
REMARK 500 OD1 ASN B 141 ND2 ASN B 166 2.03
REMARK 500 O TYR B 143 OH TYR B 474 1.80
REMARK 500 OE1 GLU B 158 CB THR B 494 1.77
REMARK 500 OE1 GLU B 158 CG2 THR B 494 2.08
REMARK 500 O GLY B 171 O HOH B 2011 2.14
REMARK 500 OG SER B 186 O HOH B 2013 2.04
REMARK 500 OD2 ASP B 210 CE LYS B 213 1.92
REMARK 500 NH2 ARG B 246 O VAL B 493 2.12
REMARK 500 SG CYS B 279 CB CYS B 288 1.78
REMARK 500 CG ASP B 284 CB ALA B 287 2.19
REMARK 500 OD1 ASP B 284 CA ALA B 287 2.11
REMARK 500 OD1 ASP B 284 CB ALA B 287 1.31
REMARK 500 C CYS B 288 OG1 THR B 291 2.00
REMARK 500 O CYS B 288 OG1 THR B 291 0.92
REMARK 500 O ALA B 300 OG SER B 303 1.66
REMARK 500 OE2 GLU B 331 NH2 ARG B 548 2.08
REMARK 500 OE1 GLU B 350 OG SER B 453 1.62
REMARK 500 ND2 ASN B 362 C2 NAG B 1551 2.03
REMARK 500 C SER B 365 CD1 ILE B 369 1.80
REMARK 500 O SER B 365 CD1 ILE B 369 1.46
REMARK 500 N THR B 366 CD1 ILE B 369 2.19
REMARK 500 O THR B 366 CG2 VAL B 370 1.99
REMARK 500 OG1 THR B 382 OE1 GLN B 385 2.13
REMARK 500 O PHE B 389 OG1 THR B 392 1.43
REMARK 500 OH TYR B 393 OD2 ASP B 424 1.73
REMARK 500 OD2 ASP B 396 OG1 THR B 398 1.77
REMARK 500 O ASN B 404 OH TYR B 456 2.20
REMARK 500 O ALA B 419 O HOH B 2026 2.15
REMARK 500 O LEU B 435 OG SER B 439 2.16
REMARK 500 O PHE B 464 OG1 THR B 467 2.13
REMARK 500 O TYR B 480 OG SER B 484 1.65
REMARK 500 O SER B 482 CG GLN B 486 1.82
REMARK 500 O HOH A 2004 O HOH A 2006 2.16
REMARK 500 O HOH A 2005 O HOH A 2007 2.19
REMARK 500 O HOH A 2017 O HOH A 2092 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN A 18 NZ LYS A 296 7554 1.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 288 CA CYS A 288 CB 0.082
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 288 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 PRO B 159 C - N - CD ANGL. DEV. = -16.2 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 220 -117.77 61.31
REMARK 500 SER A 252 70.35 61.92
REMARK 500 SER A 254 -94.49 -157.78
REMARK 500 SER A 312 -119.29 58.23
REMARK 500 VAL A 324 -65.81 -124.03
REMARK 500 TYR A 377 -73.39 -106.07
REMARK 500 PHE A 427 -82.01 -121.27
REMARK 500 PHE A 460 -36.59 74.67
REMARK 500 ASN A 479 -167.23 -166.68
REMARK 500 ASN B 16 -36.47 -171.94
REMARK 500 ALA B 117 117.11 113.12
REMARK 500 LYS B 178 -81.48 9.79
REMARK 500 SER B 220 -114.41 57.27
REMARK 500 SER B 254 -95.81 -167.89
REMARK 500 SER B 312 -124.82 57.27
REMARK 500 VAL B 324 -66.41 -124.85
REMARK 500 PHE B 427 -74.95 -121.16
REMARK 500 ASP B 444 -5.10 86.04
REMARK 500 PHE B 460 -47.58 73.98
REMARK 500 ASN B 479 -163.31 -170.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL B 15 ASN B 16 -40.45
REMARK 500 SER B 212 LYS B 213 146.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 16 23.6 L L OUTSIDE RANGE
REMARK 500 HIS B 272 23.6 L L OUTSIDE RANGE
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 7P9 A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7P9 B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1552 BOUND TO ASN A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1553 BOUND TO ASN A 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1551 BOUND TO ASN B 362
DBREF 4UPD A 13 549 UNP Q2TFW1 Q2TFW1_9PEZI 13 549
DBREF 4UPD B 13 549 UNP Q2TFW1 Q2TFW1_9PEZI 13 549
SEQADV 4UPD GLU A 5 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD ALA A 6 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD GLU A 7 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD ALA A 8 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD TYR A 9 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD VAL A 10 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD GLU A 11 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD PHE A 12 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD TRP A 544 UNP Q2TFW1 ILE 544 ENGINEERED MUTATION
SEQADV 4UPD GLU B 5 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD ALA B 6 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD GLU B 7 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD ALA B 8 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD TYR B 9 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD VAL B 10 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD GLU B 11 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD PHE B 12 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4UPD TRP B 544 UNP Q2TFW1 ILE 544 ENGINEERED MUTATION
SEQRES 1 A 545 GLU ALA GLU ALA TYR VAL GLU PHE THR THR VAL ASN VAL
SEQRES 2 A 545 ASN TYR PRO GLU GLY GLU VAL VAL GLY VAL SER VAL LEU
SEQRES 3 A 545 GLY ILE GLU SER PHE ARG GLY VAL PRO PHE ALA GLN PRO
SEQRES 4 A 545 PRO VAL GLY ASN LEU ARG LEU LYS PRO PRO VAL ARG TYR
SEQRES 5 A 545 THR GLU ASN ILE GLY THR LYS ASP THR THR GLY ILE GLY
SEQRES 6 A 545 PRO SER CYS PRO GLN MET TYR LEU SER THR GLY ASN GLY
SEQRES 7 A 545 GLU LEU LEU PHE GLN LEU VAL GLY ASN LEU ILE ASN ILE
SEQRES 8 A 545 PRO LEU PHE GLN THR ALA THR LEU SER SER GLU ASP CYS
SEQRES 9 A 545 LEU THR LEU ASN ILE GLN ARG PRO ALA GLY THR THR SER
SEQRES 10 A 545 ASN SER SER LEU PRO VAL LEU PHE TRP ILE PHE GLY GLY
SEQRES 11 A 545 GLY PHE GLU LEU GLY THR ASN GLN TYR TYR ASP GLY ILE
SEQRES 12 A 545 ASP LEU LEU THR GLU GLY ILE SER LEU GLY GLU PRO PHE
SEQRES 13 A 545 ILE PHE VAL ALA ILE ASN TYR ARG VAL GLY GLY PHE GLY
SEQRES 14 A 545 PHE LEU GLY GLY LYS GLU ILE LYS ALA ASP GLY SER SER
SEQRES 15 A 545 ASN LEU GLY LEU LEU ASP GLN ARG ILE ALA LEU GLU TRP
SEQRES 16 A 545 VAL ALA ASP ASN ILE ALA SER PHE GLY GLY ASP PRO SER
SEQRES 17 A 545 LYS VAL THR ILE TRP GLY GLU SER ALA GLY SER ILE SER
SEQRES 18 A 545 VAL PHE ASP GLN MET ALA LEU TYR GLY GLY ASN ASN LYS
SEQRES 19 A 545 TYR LYS GLY LYS ALA LEU PHE ARG GLY GLY ILE MET ASN
SEQRES 20 A 545 SER GLY SER VAL VAL PRO ALA ALA PRO VAL ASP GLY VAL
SEQRES 21 A 545 LYS ALA GLN ALA ILE TYR ASP HIS VAL VAL SER GLU ALA
SEQRES 22 A 545 GLY CYS ALA GLY THR SER ASP THR LEU ALA CYS LEU ARG
SEQRES 23 A 545 THR VAL ASP TYR THR LYS PHE LEU THR ALA VAL ASN SER
SEQRES 24 A 545 VAL PRO GLY ILE VAL SER TYR SER SER ILE ALA LEU SER
SEQRES 25 A 545 TYR LEU PRO ARG PRO ASP GLY VAL VAL LEU ILE ASP SER
SEQRES 26 A 545 PRO GLU GLU ILE VAL LYS ASN LYS GLN TYR ALA ALA VAL
SEQRES 27 A 545 PRO MET ILE ILE GLY ASP GLN GLU ASP GLU GLY THR LEU
SEQRES 28 A 545 PHE ALA VAL LEU PRO ASN ASN ILE THR SER THR ALA LYS
SEQRES 29 A 545 ILE VAL GLN TYR PHE GLN ASP LEU TYR PHE TYR ASN ALA
SEQRES 30 A 545 THR LYS GLU GLN LEU THR ALA PHE VAL ASN THR TYR PRO
SEQRES 31 A 545 THR ASP ILE THR ALA GLY SER PRO PHE ASN THR GLY ILE
SEQRES 32 A 545 PHE ASN GLU LEU TYR PRO GLY PHE LYS ARG LEU ALA ALA
SEQRES 33 A 545 ILE LEU GLY ASP MET THR PHE THR LEU ALA ARG ARG ALA
SEQRES 34 A 545 PHE LEU GLN LEU CYS SER GLU VAL ASN PRO ASP VAL PRO
SEQRES 35 A 545 SER TRP SER TYR LEU ALA SER TYR ASP TYR GLY PHE PRO
SEQRES 36 A 545 PHE LEU GLY THR PHE HIS ALA THR ASP ILE LEU GLN VAL
SEQRES 37 A 545 PHE TYR GLY VAL LEU PRO ASN TYR ALA SER GLY SER ILE
SEQRES 38 A 545 GLN LYS TYR TYR ILE ASN PHE VAL THR THR GLY ASP PRO
SEQRES 39 A 545 ASN LYS GLY ALA ALA VAL ASP ILE GLN TRP PRO GLN TRP
SEQRES 40 A 545 SER ALA LYS LYS ASN ILE LEU GLN ILE TYR ALA THR LYS
SEQRES 41 A 545 ALA VAL ILE VAL ALA ASP ASN PHE ARG ALA LYS SER TYR
SEQRES 42 A 545 GLU TYR LEU TYR ASN ASN TRP GLY ILE PHE ARG ILE
SEQRES 1 B 545 GLU ALA GLU ALA TYR VAL GLU PHE THR THR VAL ASN VAL
SEQRES 2 B 545 ASN TYR PRO GLU GLY GLU VAL VAL GLY VAL SER VAL LEU
SEQRES 3 B 545 GLY ILE GLU SER PHE ARG GLY VAL PRO PHE ALA GLN PRO
SEQRES 4 B 545 PRO VAL GLY ASN LEU ARG LEU LYS PRO PRO VAL ARG TYR
SEQRES 5 B 545 THR GLU ASN ILE GLY THR LYS ASP THR THR GLY ILE GLY
SEQRES 6 B 545 PRO SER CYS PRO GLN MET TYR LEU SER THR GLY ASN GLY
SEQRES 7 B 545 GLU LEU LEU PHE GLN LEU VAL GLY ASN LEU ILE ASN ILE
SEQRES 8 B 545 PRO LEU PHE GLN THR ALA THR LEU SER SER GLU ASP CYS
SEQRES 9 B 545 LEU THR LEU ASN ILE GLN ARG PRO ALA GLY THR THR SER
SEQRES 10 B 545 ASN SER SER LEU PRO VAL LEU PHE TRP ILE PHE GLY GLY
SEQRES 11 B 545 GLY PHE GLU LEU GLY THR ASN GLN TYR TYR ASP GLY ILE
SEQRES 12 B 545 ASP LEU LEU THR GLU GLY ILE SER LEU GLY GLU PRO PHE
SEQRES 13 B 545 ILE PHE VAL ALA ILE ASN TYR ARG VAL GLY GLY PHE GLY
SEQRES 14 B 545 PHE LEU GLY GLY LYS GLU ILE LYS ALA ASP GLY SER SER
SEQRES 15 B 545 ASN LEU GLY LEU LEU ASP GLN ARG ILE ALA LEU GLU TRP
SEQRES 16 B 545 VAL ALA ASP ASN ILE ALA SER PHE GLY GLY ASP PRO SER
SEQRES 17 B 545 LYS VAL THR ILE TRP GLY GLU SER ALA GLY SER ILE SER
SEQRES 18 B 545 VAL PHE ASP GLN MET ALA LEU TYR GLY GLY ASN ASN LYS
SEQRES 19 B 545 TYR LYS GLY LYS ALA LEU PHE ARG GLY GLY ILE MET ASN
SEQRES 20 B 545 SER GLY SER VAL VAL PRO ALA ALA PRO VAL ASP GLY VAL
SEQRES 21 B 545 LYS ALA GLN ALA ILE TYR ASP HIS VAL VAL SER GLU ALA
SEQRES 22 B 545 GLY CYS ALA GLY THR SER ASP THR LEU ALA CYS LEU ARG
SEQRES 23 B 545 THR VAL ASP TYR THR LYS PHE LEU THR ALA VAL ASN SER
SEQRES 24 B 545 VAL PRO GLY ILE VAL SER TYR SER SER ILE ALA LEU SER
SEQRES 25 B 545 TYR LEU PRO ARG PRO ASP GLY VAL VAL LEU ILE ASP SER
SEQRES 26 B 545 PRO GLU GLU ILE VAL LYS ASN LYS GLN TYR ALA ALA VAL
SEQRES 27 B 545 PRO MET ILE ILE GLY ASP GLN GLU ASP GLU GLY THR LEU
SEQRES 28 B 545 PHE ALA VAL LEU PRO ASN ASN ILE THR SER THR ALA LYS
SEQRES 29 B 545 ILE VAL GLN TYR PHE GLN ASP LEU TYR PHE TYR ASN ALA
SEQRES 30 B 545 THR LYS GLU GLN LEU THR ALA PHE VAL ASN THR TYR PRO
SEQRES 31 B 545 THR ASP ILE THR ALA GLY SER PRO PHE ASN THR GLY ILE
SEQRES 32 B 545 PHE ASN GLU LEU TYR PRO GLY PHE LYS ARG LEU ALA ALA
SEQRES 33 B 545 ILE LEU GLY ASP MET THR PHE THR LEU ALA ARG ARG ALA
SEQRES 34 B 545 PHE LEU GLN LEU CYS SER GLU VAL ASN PRO ASP VAL PRO
SEQRES 35 B 545 SER TRP SER TYR LEU ALA SER TYR ASP TYR GLY PHE PRO
SEQRES 36 B 545 PHE LEU GLY THR PHE HIS ALA THR ASP ILE LEU GLN VAL
SEQRES 37 B 545 PHE TYR GLY VAL LEU PRO ASN TYR ALA SER GLY SER ILE
SEQRES 38 B 545 GLN LYS TYR TYR ILE ASN PHE VAL THR THR GLY ASP PRO
SEQRES 39 B 545 ASN LYS GLY ALA ALA VAL ASP ILE GLN TRP PRO GLN TRP
SEQRES 40 B 545 SER ALA LYS LYS ASN ILE LEU GLN ILE TYR ALA THR LYS
SEQRES 41 B 545 ALA VAL ILE VAL ALA ASP ASN PHE ARG ALA LYS SER TYR
SEQRES 42 B 545 GLU TYR LEU TYR ASN ASN TRP GLY ILE PHE ARG ILE
HET 7P9 A1550 28
HET 7P9 B1550 28
HET PGE A1551 10
HET NAG A1552 14
HET NAG A1553 14
HET NAG B1551 14
HETNAM 7P9 [(2R)-2-HEPTANOYLOXY-3-PHOSPHONOOXY-PROPYL]
HETNAM 2 7P9 NONANOATE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 7P9 2(C19 H37 O8 P)
FORMUL 4 PGE C6 H14 O4
FORMUL 5 NAG 3(C8 H15 N O6)
FORMUL 6 HOH *335(H2 O)
HELIX 1 1 VAL A 45 ARG A 49 5 5
HELIX 2 2 GLU A 83 ASN A 94 1 12
HELIX 3 3 ILE A 95 THR A 102 1 8
HELIX 4 4 THR A 140 TYR A 144 5 5
HELIX 5 5 GLY A 146 LEU A 156 1 11
HELIX 6 6 VAL A 169 GLY A 173 5 5
HELIX 7 7 GLY A 177 GLY A 184 1 8
HELIX 8 8 ASN A 187 ILE A 204 1 18
HELIX 9 9 ALA A 205 PHE A 207 5 3
HELIX 10 10 SER A 220 ASN A 236 1 17
HELIX 11 11 GLY A 263 ALA A 277 1 15
HELIX 12 12 ASP A 284 VAL A 292 1 9
HELIX 13 13 ASP A 293 ASN A 302 1 10
HELIX 14 14 SER A 329 ASN A 336 1 8
HELIX 15 15 THR A 354 VAL A 358 5 5
HELIX 16 16 SER A 365 TYR A 377 1 13
HELIX 17 17 THR A 382 ASN A 391 1 10
HELIX 18 18 ASP A 396 GLY A 400 5 5
HELIX 19 19 GLY A 414 PHE A 427 1 14
HELIX 20 20 PHE A 427 ASN A 442 1 16
HELIX 21 21 ALA A 466 VAL A 472 1 7
HELIX 22 22 ASN A 479 GLY A 496 1 18
HELIX 23 23 GLN A 510 LYS A 515 1 6
HELIX 24 24 ARG A 533 ASN A 543 1 11
HELIX 25 25 TRP A 544 ARG A 548 5 5
HELIX 26 26 VAL B 45 ARG B 49 5 5
HELIX 27 27 GLU B 83 ASN B 94 1 12
HELIX 28 28 ILE B 95 THR B 102 1 8
HELIX 29 29 GLY B 146 LEU B 156 1 11
HELIX 30 30 VAL B 169 LEU B 175 1 7
HELIX 31 31 GLY B 177 ASP B 183 1 7
HELIX 32 32 ASN B 187 ILE B 204 1 18
HELIX 33 33 ALA B 205 PHE B 207 5 3
HELIX 34 34 SER B 220 ASN B 236 1 17
HELIX 35 35 GLY B 263 GLY B 278 1 16
HELIX 36 36 ASP B 284 ARG B 290 1 7
HELIX 37 37 ASP B 293 ASN B 302 1 10
HELIX 38 38 SER B 329 ASN B 336 1 8
HELIX 39 39 GLY B 353 VAL B 358 1 6
HELIX 40 40 SER B 365 TYR B 377 1 13
HELIX 41 41 THR B 382 THR B 392 1 11
HELIX 42 42 ASP B 396 GLY B 400 5 5
HELIX 43 43 GLY B 414 PHE B 427 1 14
HELIX 44 44 PHE B 427 ASN B 442 1 16
HELIX 45 45 ALA B 466 VAL B 472 1 7
HELIX 46 46 ASN B 479 GLY B 496 1 18
HELIX 47 47 GLN B 510 LYS B 515 1 6
HELIX 48 48 ARG B 533 ASN B 543 1 11
HELIX 49 49 TRP B 544 ARG B 548 5 5
SHEET 1 AA 2 THR A 13 TYR A 19 0
SHEET 2 AA 2 GLY A 22 VAL A 29 -1 O GLY A 22 N TYR A 19
SHEET 1 AB 2 THR A 62 ASP A 64 0
SHEET 2 AB 2 GLY A 22 VAL A 29 1 O GLU A 23 N LYS A 63
SHEET 1 AC12 ALA A 525 ALA A 529 0
SHEET 2 AC12 ASN A 516 ILE A 520 -1 O ILE A 517 N VAL A 528
SHEET 3 AC12 SER A 447 ALA A 452 1 O SER A 449 N LEU A 518
SHEET 4 AC12 MET A 344 GLN A 349 1 O MET A 344 N TRP A 448
SHEET 5 AC12 GLY A 247 ASN A 251 1 O GLY A 248 N ILE A 345
SHEET 6 AC12 GLY A 209 GLU A 219 1 O ILE A 216 N ILE A 249
SHEET 7 AC12 LEU A 125 ILE A 131 1 O LEU A 125 N ASP A 210
SHEET 8 AC12 ILE A 161 ILE A 165 1 O ILE A 161 N LEU A 128
SHEET 9 AC12 THR A 110 PRO A 116 -1 O ASN A 112 N ALA A 164
SHEET 10 AC12 ILE A 32 PRO A 39 -1 O GLU A 33 N ARG A 115
SHEET 11 AC12 GLY A 22 VAL A 29 -1 O VAL A 27 N SER A 34
SHEET 12 AC12 THR A 62 ASP A 64 1 O LYS A 63 N VAL A 25
SHEET 1 AD12 ALA A 525 ALA A 529 0
SHEET 2 AD12 ASN A 516 ILE A 520 -1 O ILE A 517 N VAL A 528
SHEET 3 AD12 SER A 447 ALA A 452 1 O SER A 449 N LEU A 518
SHEET 4 AD12 MET A 344 GLN A 349 1 O MET A 344 N TRP A 448
SHEET 5 AD12 GLY A 247 ASN A 251 1 O GLY A 248 N ILE A 345
SHEET 6 AD12 GLY A 209 GLU A 219 1 O ILE A 216 N ILE A 249
SHEET 7 AD12 LEU A 125 ILE A 131 1 O LEU A 125 N ASP A 210
SHEET 8 AD12 ILE A 161 ILE A 165 1 O ILE A 161 N LEU A 128
SHEET 9 AD12 THR A 110 PRO A 116 -1 O ASN A 112 N ALA A 164
SHEET 10 AD12 ILE A 32 PRO A 39 -1 O GLU A 33 N ARG A 115
SHEET 11 AD12 GLY A 22 VAL A 29 -1 O VAL A 27 N SER A 34
SHEET 12 AD12 THR A 13 TYR A 19 -1 O THR A 13 N SER A 28
SHEET 1 AE 2 LYS A 238 TYR A 239 0
SHEET 2 AE 2 LYS A 242 ALA A 243 -1 O LYS A 242 N TYR A 239
SHEET 1 BA 2 GLY B 22 VAL B 25 0
SHEET 2 BA 2 GLY B 61 ASP B 64 1 O GLY B 61 N GLU B 23
SHEET 1 BB11 VAL B 27 VAL B 29 0
SHEET 2 BB11 ILE B 32 PRO B 39 -1 O ILE B 32 N VAL B 29
SHEET 3 BB11 THR B 110 ARG B 115 -1 O LEU B 111 N VAL B 38
SHEET 4 BB11 ILE B 161 ILE B 165 -1 O PHE B 162 N GLN B 114
SHEET 5 BB11 LEU B 125 ILE B 131 1 O PRO B 126 N ILE B 161
SHEET 6 BB11 GLY B 209 GLU B 219 1 N ASP B 210 O LEU B 125
SHEET 7 BB11 GLY B 247 ASN B 251 1 O GLY B 247 N ILE B 216
SHEET 8 BB11 MET B 344 GLN B 349 1 O ILE B 345 N MET B 250
SHEET 9 BB11 SER B 447 ALA B 452 1 O TRP B 448 N ILE B 346
SHEET 10 BB11 ASN B 516 ILE B 520 1 O LEU B 518 N LEU B 451
SHEET 11 BB11 ALA B 525 ALA B 529 -1 O VAL B 526 N GLN B 519
SHEET 1 BC 2 LYS B 238 TYR B 239 0
SHEET 2 BC 2 LYS B 242 ALA B 243 -1 O LYS B 242 N TYR B 239
LINK ND2 ASN A 362 C1 NAG A1552 1555 1555 1.53
LINK ND2 ASN A 380 C1 NAG A1553 1555 1555 1.08
LINK ND2 ASN B 362 C1 NAG B1551 1555 1555 1.25
CISPEP 1 SER A 401 PRO A 402 0 12.12
CISPEP 2 VAL A 476 LEU A 477 0 -6.75
CISPEP 3 SER B 401 PRO B 402 0 10.04
CISPEP 4 VAL B 476 LEU B 477 0 -12.92
SITE 1 AC1 9 ASP A 455 PHE A 458 GLN A 471 VAL A 476
SITE 2 AC1 9 LEU A 477 ASN A 479 HOH A2256 HOH A2257
SITE 3 AC1 9 HOH A2285
SITE 1 AC2 6 ASP B 455 GLN B 471 VAL B 476 LEU B 477
SITE 2 AC2 6 ASN B 479 HOH B2040
SITE 1 AC3 4 SER A 220 ILE A 307 THR A 426 HIS A 465
SITE 1 AC4 3 TYR A 310 ASN A 362 ILE A 363
SITE 1 AC5 6 ALA A 259 ASN A 380 GLU A 384 ARG A 548
SITE 2 AC5 6 HOH A2283 HOH A2286
SITE 1 AC6 2 TYR B 310 ASN B 362
CRYST1 164.860 164.860 94.140 90.00 90.00 90.00 I 41 16
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 0.006066 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006066 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010622 0.00000
TER 4138 ILE A 549
TER 8265 ILE B 549
MASTER 461 0 6 49 45 0 10 6 8706 2 111 84
END
|