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HEADER SUGAR BINDING PROTEIN 14-MAY-19 6OYC
TITLE GLYCOSYLATION ASSOCIATE PROTEIN (GAP123) COMPLEX FROM STREPTOCOCCUS
TITLE 2 AGALACTIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSYLATION ASSOCIATE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GLYCOSYLATION ASSOCIATE PROTEIN 2;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: GLYCOSYLATION ASSOCIATE PROTEIN 3;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE SEROTYPE V (STRAIN
SOURCE 3 ATCC BAA-611 / 2603 V/R);
SOURCE 4 ORGANISM_TAXID: 208435;
SOURCE 5 STRAIN: ATCC BAA-611 / 2603 V/R;
SOURCE 6 GENE: SAG1452;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE SEROTYPE V (STRAIN
SOURCE 11 ATCC BAA-611 / 2603 V/R);
SOURCE 12 ORGANISM_TAXID: 208435;
SOURCE 13 STRAIN: ATCC BAA-611 / 2603 V/R;
SOURCE 14 GENE: SAG1451;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE SEROTYPE V (STRAIN
SOURCE 19 ATCC BAA-611 / 2603 V/R);
SOURCE 20 ORGANISM_TAXID: 208435;
SOURCE 21 STRAIN: ATCC BAA-611 / 2603 V/R;
SOURCE 22 GENE: SAG1450;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS GLYCOSYLATION, SECRETION, LECTIN, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,H.WU
REVDAT 1 20-MAY-20 6OYC 0
JRNL AUTH H.ZHANG,F.ZHU,H.WU
JRNL TITL GLYCOSYLATION ASSOCIATE PROTEIN (GAP123) COMPLEX FROM
JRNL TITL 2 STREPTOCOCCUS AGALACTIAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3051: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 72660
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.750
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 49.2829 - 5.6647 0.99 5306 149 0.1824 0.1725
REMARK 3 2 5.6647 - 4.4972 1.00 5141 148 0.1557 0.1857
REMARK 3 3 4.4972 - 3.9290 1.00 5134 142 0.1495 0.2008
REMARK 3 4 3.9290 - 3.5699 1.00 5055 143 0.1696 0.2283
REMARK 3 5 3.5699 - 3.3141 1.00 5078 141 0.1848 0.2572
REMARK 3 6 3.3141 - 3.1187 1.00 5020 145 0.1956 0.2635
REMARK 3 7 3.1187 - 2.9625 1.00 5062 146 0.1986 0.2567
REMARK 3 8 2.9625 - 2.8336 1.00 5031 136 0.2055 0.2567
REMARK 3 9 2.8336 - 2.7245 1.00 5018 139 0.2008 0.2564
REMARK 3 10 2.7245 - 2.6305 1.00 4978 148 0.1991 0.2773
REMARK 3 11 2.6305 - 2.5483 1.00 5013 143 0.2048 0.2692
REMARK 3 12 2.5483 - 2.4754 0.99 4958 144 0.2089 0.2968
REMARK 3 13 2.4754 - 2.4103 0.99 4948 134 0.2174 0.2801
REMARK 3 14 2.4103 - 2.3515 0.98 4918 142 0.2294 0.2848
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.210
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 : 0.008 11159
REMARK 3 ANGLE : 0.928 15069
REMARK 3 CHIRALITY : 0.054 1620
REMARK 3 PLANARITY : 0.005 1921
REMARK 3 DIHEDRAL : 3.767 6605
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: NULL
REMARK 4
REMARK 4 6OYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1000240647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-17
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 : 22-ID
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
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72701
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 49.272
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 6E2I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 5% PEG 400, 2M
REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 51.50450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.16050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.50450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.16050
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 552 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 386
REMARK 465 ASP A 387
REMARK 465 ASP A 388
REMARK 465 ALA A 389
REMARK 465 ASN A 390
REMARK 465 GLN A 391
REMARK 465 VAL A 392
REMARK 465 LEU A 393
REMARK 465 MET A 394
REMARK 465 GLN A 395
REMARK 465 SER A 396
REMARK 465 ASP A 397
REMARK 465 GLU A 398
REMARK 465 VAL A 399
REMARK 465 GLU A 400
REMARK 465 LYS A 401
REMARK 465 MET B 1
REMARK 465 GLU B 519
REMARK 465 MET C 1
REMARK 465 ASP C 143
REMARK 465 SER C 144
REMARK 465 VAL C 145
REMARK 465 ILE C 146
REMARK 465 GLN C 147
REMARK 465 GLU C 148
REMARK 465 LYS C 149
REMARK 465 LEU C 319
REMARK 465 LEU C 320
REMARK 465 LYS C 321
REMARK 465 LYS C 322
REMARK 465 GLN C 323
REMARK 465 ASP C 324
REMARK 465 ASP C 325
REMARK 465 ASN C 326
REMARK 465 TYR C 327
REMARK 465 ASP C 328
REMARK 465 SER C 329
REMARK 465 LEU C 330
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 LYS B 459 CG CD CE NZ
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 TRP A 8 48.36 -108.92
REMARK 500 ARG A 13 88.32 -163.54
REMARK 500 PHE A 24 43.64 -147.95
REMARK 500 ASN A 85 74.19 -100.16
REMARK 500 PHE A 109 -33.15 -133.16
REMARK 500 ALA A 166 -61.78 -109.20
REMARK 500 ASN A 245 34.37 -99.91
REMARK 500 PHE A 382 57.96 -116.30
REMARK 500 ARG A 461 15.54 59.41
REMARK 500 TYR B 84 -0.03 64.55
REMARK 500 ASP B 213 36.73 -166.41
REMARK 500 LYS B 223 -104.72 29.88
REMARK 500 PHE B 269 -75.66 65.42
REMARK 500 VAL B 291 -117.20 53.42
REMARK 500 LEU B 331 -136.28 61.48
REMARK 500 SER B 371 -104.51 44.65
REMARK 500 LYS B 393 63.54 60.58
REMARK 500 GLU B 408 51.54 -94.47
REMARK 500 ASP B 411 90.57 -164.13
REMARK 500 ASN B 460 47.78 -108.20
REMARK 500 PHE B 475 -71.12 -113.53
REMARK 500 ARG B 476 -47.92 63.31
REMARK 500 LYS B 478 87.63 -66.42
REMARK 500 ASP C 79 -74.08 -81.64
REMARK 500 LYS C 105 -91.36 -96.75
REMARK 500 ALA C 126 64.34 -115.87
REMARK 500 SER C 152 -168.40 -128.84
REMARK 500 TYR C 176 -82.02 -120.34
REMARK 500 LYS C 179 78.62 -155.38
REMARK 500 ILE C 180 -40.71 55.03
REMARK 500 GLU C 181 38.23 -82.65
REMARK 500 ILE C 183 28.47 47.65
REMARK 500 SER C 184 2.61 80.74
REMARK 500 LEU C 186 -103.01 -118.04
REMARK 500 GLN C 187 14.35 -142.44
REMARK 500 PHE C 219 66.93 -113.80
REMARK 500 GLU C 312 0.89 -67.53
REMARK 500 TYR C 316 1.97 -61.54
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 870 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 871 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 872 DISTANCE = 7.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 403
DBREF 6OYC A 1 514 UNP Q8DYM4 Q8DYM4_STRA5 1 514
DBREF 6OYC B 26 519 UNP Q8DYM5 Q8DYM5_STRA5 1 494
DBREF 6OYC C 1 330 UNP Q8DYM6 Q8DYM6_STRA5 1 330
SEQADV 6OYC MET B 1 UNP Q8DYM5 INITIATING METHIONINE
SEQADV 6OYC SER B 2 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC LYS B 3 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ILE B 4 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC LYS B 5 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC LEU B 6 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC THR B 7 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ILE B 8 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC LEU B 9 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC GLN B 10 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC VAL B 11 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC GLY B 12 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC GLU B 13 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC GLU B 14 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ASN B 15 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC TRP B 16 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ALA B 17 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC THR B 18 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC LYS B 19 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC GLU B 20 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ASN B 21 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ILE B 22 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC PRO B 23 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ASN B 24 UNP Q8DYM5 EXPRESSION TAG
SEQADV 6OYC ASN B 25 UNP Q8DYM5 EXPRESSION TAG
SEQRES 1 A 514 MET PHE HIS PHE ILE PRO SER TRP TYR ASN GLU ASN ARG
SEQRES 2 A 514 THR TRP TYR ASP ASN ASN TYR LEU TRP TYR PHE LYS PRO
SEQRES 3 A 514 THR ASN VAL GLY PHE ASP ASP THR ILE ASN GLN MET LYS
SEQRES 4 A 514 MET PHE ASP TYR ALA GLY LYS GLU SER ARG LEU VAL VAL
SEQRES 5 A 514 LEU ASN TYR MET PRO ASN LEU ARG TYR TYR LEU HIS ARG
SEQRES 6 A 514 TYR ASP LEU LEU GLU SER GLY TYR TYR SER VAL PHE ASP
SEQRES 7 A 514 ASP ILE GLN GLU ILE GLY ASN VAL ARG GLN GLN MET ILE
SEQRES 8 A 514 ASP PHE ARG GLN LEU ASN TRP PRO GLU GLY VAL ASP PHE
SEQRES 9 A 514 THR TYR THR PRO PHE ILE VAL LEU VAL LYS LYS SER GLY
SEQRES 10 A 514 ASP LEU ILE ALA LYS VAL GLN PHE GLY GLU GLU GLY ASN
SEQRES 11 A 514 LEU THR HIS ILE ASP TYR PHE ALA ASN GLU GLN ILE ALA
SEQRES 12 A 514 LYS LYS TYR LEU PHE ASP ASP ARG GLY PHE LEU SER SER
SEQRES 13 A 514 ILE LEU TYR TYR ASP ASN GLY GLY GLU ALA TYR GLN ASP
SEQRES 14 A 514 TYR LEU ALA PRO SER GLY GLU ARG ILE MET ARG GLU TYR
SEQRES 15 A 514 LEU ARG GLU GLY ASP HIS HIS VAL GLU ILE ASN PRO LYS
SEQRES 16 A 514 LYS ALA ILE HIS PHE LEU LYS LEU SER TYR SER ASP ILE
SEQRES 17 A 514 GLU GLU LEU ILE ARG GLU LYS TYR LEU THR TYR LEU HIS
SEQRES 18 A 514 LYS GLU VAL SER LYS SER ASP THR ILE ILE VAL SER PHE
SEQRES 19 A 514 ASN GLN VAL HIS ASN ALA PHE ILE VAL GLY ASN THR SER
SEQRES 20 A 514 LYS GLY ASN LEU ILE LEU SER VAL PHE SER GLU ARG ASN
SEQRES 21 A 514 ASN ALA HIS ASN VAL LEU GLU ASP TYR SER SER LEU SER
SEQRES 22 A 514 ARG ALA ASP ALA ILE ILE CYS ASP ARG LEU ASP ILE ALA
SEQRES 23 A 514 ALA GLN LEU LYS GLU LYS ILE ASP LYS PRO VAL VAL HIS
SEQRES 24 A 514 VAL SER PRO PHE ASP THR ARG LEU ALA LEU GLY LYS SER
SEQRES 25 A 514 ASN GLN VAL ARG ASP LEU GLU ILE TYR PHE VAL VAL ASP
SEQRES 26 A 514 ARG LEU SER HIS LYS GLU LEU GLN LYS SER LEU THR SER
SEQRES 27 A 514 LEU TYR LYS VAL MET LEU LYS ASN ASN ASP ILE LYS VAL
SEQRES 28 A 514 THR PHE VAL SER TYR GLU ARG GLU PHE GLU SER ARG GLN
SEQRES 29 A 514 LEU THR TYR ASP TYR LEU LYS GLU ALA THR LYS VAL PHE
SEQRES 30 A 514 ASP GLN LYS PHE PHE SER LEU SER ASP ASP ASP ALA ASN
SEQRES 31 A 514 GLN VAL LEU MET GLN SER ASP GLU VAL GLU LYS GLU LYS
SEQRES 32 A 514 THR ARG LEU SER PHE THR HIS PRO LEU SER GLU THR ASP
SEQRES 33 A 514 ILE ILE ASN ARG LEU GLU TYR VAL ARG LEU ILE ILE ASP
SEQRES 34 A 514 ILE SER LYS ILE PRO ASP LEU TYR THR GLN ILE ALA GLY
SEQRES 35 A 514 ILE SER SER GLY ILE PRO GLN ILE ASN THR ILE LEU THR
SEQRES 36 A 514 GLU PHE VAL GLU HIS ARG LYS ASN GLY TYR ILE ILE GLU
SEQRES 37 A 514 GLU ILE GLN GLU LEU GLU LYS ALA ILE PRO TYR TYR CYS
SEQRES 38 A 514 GLU GLN LEU THR ASN TRP ASN ARG SER LEU ILE TYR SER
SEQRES 39 A 514 ILE ASP LYS ILE ASN ASP TYR THR GLY GLY GLN LEU VAL
SEQRES 40 A 514 GLU ARG ILE ILE ASN SER TYR
SEQRES 1 B 519 MET SER LYS ILE LYS LEU THR ILE LEU GLN VAL GLY GLU
SEQRES 2 B 519 GLU ASN TRP ALA THR LYS GLU ASN ILE PRO ASN ASN MET
SEQRES 3 B 519 GLU TRP LEU PHE ILE LYS PRO ASP GLN ILE SER ASP PHE
SEQRES 4 B 519 VAL THR THR GLU ASN ASN TYR LEU THR SER SER LYS LEU
SEQRES 5 B 519 LEU GLN LYS LEU PRO ARG LYS ILE SER ALA LEU LEU LEU
SEQRES 6 B 519 THR GLU GLN THR TYR GLY PRO GLU LEU SER SER LEU SER
SEQRES 7 B 519 SER PHE PHE GLU VAL TYR GLU VAL PHE TYR PRO LYS ASP
SEQRES 8 B 519 LYS HIS ALA THR GLY ILE THR GLU GLU PHE LEU ARG SER
SEQRES 9 B 519 LYS MET ALA GLN ARG TYR ASP SER SER SER PRO ASP GLN
SEQRES 10 B 519 LEU ILE ARG GLN PHE TYR LYS GLY LEU PHE ILE GLY GLN
SEQRES 11 B 519 TYR GLY GLU LYS LEU GLN VAL SER GLN ILE GLN ILE ARG
SEQRES 12 B 519 ASN ASP PHE GLU GLY VAL VAL ASN TYR GLN GLY ASN ASN
SEQRES 13 B 519 TYR LEU GLU LEU GLU GLY GLN PHE GLY GLU ASN TYR SER
SEQRES 14 B 519 PHE LEU LEU ASN PHE ALA TYR ASN ILE PRO PHE SER SER
SEQRES 15 B 519 ASP PHE TYR ASN GLU LEU PHE LEU GLU HIS ILE ILE GLU
SEQRES 16 B 519 GLY ASP ILE ASP ILE ARG LEU VAL ILE SER LEU ILE VAL
SEQRES 17 B 519 ASP GLY SER VAL ASP ASP ILE ALA LYS GLU TRP TYR PHE
SEQRES 18 B 519 GLU LYS GLU ASP LEU ASN GLN LEU ILE SER LEU GLU SER
SEQRES 19 B 519 ASP ILE SER GLY SER LEU ALA VAL LYS LEU PHE ALA LYS
SEQRES 20 B 519 GLY LYS GLY ILE VAL LYS LEU GLY PRO LEU HIS ARG ARG
SEQRES 21 B 519 ASN GLY ARG GLY GLY LEU GLY THR PHE LEU LEU GLY GLY
SEQRES 22 B 519 GLU ARG HIS ILE ASP ALA ILE GLY HIS GLU PHE MET THR
SEQRES 23 B 519 TYR PHE ASP PRO VAL ASP PHE LYS PRO PRO LEU THR VAL
SEQRES 24 B 519 TYR PHE SER GLY PHE ARG SER ALA GLU GLY PHE GLU GLY
SEQRES 25 B 519 PHE TRP MET MET LYS SER MET LYS THR PRO PHE MET LEU
SEQRES 26 B 519 ILE CYS ASP PRO ARG LEU GLN GLY GLY ALA PHE TYR ILE
SEQRES 27 B 519 GLY SER LYS GLU TYR GLU GLN LYS ILE VAL ASP ALA ILE
SEQRES 28 B 519 GLN GLU LYS LEU ALA PHE LEU ASN PHE SER SER ASP GLN
SEQRES 29 B 519 LEU ILE LEU SER GLY LEU SER MET GLY THR TYR GLY ALA
SEQRES 30 B 519 THR TYR HIS GLY ALA LYS LEU ASN PRO HIS ALA ILE ILE
SEQRES 31 B 519 ILE GLY LYS PRO ILE PHE ASN LEU GLY THR VAL ALA GLN
SEQRES 32 B 519 ARG GLU ARG LEU GLU ARG PRO ASP GLY PHE ALA THR SER
SEQRES 33 B 519 LEU ASP ILE GLN LEU LEU ASN GLN GLY ASP LEU THR SER
SEQRES 34 B 519 SER SER SER GLU LYS LEU ASN ASN TYR PHE TRP LYS SER
SEQRES 35 B 519 ILE GLU GLU GLY ASP PHE SER ASN THR THR PHE ALA LEU
SEQRES 36 B 519 ALA TYR MET LYS ASN ASP ASP TYR ASP ALA THR ALA PHE
SEQRES 37 B 519 SER ASP LEU LEU GLN TYR PHE ARG GLY LYS LYS HIS LYS
SEQRES 38 B 519 ILE LEU GLY ARG GLY TRP ASP GLY ARG HIS GLY ASP CYS
SEQRES 39 B 519 SER ALA GLU VAL GLY ALA TRP PHE THR SER GLN TYR ARG
SEQRES 40 B 519 ARG MET LEU SER ASN ASP PHE GLY ARG LYS GLU GLU
SEQRES 1 C 330 MET SER THR ILE SER TYR ILE TYR TRP ASP ASP PHE SER
SEQRES 2 C 330 ARG PHE SER TYR ASN PHE GLY THR LYS LEU GLN PHE LEU
SEQRES 3 C 330 GLY LYS SER VAL CYS PHE GLU ASN PRO LEU ALA PRO SER
SEQRES 4 C 330 SER THR ASN LEU TYR THR TRP SER SER GLN THR ASN TYR
SEQRES 5 C 330 GLN SER LYS ARG ILE SER PRO ASN LEU PRO LEU LEU ARG
SEQRES 6 C 330 LYS GLY THR ARG TYR SER LEU SER LEU ASN ALA GLU LEU
SEQRES 7 C 330 ASP LEU VAL SER SER LEU PHE VAL ARG ILE GLU PHE TYR
SEQRES 8 C 330 ASN ARG PHE ASN GLU SER VAL GLY PHE GLU LEU LEU LYS
SEQRES 9 C 330 LYS ASP SER ILE ILE PHE ILE TYR PRO LYS GLU ALA TYR
SEQRES 10 C 330 THR TYR THR ILE SER LEU ILE ASN ALA GLY CYS SER ASP
SEQRES 11 C 330 PHE THR PHE HIS TYR LEU LYS LEU GLU GLU VAL THR ASP
SEQRES 12 C 330 SER VAL ILE GLN GLU LYS ASN LEU SER THR GLU PHE THR
SEQRES 13 C 330 ILE GLU GLU HIS GLN ASP VAL LEU ASN LEU LEU LEU VAL
SEQRES 14 C 330 GLU LYS LYS ASP SER VAL TYR ILE ASN LYS ILE GLU SER
SEQRES 15 C 330 ILE SER GLN LEU GLN GLN LYS VAL GLU LEU VAL SER ASN
SEQRES 16 C 330 PRO SER LEU ASN SER ASP SER LEU ILE LEU PRO GLU LEU
SEQRES 17 C 330 GLU LYS GLY LEU GLU ASP ALA LEU LYS VAL PHE PRO ASN
SEQRES 18 C 330 ILE LYS ILE ASN VAL ILE ALA TYR GLY THR GLN GLY ASN
SEQRES 19 C 330 PHE ALA ALA LEU TYR TYR ALA LYS LYS PHE PRO ARG ILE
SEQRES 20 C 330 THR ALA TYR ILE ASN ASP CYS PHE ALA PRO PHE GLY ILE
SEQRES 21 C 330 LEU LEU LYS SER LEU PRO HIS LEU THR ALA LYS GLN GLN
SEQRES 22 C 330 ILE PHE LEU ARG GLU VAL TRP ASP THR ARG GLU THR SER
SEQRES 23 C 330 PRO ASN VAL LYS HIS TYR GLY LEU VAL SER GLU ASN SER
SEQRES 24 C 330 SER LEU ASN LEU VAL SER MET ILE LEU SER GLY ASN GLU
SEQRES 25 C 330 HIS LEU PRO TYR LEU THR LEU LEU LYS LYS GLN ASP ASP
SEQRES 26 C 330 ASN TYR ASP SER LEU
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET GOL A 605 6
HET GOL A 606 6
HET SO4 A 607 5
HET SO4 A 608 5
HET GOL B 601 6
HET GOL B 602 6
HET GOL B 603 6
HET GOL B 604 6
HET SO4 B 605 5
HET GOL C 401 6
HET GOL C 402 6
HET GOL C 403 6
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL 13(C3 H8 O3)
FORMUL 10 SO4 3(O4 S 2-)
FORMUL 20 HOH *403(H2 O)
HELIX 1 AA1 ASP A 32 ALA A 44 1 13
HELIX 2 AA2 ASN A 58 TYR A 66 1 9
HELIX 3 AA3 VAL A 76 GLN A 81 1 6
HELIX 4 AA4 ASP A 92 LEU A 96 5 5
HELIX 5 AA5 PRO A 194 PHE A 200 5 7
HELIX 6 AA6 ASP A 207 VAL A 224 1 18
HELIX 7 AA7 HIS A 238 VAL A 243 1 6
HELIX 8 AA8 ASN A 261 ASP A 268 1 8
HELIX 9 AA9 ASP A 268 ARG A 274 1 7
HELIX 10 AB1 ARG A 282 ILE A 293 1 12
HELIX 11 AB2 GLY A 310 VAL A 315 5 6
HELIX 12 AB3 SER A 328 LYS A 345 1 18
HELIX 13 AB4 GLU A 359 VAL A 376 1 18
HELIX 14 AB5 PHE A 377 ASP A 378 5 2
HELIX 15 AB6 GLN A 379 SER A 383 5 5
HELIX 16 AB7 SER A 413 LEU A 421 1 9
HELIX 17 AB8 ASP A 435 GLY A 446 1 12
HELIX 18 AB9 GLU A 469 GLN A 471 5 3
HELIX 19 AC1 GLU A 472 GLU A 482 1 11
HELIX 20 AC2 GLN A 483 GLY A 503 1 21
HELIX 21 AC3 GLY A 504 SER A 513 1 10
HELIX 22 AC4 ASN B 15 LYS B 19 5 5
HELIX 23 AC5 LYS B 32 ASP B 34 5 3
HELIX 24 AC6 GLN B 35 LEU B 53 1 19
HELIX 25 AC7 GLY B 71 PHE B 81 5 11
HELIX 26 AC8 THR B 95 LYS B 105 1 11
HELIX 27 AC9 SER B 114 LEU B 126 1 13
HELIX 28 AD1 GLN B 136 SER B 138 5 3
HELIX 29 AD2 GLU B 224 GLN B 228 5 5
HELIX 30 AD3 GLY B 312 MET B 319 1 8
HELIX 31 AD4 SER B 340 ASN B 359 1 20
HELIX 32 AD5 SER B 361 ASP B 363 5 3
HELIX 33 AD6 SER B 371 ALA B 382 1 12
HELIX 34 AD7 ASN B 397 ARG B 404 1 8
HELIX 35 AD8 GLU B 405 LEU B 407 5 3
HELIX 36 AD9 THR B 415 GLY B 425 1 11
HELIX 37 AE1 THR B 428 GLU B 445 1 18
HELIX 38 AE2 THR B 466 TYR B 474 1 9
HELIX 39 AE3 CYS B 494 GLY B 515 1 22
HELIX 40 AE4 ASN C 51 ARG C 56 1 6
HELIX 41 AE5 LEU C 80 SER C 82 5 3
HELIX 42 AE6 GLU C 170 VAL C 175 1 6
HELIX 43 AE7 LEU C 205 PHE C 219 1 15
HELIX 44 AE8 GLY C 230 PHE C 244 1 15
HELIX 45 AE9 PRO C 257 LYS C 263 1 7
HELIX 46 AF1 THR C 269 THR C 282 1 14
HELIX 47 AF2 LEU C 294 SER C 305 5 12
HELIX 48 AF3 SER C 309 THR C 318 5 10
SHEET 1 AA1 7 TYR A 73 SER A 75 0
SHEET 2 AA1 7 SER A 48 VAL A 52 1 N VAL A 52 O TYR A 74
SHEET 3 AA1 7 PHE A 2 ILE A 5 1 N PHE A 4 O ARG A 49
SHEET 4 AA1 7 THR A 229 SER A 233 1 O ILE A 231 N HIS A 3
SHEET 5 AA1 7 ASN A 250 VAL A 255 1 O ASN A 250 N ILE A 230
SHEET 6 AA1 7 ALA A 277 CYS A 280 1 O ILE A 279 N VAL A 255
SHEET 7 AA1 7 VAL A 297 HIS A 299 1 O VAL A 298 N ILE A 278
SHEET 1 AA210 ASP A 103 TYR A 106 0
SHEET 2 AA210 VAL A 111 LYS A 115 -1 O LEU A 112 N THR A 105
SHEET 3 AA210 ASP A 118 PHE A 125 -1 O ILE A 120 N VAL A 113
SHEET 4 AA210 LEU A 131 ALA A 138 -1 O PHE A 137 N ILE A 120
SHEET 5 AA210 GLN A 141 PHE A 148 -1 O LYS A 144 N TYR A 136
SHEET 6 AA210 LEU A 154 ASP A 161 -1 O SER A 156 N LEU A 147
SHEET 7 AA210 GLY A 164 LEU A 171 -1 O TYR A 167 N TYR A 159
SHEET 8 AA210 ARG A 177 TYR A 182 -1 O ILE A 178 N TYR A 170
SHEET 9 AA210 VAL A 190 ILE A 192 -1 O GLU A 191 N ARG A 180
SHEET 10 AA210 SER A 204 TYR A 205 -1 O TYR A 205 N VAL A 190
SHEET 1 AA3 6 LEU A 406 THR A 409 0
SHEET 2 AA3 6 ILE A 349 VAL A 354 1 N PHE A 353 O SER A 407
SHEET 3 AA3 6 LEU A 318 VAL A 323 1 N ILE A 320 O THR A 352
SHEET 4 AA3 6 LEU A 426 ILE A 428 1 O LEU A 426 N TYR A 321
SHEET 5 AA3 6 GLN A 449 ASN A 451 1 O ILE A 450 N ILE A 427
SHEET 6 AA3 6 GLY A 464 ILE A 466 1 O TYR A 465 N GLN A 449
SHEET 1 AA4 5 MET B 26 ILE B 31 0
SHEET 2 AA4 5 LEU B 6 VAL B 11 1 N ILE B 8 O LEU B 29
SHEET 3 AA4 5 ALA B 62 LEU B 65 1 O LEU B 64 N LEU B 9
SHEET 4 AA4 5 VAL B 86 PRO B 89 1 O PHE B 87 N LEU B 65
SHEET 5 AA4 5 GLN B 108 TYR B 110 1 O GLN B 108 N VAL B 86
SHEET 1 AA5 4 GLY B 132 LEU B 135 0
SHEET 2 AA5 4 GLY B 238 GLY B 262 -1 O LEU B 257 N LEU B 135
SHEET 3 AA5 4 TYR B 157 PHE B 174 -1 N LEU B 158 O LEU B 254
SHEET 4 AA5 4 ILE B 140 ILE B 142 -1 N GLN B 141 O ASN B 173
SHEET 1 AA6 4 GLY B 132 LEU B 135 0
SHEET 2 AA6 4 GLY B 238 GLY B 262 -1 O LEU B 257 N LEU B 135
SHEET 3 AA6 4 TYR B 185 VAL B 208 -1 N GLU B 191 O GLY B 255
SHEET 4 AA6 4 ILE B 215 GLU B 222 -1 O LYS B 217 N LEU B 206
SHEET 1 AA7 4 GLY B 132 LEU B 135 0
SHEET 2 AA7 4 GLY B 238 GLY B 262 -1 O LEU B 257 N LEU B 135
SHEET 3 AA7 4 TYR B 185 VAL B 208 -1 N GLU B 191 O GLY B 255
SHEET 4 AA7 4 ILE B 230 LEU B 232 -1 O LEU B 232 N ASN B 186
SHEET 1 AA8 3 GLY B 132 LEU B 135 0
SHEET 2 AA8 3 GLY B 238 GLY B 262 -1 O LEU B 257 N LEU B 135
SHEET 3 AA8 3 ILE B 178 PHE B 180 -1 N PHE B 180 O GLY B 238
SHEET 1 AA9 8 GLY B 132 LEU B 135 0
SHEET 2 AA9 8 GLY B 238 GLY B 262 -1 O LEU B 257 N LEU B 135
SHEET 3 AA9 8 TYR B 157 PHE B 174 -1 N LEU B 158 O LEU B 254
SHEET 4 AA9 8 VAL B 149 GLN B 153 -1 N ASN B 151 O GLU B 159
SHEET 5 AA9 8 LYS C 22 LEU C 26 -1 O LEU C 23 N TYR B 152
SHEET 6 AA9 8 SER C 29 GLU C 33 -1 O CYS C 31 N GLN C 24
SHEET 7 AA9 8 ASP C 130 GLU C 140 -1 O PHE C 131 N PHE C 32
SHEET 8 AA9 8 ILE C 4 ILE C 7 -1 N SER C 5 O LEU C 138
SHEET 1 AB1 8 ILE B 140 ILE B 142 0
SHEET 2 AB1 8 TYR B 157 PHE B 174 -1 O ASN B 173 N GLN B 141
SHEET 3 AB1 8 VAL B 149 GLN B 153 -1 N ASN B 151 O GLU B 159
SHEET 4 AB1 8 LYS C 22 LEU C 26 -1 O LEU C 23 N TYR B 152
SHEET 5 AB1 8 SER C 29 GLU C 33 -1 O CYS C 31 N GLN C 24
SHEET 6 AB1 8 ASP C 130 GLU C 140 -1 O PHE C 131 N PHE C 32
SHEET 7 AB1 8 ARG C 69 LEU C 78 -1 N SER C 71 O GLU C 139
SHEET 8 AB1 8 SER C 107 ILE C 111 -1 O PHE C 110 N TYR C 70
SHEET 1 AB2 8 GLU B 274 ILE B 277 0
SHEET 2 AB2 8 GLU B 283 ASP B 289 -1 O THR B 286 N GLU B 274
SHEET 3 AB2 8 PHE B 323 CYS B 327 -1 O LEU B 325 N TYR B 287
SHEET 4 AB2 8 LEU B 297 PHE B 301 1 N TYR B 300 O MET B 324
SHEET 5 AB2 8 LEU B 365 LEU B 370 1 O ILE B 366 N VAL B 299
SHEET 6 AB2 8 ALA B 388 GLY B 392 1 O ALA B 388 N LEU B 367
SHEET 7 AB2 8 THR B 452 MET B 458 1 O ALA B 454 N ILE B 391
SHEET 8 AB2 8 ILE B 482 TRP B 487 1 O LEU B 483 N PHE B 453
SHEET 1 AB3 4 THR C 41 SER C 47 0
SHEET 2 AB3 4 THR C 118 ASN C 125 -1 O ILE C 121 N TRP C 46
SHEET 3 AB3 4 LEU C 84 TYR C 91 -1 N PHE C 85 O ILE C 124
SHEET 4 AB3 4 SER C 97 LEU C 103 -1 O LEU C 103 N VAL C 86
SHEET 1 AB4 5 GLU C 191 VAL C 193 0
SHEET 2 AB4 5 VAL C 163 LEU C 168 1 N ASN C 165 O GLU C 191
SHEET 3 AB4 5 LYS C 223 ILE C 227 1 O LYS C 223 N LEU C 164
SHEET 4 AB4 5 THR C 248 ILE C 251 1 O TYR C 250 N VAL C 226
SHEET 5 AB4 5 VAL C 289 HIS C 291 1 O LYS C 290 N ALA C 249
CISPEP 1 PRO B 295 PRO B 296 0 1.80
SITE 1 AC1 6 ASP A 103 LYS A 114 SER A 116 GLY A 117
SITE 2 AC1 6 GLU B 218 LYS B 243
SITE 1 AC2 2 SER A 48 ARG A 49
SITE 1 AC3 3 GLU A 11 PRO A 26 ARG A 358
SITE 1 AC4 4 ARG A 326 ASN B 167 TYR B 168 ARG B 201
SITE 1 AC5 2 VAL A 297 HIS A 299
SITE 1 AC6 8 SER A 7 TRP A 8 TYR A 9 ASN A 18
SITE 2 AC6 8 VAL A 29 GLY A 30 ASP A 32 TYR A 62
SITE 1 AC7 6 PHE A 234 ASN A 235 GLN A 236 ASN A 260
SITE 2 AC7 6 ASN A 261 ASN A 264
SITE 1 AC8 5 THR A 27 ARG A 358 HOH A 775 GLU B 166
SITE 2 AC8 5 LYS B 247
SITE 1 AC9 2 LYS B 3 GLU B 27
SITE 1 AD1 2 SER B 306 ALA B 307
SITE 1 AD2 6 GLN B 108 ARG B 109 TYR B 110 GLN B 121
SITE 2 AD2 6 GLY B 265 LEU B 266
SITE 1 AD3 4 TYR B 131 ARG B 259 ASN B 261 HOH B 757
SITE 1 AD4 6 HIS A 263 LEU A 266 LYS B 217 TRP B 219
SITE 2 AD4 6 HOH B 716 HOH B 790
SITE 1 AD5 8 ASN A 97 TYR A 136 LYS A 144 TYR A 146
SITE 2 AD5 8 SER C 299 SER C 300 ASN C 302 LEU C 303
SITE 1 AD6 3 GLN C 49 ASN C 95 THR C 118
SITE 1 AD7 3 PRO C 206 GLU C 209 TYR C 239
CRYST1 103.009 168.321 100.034 90.00 90.00 90.00 P 21 21 2 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 0.009708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005941 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009997 0.00000
TER 4151 TYR A 514
TER 8315 GLU B 518
TER 10830 THR C 318
MASTER 420 0 16 48 76 0 23 611323 3 93 106
END |