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HEADER HYDROLASE 06-MAR-13 4BE9
TITLE OPEN CONFORMATION OF O. PICEAE STEROL ESTERASE
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 OTHER_DETAILS: N-ACETYLGLUCOSAMINE GLYCOSYLATIONS IN POSITIONS 362
COMPND 8 AND 380
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPHIOSTOMA PICEAE;
SOURCE 3 ORGANISM_TAXID: 61273;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA 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, OPHIOSTOMA
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 26-MAR-14 4BE9 0
JRNL AUTH J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,
JRNL AUTH 2 M.J.GONZALEZ,J.A.HERMOSO
JRNL TITL CRYSTAL STRUCTURE OF OPE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.000
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.561
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.99
REMARK 3 NUMBER OF REFLECTIONS : 84172
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1694
REMARK 3 R VALUE (WORKING SET) : 0.1675
REMARK 3 FREE R VALUE : 0.2059
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4204
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 43.5710 - 6.2088 1.00 2739 152 0.1953 0.1948
REMARK 3 2 6.2088 - 4.9303 1.00 2699 141 0.1816 0.1989
REMARK 3 3 4.9303 - 4.3077 1.00 2675 154 0.1365 0.1777
REMARK 3 4 4.3077 - 3.9141 1.00 2681 144 0.1487 0.1774
REMARK 3 5 3.9141 - 3.6337 1.00 2687 146 0.1556 0.1969
REMARK 3 6 3.6337 - 3.4196 1.00 2656 149 0.1595 0.1880
REMARK 3 7 3.4196 - 3.2484 1.00 2675 131 0.1589 0.2005
REMARK 3 8 3.2484 - 3.1070 1.00 2663 149 0.1548 0.1742
REMARK 3 9 3.1070 - 2.9874 1.00 2664 129 0.1591 0.1970
REMARK 3 10 2.9874 - 2.8844 1.00 2690 134 0.1499 0.1877
REMARK 3 11 2.8844 - 2.7942 1.00 2672 138 0.1516 0.2022
REMARK 3 12 2.7942 - 2.7143 1.00 2636 163 0.1625 0.1967
REMARK 3 13 2.7143 - 2.6429 1.00 2665 138 0.1572 0.2291
REMARK 3 14 2.6429 - 2.5784 1.00 2661 144 0.1602 0.2107
REMARK 3 15 2.5784 - 2.5198 1.00 2630 143 0.1649 0.2329
REMARK 3 16 2.5198 - 2.4662 1.00 2636 148 0.1689 0.2263
REMARK 3 17 2.4662 - 2.4169 1.00 2682 134 0.1709 0.2238
REMARK 3 18 2.4169 - 2.3713 1.00 2657 139 0.1652 0.2435
REMARK 3 19 2.3713 - 2.3289 1.00 2686 127 0.1666 0.1848
REMARK 3 20 2.3289 - 2.2894 1.00 2647 119 0.1708 0.2091
REMARK 3 21 2.2894 - 2.2525 1.00 2617 153 0.1822 0.2702
REMARK 3 22 2.2525 - 2.2178 1.00 2674 143 0.1773 0.2592
REMARK 3 23 2.2178 - 2.1852 1.00 2663 150 0.1815 0.2520
REMARK 3 24 2.1852 - 2.1545 1.00 2669 130 0.1888 0.2462
REMARK 3 25 2.1545 - 2.1253 1.00 2628 131 0.1936 0.2360
REMARK 3 26 2.1253 - 2.0977 1.00 2690 144 0.1953 0.2495
REMARK 3 27 2.0977 - 2.0715 1.00 2655 131 0.2082 0.2627
REMARK 3 28 2.0715 - 2.0466 1.00 2656 129 0.2073 0.2775
REMARK 3 29 2.0466 - 2.0228 1.00 2653 144 0.2378 0.2755
REMARK 3 30 2.0228 - 2.0000 1.00 2662 127 0.2697 0.2975
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.328
REMARK 3 B_SOL : 41.224
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.53
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.6444
REMARK 3 B22 (A**2) : 1.6444
REMARK 3 B33 (A**2) : -3.2889
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
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 8743
REMARK 3 ANGLE : 1.051 11877
REMARK 3 CHIRALITY : 0.073 1323
REMARK 3 PLANARITY : 0.005 1527
REMARK 3 DIHEDRAL : 14.118 3136
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4231 0.2326 28.1470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0070 T22: 0.0676
REMARK 3 T33: 0.0352 T12: 0.0846
REMARK 3 T13: 0.0328 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.4222 L22: 0.4489
REMARK 3 L33: 0.5376 L12: -0.0740
REMARK 3 L13: -0.0914 L23: 0.1270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: -0.2018 S13: -0.0904
REMARK 3 S21: 0.2746 S22: 0.0089 S23: -0.0598
REMARK 3 S31: 0.0889 S32: 0.0832 S33: -0.0418
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FIRST 8 AMINO ACIDS OF THE SAMPLE
REMARK 3 (EAEAYVEF) CORRESPOND TO A PURIFICATION TAG. THIS REGION IS MAINLY
REMARK 3 DISORDERED IN THE CRYSTAL.
REMARK 4
REMARK 4 4BE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-13.
REMARK 100 THE PDBE ID CODE IS EBI-55740.
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 : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97908
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84190
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 47.28
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.0
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.1
REMARK 200 R MERGE FOR SHELL (I) : 0.81
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.50
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 1LPN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
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 82.06150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 82.06150
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.99700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 82.06150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.49850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 82.06150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 70.49550
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 82.06150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.06150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 46.99700
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 82.06150
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 70.49550
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 82.06150
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 23.49850
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: 7760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.5 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 OD2 ASP A 293 O HOH A 2340 2.12
REMARK 500 OD1 ASN A 391 O HOH A 2393 1.91
REMARK 500 OD2 ASP A 396 OG1 THR A 398 2.20
REMARK 500 NE2 GLN A 510 O HOH A 2495 2.08
REMARK 500 OH TYR A 541 O HOH A 2451 2.13
REMARK 500 ND2 ASN B 18 OE1 GLU B 23 2.04
REMARK 500 NH2 ARG B 55 O HOH B 2004 2.02
REMARK 500 OG SER B 123 O HOH B 2059 2.16
REMARK 500 ND2 ASN B 203 O HOH B 2004 2.19
REMARK 500 N LEU B 477 O8 7P9 B 1551 2.11
REMARK 500 O7 NAG A 1550 O HOH A 2395 2.12
REMARK 500 O2 7P9 A 1552 O HOH A 2472 2.09
REMARK 500 O2 NO3 A 1557 O HOH A 2531 2.09
REMARK 500 O HOH A 2065 O HOH A 2339 2.16
REMARK 500 O HOH A 2123 O HOH A 2278 2.08
REMARK 500 O HOH A 2140 O HOH A 2295 2.17
REMARK 500 O HOH A 2461 O HOH A 2462 1.97
REMARK 500 O HOH B 2017 O HOH B 2049 2.05
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 PHE A 136 19.78 59.51
REMARK 500 SER A 220 -120.16 63.87
REMARK 500 SER A 252 76.63 68.91
REMARK 500 SER A 254 -90.92 -153.91
REMARK 500 SER A 309 -178.74 -177.27
REMARK 500 SER A 312 -121.71 47.66
REMARK 500 VAL A 324 -59.18 -123.73
REMARK 500 ASP A 351 63.49 -115.30
REMARK 500 TYR A 377 -70.92 -102.67
REMARK 500 ASN A 409 11.91 81.65
REMARK 500 PHE A 427 -70.08 -126.30
REMARK 500 PHE A 460 -36.93 69.16
REMARK 500 ASN A 479 -168.90 -165.63
REMARK 500 VAL B 15 117.21 -167.81
REMARK 500 LEU B 30 65.59 -7.70
REMARK 500 PHE B 136 17.83 58.79
REMARK 500 SER B 220 -118.81 50.25
REMARK 500 SER B 252 77.84 70.96
REMARK 500 SER B 254 -97.62 -152.81
REMARK 500 SER B 312 -122.09 46.33
REMARK 500 VAL B 324 -54.64 -133.02
REMARK 500 PRO B 343 141.75 -39.65
REMARK 500 ASP B 351 61.10 -115.22
REMARK 500 PRO B 360 47.63 -72.70
REMARK 500 TYR B 377 -65.69 -100.40
REMARK 500 ASN B 380 40.59 -104.86
REMARK 500 ASN B 409 13.48 80.02
REMARK 500 PHE B 427 -65.19 -127.11
REMARK 500 PHE B 460 -43.73 73.00
REMARK 500 ALA B 466 2.07 81.67
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 B 16 24.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): COVALENTLY BOUND TO A-ASN362,
REMARK 600 A-ASN380 AND B-ASN362 RESPECTIVELY, BY N-GLYCOSIDIC
REMARK 600 LINKAGES
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7P9 A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7P9 B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1550 BOUND TO ASN A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1551 BOUND TO ASN A 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1550 BOUND TO ASN B 362
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BE4 RELATED DB: PDB
REMARK 900 CLOSED CONFORMATION OF O. PICEAE STEROL ESTERASE
DBREF 4BE9 A 13 549 UNP Q2TFW1 Q2TFW1_9PEZI 13 549
DBREF 4BE9 B 13 549 UNP Q2TFW1 Q2TFW1_9PEZI 13 549
SEQADV 4BE9 GLU A 5 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 ALA A 6 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 GLU A 7 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 ALA A 8 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 TYR A 9 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 VAL A 10 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 GLU A 11 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 PHE A 12 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 GLU B 5 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 ALA B 6 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 GLU B 7 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 ALA B 8 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 TYR B 9 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 VAL B 10 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 GLU B 11 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE9 PHE B 12 UNP Q2TFW1 EXPRESSION TAG
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 ILE 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 ILE GLY ILE PHE ARG ILE
HET NAG A1550 14
HET NAG A1551 14
HET NAG B1550 14
HET 7P9 A1552 28
HET 7P9 B1551 28
HET 1PE A1553 16
HET PGE A1554 10
HET PEG A1555 7
HET PGE A1558 10
HET PEG A1559 7
HET PEG B1552 7
HET PEG B1553 7
HET PEG B1554 7
HET PEG B1555 7
HET PGE B1556 10
HET GOL A1556 6
HET GOL B1557 6
HET GOL B1558 6
HET NO3 A1557 4
HET NO3 B1559 4
HETNAM NO3 NITRATE ION
HETNAM 7P9 [(2R)-2-HEPTANOYLOXY-3-PHOSPHONOOXY-PROPYL]
HETNAM 2 7P9 NONANOATE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN 1PE PEG400
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NO3 2(N O3 1-)
FORMUL 3 7P9 2(C19 H37 O8 P)
FORMUL 4 1PE C10 H22 O6
FORMUL 5 PGE 3(C6 H14 O4)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 7 PEG 6(C4 H10 O3)
FORMUL 8 NAG 3(C8 H15 N O6)
FORMUL 9 HOH *768(H2 O)
HELIX 1 1 VAL A 45 ARG A 49 5 5
HELIX 2 2 GLU A 83 ILE A 93 1 11
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 PHE A 174 1 6
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 ARG A 290 1 7
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 THR A 392 1 11
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 ILE 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 THR B 140 TYR B 144 5 5
HELIX 30 30 GLY B 146 GLY B 157 1 12
HELIX 31 31 VAL B 169 PHE B 174 1 6
HELIX 32 32 GLY B 177 ASP B 183 1 7
HELIX 33 33 ASN B 187 ILE B 204 1 18
HELIX 34 34 ALA B 205 PHE B 207 5 3
HELIX 35 35 SER B 220 ASN B 236 1 17
HELIX 36 36 GLY B 263 ALA B 277 1 15
HELIX 37 37 ASP B 284 ARG B 290 1 7
HELIX 38 38 ASP B 293 ASN B 302 1 10
HELIX 39 39 SER B 329 ASN B 336 1 8
HELIX 40 40 GLY B 353 VAL B 358 1 6
HELIX 41 41 SER B 365 TYR B 377 1 13
HELIX 42 42 THR B 382 ASN B 391 1 10
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 ILE 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 THR B 14 TYR B 19 0
SHEET 2 BA 2 GLY B 22 VAL B 29 -1 O GLY B 22 N TYR B 19
SHEET 1 BB 2 THR B 62 ASP B 64 0
SHEET 2 BB 2 GLY B 22 VAL B 29 1 O GLU B 23 N LYS B 63
SHEET 1 BC12 ALA B 525 ALA B 529 0
SHEET 2 BC12 ASN B 516 ILE B 520 -1 O ILE B 517 N VAL B 528
SHEET 3 BC12 SER B 447 ALA B 452 1 O SER B 449 N LEU B 518
SHEET 4 BC12 MET B 344 GLN B 349 1 O MET B 344 N TRP B 448
SHEET 5 BC12 GLY B 247 ASN B 251 1 O GLY B 248 N ILE B 345
SHEET 6 BC12 GLY B 209 GLU B 219 1 O ILE B 216 N ILE B 249
SHEET 7 BC12 LEU B 125 ILE B 131 1 O LEU B 125 N ASP B 210
SHEET 8 BC12 ILE B 161 ILE B 165 1 O ILE B 161 N LEU B 128
SHEET 9 BC12 THR B 110 PRO B 116 -1 O ASN B 112 N ALA B 164
SHEET 10 BC12 ILE B 32 PRO B 39 -1 O GLU B 33 N ARG B 115
SHEET 11 BC12 GLY B 22 VAL B 29 -1 O VAL B 27 N SER B 34
SHEET 12 BC12 THR B 62 ASP B 64 1 O LYS B 63 N VAL B 25
SHEET 1 BD12 ALA B 525 ALA B 529 0
SHEET 2 BD12 ASN B 516 ILE B 520 -1 O ILE B 517 N VAL B 528
SHEET 3 BD12 SER B 447 ALA B 452 1 O SER B 449 N LEU B 518
SHEET 4 BD12 MET B 344 GLN B 349 1 O MET B 344 N TRP B 448
SHEET 5 BD12 GLY B 247 ASN B 251 1 O GLY B 248 N ILE B 345
SHEET 6 BD12 GLY B 209 GLU B 219 1 O ILE B 216 N ILE B 249
SHEET 7 BD12 LEU B 125 ILE B 131 1 O LEU B 125 N ASP B 210
SHEET 8 BD12 ILE B 161 ILE B 165 1 O ILE B 161 N LEU B 128
SHEET 9 BD12 THR B 110 PRO B 116 -1 O ASN B 112 N ALA B 164
SHEET 10 BD12 ILE B 32 PRO B 39 -1 O GLU B 33 N ARG B 115
SHEET 11 BD12 GLY B 22 VAL B 29 -1 O VAL B 27 N SER B 34
SHEET 12 BD12 THR B 14 TYR B 19 -1 O VAL B 15 N GLY B 26
SHEET 1 BE 2 LYS B 238 TYR B 239 0
SHEET 2 BE 2 LYS B 242 ALA B 243 -1 O LYS B 242 N TYR B 239
SSBOND 1 CYS A 72 CYS A 108 1555 1555 2.05
SSBOND 2 CYS A 279 CYS A 288 1555 1555 2.10
SSBOND 3 CYS B 72 CYS B 108 1555 1555 2.04
SSBOND 4 CYS B 279 CYS B 288 1555 1555 2.04
LINK ND2 ASN A 362 C1 NAG A1550 1555 1555 1.38
LINK ND2 ASN A 380 C1 NAG A1551 1555 1555 1.31
LINK ND2 ASN B 362 C1 NAG B1550 1555 1555 1.35
CISPEP 1 SER A 401 PRO A 402 0 4.28
CISPEP 2 VAL A 476 LEU A 477 0 -1.74
CISPEP 3 SER B 401 PRO B 402 0 5.37
CISPEP 4 VAL B 476 LEU B 477 0 -3.91
SITE 1 AC1 14 ASP A 455 PHE A 458 LEU A 470 GLN A 471
SITE 2 AC1 14 VAL A 476 LEU A 477 ASN A 479 ALA A 522
SITE 3 AC1 14 HOH A2462 HOH A2463 HOH A2464 HOH A2472
SITE 4 AC1 14 HOH A2528 HOH A2529
SITE 1 AC2 7 PHE A 98 ASP B 455 PHE B 458 LEU B 470
SITE 2 AC2 7 GLN B 471 VAL B 476 LEU B 477
SITE 1 AC3 13 GLY A 135 SER A 220 ALA A 221 ILE A 224
SITE 2 AC3 13 PRO A 257 ILE A 313 LEU A 315 MET A 425
SITE 3 AC3 13 THR A 426 PHE A 427 ILE A 544 PHE A 547
SITE 4 AC3 13 HOH A2184
SITE 1 AC4 1 TYR A 144
SITE 1 AC5 2 LEU A 355 HOH A2530
SITE 1 AC6 6 GLY B 135 SER B 220 ALA B 221 ILE B 224
SITE 2 AC6 6 THR B 426 HOH B2065
SITE 1 AC7 2 PEG B1554 PEG B1555
SITE 1 AC8 1 PEG B1553
SITE 1 AC9 2 PHE B 464 PEG B1553
SITE 1 BC1 1 LEU B 355
SITE 1 BC2 7 GLU A 350 PHE A 403 ASN A 404 LEU A 451
SITE 2 BC2 7 ARG A 533 HOH A2373 HOH A2374
SITE 1 BC3 5 GLU B 350 ASN B 404 LEU B 451 GLN B 519
SITE 2 BC3 5 ARG B 533
SITE 1 BC4 2 PHE B 408 ASN B 409
SITE 1 BC5 7 ARG A 36 ASP A 64 THR A 65 THR A 66
SITE 2 BC5 7 GLY A 67 ILE A 68 HOH A2531
SITE 1 BC6 3 ASN B 81 HIS B 272 SER B 303
SITE 1 BC7 4 TYR A 310 ASN A 362 HOH A2395 HOH A2525
SITE 1 BC8 6 ALA A 259 ASN A 380 GLU A 384 ARG A 548
SITE 2 BC8 6 HOH A2523 HOH A2527
SITE 1 BC9 3 TYR B 310 ASN B 362 HOH B2139
CRYST1 164.123 164.123 93.994 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 0.006093 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010639 0.00000
TER 4179 ILE A 549
TER 8320 ILE B 549
MASTER 453 0 20 49 60 0 30 6 9295 2 223 84
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