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HEADER HYDROLASE 17-DEC-18 6NE9
TITLE BACTEROIDES INTESTINALIS ACETYL XYLAN ESTERASE (BACINT_01039)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOAMYLASE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES INTESTINALIS;
SOURCE 3 ORGANISM_TAXID: 329854;
SOURCE 4 GENE: HMPREF2531_02003;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOHYDRATE ESTERASE FAMILY 1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.KOROPATKIN,G.V.PEREIRA,I.CANN
REVDAT 1 25-DEC-19 6NE9 0
JRNL AUTH G.V.PEREIRA,C.DALESSANDRO-GABAZZA,J.FARRIS,D.WEFERS,
JRNL AUTH 2 R.MACKIE,N.M.KOROPATKIN,E.C.GABAZZA,I.CANN
JRNL TITL COMPLEX ARABINOXYLAN FERMENTING BACTEROIDETES RELEASE
JRNL TITL 2 DIETARY ANTIOXIDANTS THAT IMPACT HOST IMMUNE FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 76952
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3859
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 28.6014 - 5.2673 1.00 2995 187 0.2035 0.1987
REMARK 3 2 5.2673 - 4.1850 0.98 2867 162 0.1518 0.1976
REMARK 3 3 4.1850 - 3.6572 1.00 2870 159 0.1554 0.1846
REMARK 3 4 3.6572 - 3.3234 1.00 2894 122 0.1575 0.1943
REMARK 3 5 3.3234 - 3.0855 1.00 2876 144 0.1685 0.1984
REMARK 3 6 3.0855 - 2.9037 1.00 2863 155 0.1700 0.2191
REMARK 3 7 2.9037 - 2.7584 1.00 2847 151 0.1671 0.1932
REMARK 3 8 2.7584 - 2.6385 1.00 2826 161 0.1695 0.1993
REMARK 3 9 2.6385 - 2.5370 1.00 2827 165 0.1720 0.2187
REMARK 3 10 2.5370 - 2.4495 1.00 2820 157 0.1825 0.2237
REMARK 3 11 2.4495 - 2.3729 0.99 2813 168 0.1865 0.2413
REMARK 3 12 2.3729 - 2.3051 1.00 2814 166 0.1836 0.2085
REMARK 3 13 2.3051 - 2.2444 1.00 2826 143 0.1847 0.2372
REMARK 3 14 2.2444 - 2.1897 1.00 2813 153 0.1934 0.2440
REMARK 3 15 2.1897 - 2.1399 1.00 2846 158 0.1943 0.2216
REMARK 3 16 2.1399 - 2.0944 1.00 2832 129 0.1946 0.2442
REMARK 3 17 2.0944 - 2.0525 1.00 2834 129 0.1938 0.2068
REMARK 3 18 2.0525 - 2.0138 1.00 2855 142 0.2052 0.2411
REMARK 3 19 2.0138 - 1.9779 1.00 2789 160 0.2046 0.2413
REMARK 3 20 1.9779 - 1.9443 1.00 2803 148 0.2168 0.2622
REMARK 3 21 1.9443 - 1.9130 1.00 2810 123 0.2225 0.2826
REMARK 3 22 1.9130 - 1.8836 0.99 2833 143 0.2292 0.2699
REMARK 3 23 1.8836 - 1.8559 0.98 2757 156 0.2469 0.2766
REMARK 3 24 1.8559 - 1.8297 0.95 2657 158 0.2507 0.2820
REMARK 3 25 1.8297 - 1.8050 0.86 2420 111 0.2681 0.2785
REMARK 3 26 1.8050 - 1.7816 0.56 1601 69 0.2779 0.3357
REMARK 3 27 1.7816 - 1.7593 0.29 817 34 0.2876 0.3471
REMARK 3 28 1.7593 - 1.7381 0.10 288 6 0.2617 0.5582
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.30
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 : 0.004 5815
REMARK 3 ANGLE : 0.927 7837
REMARK 3 CHIRALITY : 0.035 799
REMARK 3 PLANARITY : 0.004 1019
REMARK 3 DIHEDRAL : 13.147 2113
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 6NE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1000237972.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145030
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.738
REMARK 200 RESOLUTION RANGE LOW (A) : 28.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 28.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.20
REMARK 200 R MERGE FOR SHELL (I) : 0.22860
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: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM AMMONIUM SULFATE, 80 MM SODIUM
REMARK 280 CACODYLATE PH 6.5, AND 21% PEG4000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 55.13000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.13000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.35150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.27650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.35150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.27650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.13000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.35150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.27650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.13000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.35150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.27650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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 A 722 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 MSE A 1
REMARK 465 LYS A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 ILE A 5
REMARK 465 LEU A 6
REMARK 465 PHE A 7
REMARK 465 TRP A 8
REMARK 465 SER A 9
REMARK 465 MSE A 10
REMARK 465 MSE A 11
REMARK 465 SER A 12
REMARK 465 TRP A 13
REMARK 465 MSE A 14
REMARK 465 VAL A 15
REMARK 465 SER A 16
REMARK 465 VAL A 17
REMARK 465 GLY A 18
REMARK 465 LEU A 19
REMARK 465 PRO A 20
REMARK 465 SER A 21
REMARK 465 PHE A 22
REMARK 465 ALA A 23
REMARK 465 GLN A 24
REMARK 465 SER A 293
REMARK 465 ASN A 294
REMARK 465 TYR A 295
REMARK 465 PRO A 296
REMARK 465 SER A 297
REMARK 465 THR A 298
REMARK 465 GLU A 299
REMARK 465 PRO A 300
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 LYS B 3
REMARK 465 GLN B 4
REMARK 465 ILE B 5
REMARK 465 LEU B 6
REMARK 465 PHE B 7
REMARK 465 TRP B 8
REMARK 465 SER B 9
REMARK 465 MSE B 10
REMARK 465 MSE B 11
REMARK 465 SER B 12
REMARK 465 TRP B 13
REMARK 465 MSE B 14
REMARK 465 VAL B 15
REMARK 465 SER B 16
REMARK 465 VAL B 17
REMARK 465 GLY B 18
REMARK 465 LEU B 19
REMARK 465 PRO B 20
REMARK 465 SER B 21
REMARK 465 PHE B 22
REMARK 465 ALA B 23
REMARK 465 GLN B 24
REMARK 465 LYS B 227
REMARK 465 SER B 228
REMARK 465 PRO B 229
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 O1 EDO A 410 O HOH A 501 2.09
REMARK 500 O HOH A 623 O HOH A 689 2.14
REMARK 500 O HOH A 681 O HOH A 717 2.15
REMARK 500 O HOH A 543 O HOH A 735 2.16
REMARK 500 O HOH A 614 O HOH A 750 2.17
REMARK 500 OE2 GLU A 33 O HOH A 502 2.17
REMARK 500 O HOH B 581 O HOH B 722 2.17
REMARK 500 O HOH A 706 O HOH A 759 2.17
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 O HOH A 713 O HOH A 713 3655 2.16
REMARK 500 O HOH A 501 O HOH B 507 6665 2.17
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 ALA A 56 72.92 -154.17
REMARK 500 ASP A 168 -75.74 -86.61
REMARK 500 ARG A 192 -79.35 -102.76
REMARK 500 SER A 266 -127.43 55.61
REMARK 500 ALA A 363 -148.79 -108.37
REMARK 500 ALA B 56 70.63 -150.62
REMARK 500 ARG B 192 -82.85 -93.08
REMARK 500 GLU B 242 -52.69 -121.39
REMARK 500 SER B 266 -123.00 49.91
REMARK 500 ALA B 363 -146.57 -108.79
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 A 763 DISTANCE = 6.37 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410
DBREF 6NE9 A 1 382 PDB 6NE9 6NE9 1 382
DBREF 6NE9 B 1 382 PDB 6NE9 6NE9 1 382
SEQRES 1 A 382 MSE LYS LYS GLN ILE LEU PHE TRP SER MSE MSE SER TRP
SEQRES 2 A 382 MSE VAL SER VAL GLY LEU PRO SER PHE ALA GLN THR VAL
SEQRES 3 A 382 GLU ASP PHE LYS PRO SER GLU VAL ASN GLN PRO GLY LYS
SEQRES 4 A 382 LEU TYR PRO GLN VAL ASN SER GLU ARG LYS VAL ARG VAL
SEQRES 5 A 382 GLN ILE SER ALA PRO GLU ALA LYS VAL VAL GLN LEU ASP
SEQRES 6 A 382 LEU GLY GLY VAL LYS TYR ASP LEU THR LYS ASP GLU LYS
SEQRES 7 A 382 GLY VAL TRP THR GLY GLU SER ALA PRO GLN GLN GLU GLY
SEQRES 8 A 382 PHE HIS TYR TYR GLN LEU ASN VAL ASP GLY ALA ALA VAL
SEQRES 9 A 382 PRO ASP PRO GLY THR ILE TYR PHE TYR GLY ALA GLY ARG
SEQRES 10 A 382 TRP GLY SER GLY ILE GLU VAL PRO ALA HIS ASP ALA ASP
SEQRES 11 A 382 PHE TYR ALA LEU LYS ASP VAL PRO HIS GLY LEU LEU SER
SEQRES 12 A 382 GLU MSE ASN TYR TYR SER ASN LEU THR LYS ALA TRP ARG
SEQRES 13 A 382 ARG CYS PHE VAL TYR THR PRO ALA GLY TYR GLY ASP ASN
SEQRES 14 A 382 LYS ASP LYS ARG TYR PRO VAL LEU TYR LEU GLN HIS GLY
SEQRES 15 A 382 SER PHE GLU ASP GLU THR GLY TRP GLY ARG GLN GLY LYS
SEQRES 16 A 382 THR ASN LEU ILE LEU ASP ASN LEU ILE ALA ALA GLY LYS
SEQRES 17 A 382 ALA VAL PRO MSE LEU VAL VAL MSE ASP ASN GLY TYR ALA
SEQRES 18 A 382 THR LYS PRO GLY GLU LYS SER PRO PHE ALA ALA SER ILE
SEQRES 19 A 382 PHE GLU GLU VAL LEU MSE ASN GLU VAL ILE PRO MSE ILE
SEQRES 20 A 382 ASP ALA LYS PHE ARG THR LEU SER GLY ARG GLU ASP ARG
SEQRES 21 A 382 ALA ILE ALA GLY LEU SER MSE GLY ALA ASN GLN THR MSE
SEQRES 22 A 382 HIS ILE ALA MSE ASN ASN PRO GLY HIS PHE ALA TYR TYR
SEQRES 23 A 382 GLY GLY PHE SER GLY THR SER ASN TYR PRO SER THR GLU
SEQRES 24 A 382 PRO LEU ASP ALA THR THR PHE LEU ASN GLY LYS PHE LYS
SEQRES 25 A 382 ASP ALA LYS ALA VAL ASN VAL GLN PHE LYS VAL PHE PHE
SEQRES 26 A 382 LEU GLY LEU GLY THR ALA GLU PRO HIS PRO PHE PRO GLY
SEQRES 27 A 382 VAL VAL LYS ALA PHE ARG GLN MSE MSE ASP LYS GLN GLY
SEQRES 28 A 382 ILE LYS TYR VAL TYR TYR GLU SER PRO ASP THR ALA HIS
SEQRES 29 A 382 GLU TRP LEU THR TRP ARG ARG ALA LEU ASN GLU PHE ALA
SEQRES 30 A 382 PRO LEU LEU PHE LYS
SEQRES 1 B 382 MSE LYS LYS GLN ILE LEU PHE TRP SER MSE MSE SER TRP
SEQRES 2 B 382 MSE VAL SER VAL GLY LEU PRO SER PHE ALA GLN THR VAL
SEQRES 3 B 382 GLU ASP PHE LYS PRO SER GLU VAL ASN GLN PRO GLY LYS
SEQRES 4 B 382 LEU TYR PRO GLN VAL ASN SER GLU ARG LYS VAL ARG VAL
SEQRES 5 B 382 GLN ILE SER ALA PRO GLU ALA LYS VAL VAL GLN LEU ASP
SEQRES 6 B 382 LEU GLY GLY VAL LYS TYR ASP LEU THR LYS ASP GLU LYS
SEQRES 7 B 382 GLY VAL TRP THR GLY GLU SER ALA PRO GLN GLN GLU GLY
SEQRES 8 B 382 PHE HIS TYR TYR GLN LEU ASN VAL ASP GLY ALA ALA VAL
SEQRES 9 B 382 PRO ASP PRO GLY THR ILE TYR PHE TYR GLY ALA GLY ARG
SEQRES 10 B 382 TRP GLY SER GLY ILE GLU VAL PRO ALA HIS ASP ALA ASP
SEQRES 11 B 382 PHE TYR ALA LEU LYS ASP VAL PRO HIS GLY LEU LEU SER
SEQRES 12 B 382 GLU MSE ASN TYR TYR SER ASN LEU THR LYS ALA TRP ARG
SEQRES 13 B 382 ARG CYS PHE VAL TYR THR PRO ALA GLY TYR GLY ASP ASN
SEQRES 14 B 382 LYS ASP LYS ARG TYR PRO VAL LEU TYR LEU GLN HIS GLY
SEQRES 15 B 382 SER PHE GLU ASP GLU THR GLY TRP GLY ARG GLN GLY LYS
SEQRES 16 B 382 THR ASN LEU ILE LEU ASP ASN LEU ILE ALA ALA GLY LYS
SEQRES 17 B 382 ALA VAL PRO MSE LEU VAL VAL MSE ASP ASN GLY TYR ALA
SEQRES 18 B 382 THR LYS PRO GLY GLU LYS SER PRO PHE ALA ALA SER ILE
SEQRES 19 B 382 PHE GLU GLU VAL LEU MSE ASN GLU VAL ILE PRO MSE ILE
SEQRES 20 B 382 ASP ALA LYS PHE ARG THR LEU SER GLY ARG GLU ASP ARG
SEQRES 21 B 382 ALA ILE ALA GLY LEU SER MSE GLY ALA ASN GLN THR MSE
SEQRES 22 B 382 HIS ILE ALA MSE ASN ASN PRO GLY HIS PHE ALA TYR TYR
SEQRES 23 B 382 GLY GLY PHE SER GLY THR SER ASN TYR PRO SER THR GLU
SEQRES 24 B 382 PRO LEU ASP ALA THR THR PHE LEU ASN GLY LYS PHE LYS
SEQRES 25 B 382 ASP ALA LYS ALA VAL ASN VAL GLN PHE LYS VAL PHE PHE
SEQRES 26 B 382 LEU GLY LEU GLY THR ALA GLU PRO HIS PRO PHE PRO GLY
SEQRES 27 B 382 VAL VAL LYS ALA PHE ARG GLN MSE MSE ASP LYS GLN GLY
SEQRES 28 B 382 ILE LYS TYR VAL TYR TYR GLU SER PRO ASP THR ALA HIS
SEQRES 29 B 382 GLU TRP LEU THR TRP ARG ARG ALA LEU ASN GLU PHE ALA
SEQRES 30 B 382 PRO LEU LEU PHE LYS
MODRES 6NE9 MSE A 212 MET MODIFIED RESIDUE
MODRES 6NE9 MSE A 216 MET MODIFIED RESIDUE
MODRES 6NE9 MSE A 246 MET MODIFIED RESIDUE
MODRES 6NE9 MSE A 267 MET MODIFIED RESIDUE
MODRES 6NE9 MSE B 212 MET MODIFIED RESIDUE
MODRES 6NE9 MSE B 216 MET MODIFIED RESIDUE
MODRES 6NE9 MSE B 246 MET MODIFIED RESIDUE
MODRES 6NE9 MSE B 267 MET MODIFIED RESIDUE
HET MSE A 145 17
HET MSE A 212 17
HET MSE A 216 17
HET MSE A 240 17
HET MSE A 246 17
HET MSE A 267 10
HET MSE A 273 17
HET MSE A 277 8
HET MSE A 346 10
HET MSE A 347 10
HET MSE B 145 17
HET MSE B 212 17
HET MSE B 216 17
HET MSE B 240 17
HET MSE B 246 17
HET MSE B 267 17
HET MSE B 273 17
HET MSE B 277 17
HET MSE B 346 17
HET MSE B 347 10
HET PEG A 401 17
HET PEG A 402 17
HET PEG A 403 17
HET EDO A 404 10
HET EDO A 405 10
HET EDO A 406 10
HET EDO A 407 10
HET EDO A 408 10
HET EDO A 409 10
HET EDO A 410 10
HET SO4 A 411 5
HET PEG B 401 17
HET PEG B 402 17
HET PEG B 403 17
HET PEG B 404 17
HET PEG B 405 17
HET EDO B 406 10
HET EDO B 407 10
HET EDO B 408 10
HET EDO B 409 10
HET EDO B 410 10
HET CL B 411 1
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 PEG 8(C4 H10 O3)
FORMUL 6 EDO 12(C2 H6 O2)
FORMUL 13 SO4 O4 S 2-
FORMUL 24 CL CL 1-
FORMUL 25 HOH *487(H2 O)
HELIX 1 AA1 ASP A 128 ALA A 133 5 6
HELIX 2 AA2 PRO A 163 ASP A 168 5 6
HELIX 3 AA3 LYS A 195 ALA A 206 1 12
HELIX 4 AA4 ILE A 234 GLU A 242 1 9
HELIX 5 AA5 GLU A 242 PHE A 251 1 10
HELIX 6 AA6 GLY A 256 GLU A 258 5 3
HELIX 7 AA7 SER A 266 ASN A 279 1 14
HELIX 8 AA8 ASP A 313 PHE A 321 1 9
HELIX 9 AA9 PRO A 335 GLY A 351 1 17
HELIX 10 AB1 GLU A 365 ALA A 377 1 13
HELIX 11 AB2 PRO A 378 LEU A 380 5 3
HELIX 12 AB3 ASP B 128 ALA B 133 5 6
HELIX 13 AB4 LYS B 195 ALA B 206 1 12
HELIX 14 AB5 ILE B 234 GLU B 242 1 9
HELIX 15 AB6 GLU B 242 PHE B 251 1 10
HELIX 16 AB7 GLY B 256 GLU B 258 5 3
HELIX 17 AB8 SER B 266 ASN B 279 1 14
HELIX 18 AB9 ASP B 313 PHE B 321 1 9
HELIX 19 AC1 PRO B 335 GLY B 351 1 17
HELIX 20 AC2 GLU B 365 ALA B 377 1 13
HELIX 21 AC3 PRO B 378 LEU B 380 5 3
SHEET 1 AA1 5 LYS A 30 PRO A 31 0
SHEET 2 AA1 5 GLN A 43 VAL A 44 -1 O VAL A 44 N LYS A 30
SHEET 3 AA1 5 VAL A 50 SER A 55 -1 O ARG A 51 N GLN A 43
SHEET 4 AA1 5 VAL A 80 GLU A 84 -1 O TRP A 81 N ILE A 54
SHEET 5 AA1 5 THR A 74 LYS A 75 -1 N THR A 74 O THR A 82
SHEET 1 AA2 4 VAL A 69 ASP A 72 0
SHEET 2 AA2 4 VAL A 62 LEU A 66 -1 N LEU A 64 O TYR A 71
SHEET 3 AA2 4 GLY A 91 VAL A 99 -1 O ASN A 98 N GLN A 63
SHEET 4 AA2 4 ALA A 102 VAL A 104 -1 O VAL A 104 N LEU A 97
SHEET 1 AA3 5 VAL A 69 ASP A 72 0
SHEET 2 AA3 5 VAL A 62 LEU A 66 -1 N LEU A 64 O TYR A 71
SHEET 3 AA3 5 GLY A 91 VAL A 99 -1 O ASN A 98 N GLN A 63
SHEET 4 AA3 5 ARG A 117 VAL A 124 -1 O VAL A 124 N GLY A 91
SHEET 5 AA3 5 TYR A 111 GLY A 114 -1 N PHE A 112 O GLY A 119
SHEET 1 AA416 VAL A 355 SER A 359 0
SHEET 2 AA416 VAL A 323 GLY A 329 1 N PHE A 324 O VAL A 355
SHEET 3 AA416 TYR A 285 PHE A 289 1 N GLY A 288 O PHE A 325
SHEET 4 AA416 ARG A 260 LEU A 265 1 N GLY A 264 O PHE A 289
SHEET 5 AA416 VAL A 176 GLN A 180 1 N TYR A 178 O ALA A 261
SHEET 6 AA416 LEU A 213 MSE A 216 1 O VAL A 215 N LEU A 177
SHEET 7 AA416 ALA A 154 TYR A 161 -1 N PHE A 159 O MSE A 216
SHEET 8 AA416 LEU A 142 SER A 149 -1 N TYR A 147 O ARG A 156
SHEET 9 AA416 LEU B 141 SER B 149 -1 O GLU B 144 N LEU A 142
SHEET 10 AA416 ALA B 154 THR B 162 -1 O ARG B 156 N TYR B 147
SHEET 11 AA416 LEU B 213 MSE B 216 -1 O MSE B 216 N PHE B 159
SHEET 12 AA416 VAL B 176 GLN B 180 1 N LEU B 177 O VAL B 215
SHEET 13 AA416 ARG B 260 LEU B 265 1 O ALA B 261 N VAL B 176
SHEET 14 AA416 TYR B 285 PHE B 289 1 O PHE B 289 N GLY B 264
SHEET 15 AA416 VAL B 323 GLY B 329 1 O PHE B 325 N TYR B 286
SHEET 16 AA416 VAL B 355 SER B 359 1 O VAL B 355 N PHE B 324
SHEET 1 AA5 5 LYS B 30 PRO B 31 0
SHEET 2 AA5 5 GLN B 43 VAL B 44 -1 O VAL B 44 N LYS B 30
SHEET 3 AA5 5 VAL B 50 SER B 55 -1 O ARG B 51 N GLN B 43
SHEET 4 AA5 5 VAL B 80 GLU B 84 -1 O TRP B 81 N ILE B 54
SHEET 5 AA5 5 THR B 74 LYS B 75 -1 N THR B 74 O THR B 82
SHEET 1 AA6 4 VAL B 69 ASP B 72 0
SHEET 2 AA6 4 VAL B 62 LEU B 66 -1 N LEU B 64 O TYR B 71
SHEET 3 AA6 4 GLY B 91 VAL B 99 -1 O GLN B 96 N ASP B 65
SHEET 4 AA6 4 ALA B 102 VAL B 104 -1 O VAL B 104 N LEU B 97
SHEET 1 AA7 4 VAL B 69 ASP B 72 0
SHEET 2 AA7 4 VAL B 62 LEU B 66 -1 N LEU B 64 O TYR B 71
SHEET 3 AA7 4 GLY B 91 VAL B 99 -1 O GLN B 96 N ASP B 65
SHEET 4 AA7 4 GLY B 121 VAL B 124 -1 O VAL B 124 N GLY B 91
SHEET 1 AA8 2 PHE B 112 GLY B 114 0
SHEET 2 AA8 2 ARG B 117 GLY B 119 -1 O GLY B 119 N PHE B 112
LINK C GLU A 144 N MSE A 145 1555 1555 1.33
LINK C MSE A 145 N ASN A 146 1555 1555 1.33
LINK C PRO A 211 N MSE A 212 1555 1555 1.33
LINK C MSE A 212 N LEU A 213 1555 1555 1.33
LINK C VAL A 215 N MSE A 216 1555 1555 1.33
LINK C MSE A 216 N ASP A 217 1555 1555 1.33
LINK C LEU A 239 N MSE A 240 1555 1555 1.33
LINK C MSE A 240 N ASN A 241 1555 1555 1.33
LINK C PRO A 245 N MSE A 246 1555 1555 1.33
LINK C MSE A 246 N ILE A 247 1555 1555 1.33
LINK C SER A 266 N MSE A 267 1555 1555 1.34
LINK C MSE A 267 N GLY A 268 1555 1555 1.33
LINK C THR A 272 N MSE A 273 1555 1555 1.33
LINK C MSE A 273 N HIS A 274 1555 1555 1.33
LINK C ALA A 276 N MSE A 277 1555 1555 1.33
LINK C MSE A 277 N ASN A 278 1555 1555 1.33
LINK C GLN A 345 N MSE A 346 1555 1555 1.33
LINK C MSE A 346 N MSE A 347 1555 1555 1.33
LINK C MSE A 347 N ASP A 348 1555 1555 1.33
LINK C GLU B 144 N MSE B 145 1555 1555 1.33
LINK C MSE B 145 N ASN B 146 1555 1555 1.33
LINK C PRO B 211 N MSE B 212 1555 1555 1.33
LINK C MSE B 212 N LEU B 213 1555 1555 1.33
LINK C VAL B 215 N MSE B 216 1555 1555 1.33
LINK C MSE B 216 N ASP B 217 1555 1555 1.33
LINK C LEU B 239 N MSE B 240 1555 1555 1.33
LINK C MSE B 240 N ASN B 241 1555 1555 1.33
LINK C PRO B 245 N MSE B 246 1555 1555 1.33
LINK C MSE B 246 N ILE B 247 1555 1555 1.33
LINK C SER B 266 N MSE B 267 1555 1555 1.34
LINK C MSE B 267 N GLY B 268 1555 1555 1.33
LINK C THR B 272 N MSE B 273 1555 1555 1.33
LINK C MSE B 273 N HIS B 274 1555 1555 1.33
LINK C ALA B 276 N MSE B 277 1555 1555 1.33
LINK C MSE B 277 N ASN B 278 1555 1555 1.33
LINK C GLN B 345 N MSE B 346 1555 1555 1.33
LINK C MSE B 346 N MSE B 347 1555 1555 1.33
LINK C MSE B 347 N ASP B 348 1555 1555 1.33
CISPEP 1 TYR A 41 PRO A 42 0 8.76
CISPEP 2 HIS A 334 PRO A 335 0 5.48
CISPEP 3 TYR B 41 PRO B 42 0 8.49
CISPEP 4 TYR B 295 PRO B 296 0 3.95
CISPEP 5 HIS B 334 PRO B 335 0 3.50
SITE 1 AC1 3 TRP A 118 ARG A 157 ARG B 192
SITE 1 AC2 9 GLY A 191 ARG A 192 LYS A 195 ASN A 197
SITE 2 AC2 9 EDO A 405 HOH A 529 HOH A 543 GLU B 144
SITE 3 AC2 9 EDO B 407
SITE 1 AC3 6 ARG A 156 ARG A 157 ASP A 217 ASN A 218
SITE 2 AC3 6 TYR A 220 HOH A 565
SITE 1 AC4 5 SER A 233 PHE A 235 GLU A 236 GLN A 271
SITE 2 AC4 5 HOH A 556
SITE 1 AC5 9 GLU A 33 PHE A 92 PHE A 112 GLU A 123
SITE 2 AC5 9 ARG A 192 LYS A 195 PEG A 402 HOH A 502
SITE 3 AC5 9 HOH A 543
SITE 1 AC6 6 ASP A 128 TYR A 357 ASN A 374 GLU A 375
SITE 2 AC6 6 HOH A 508 HOH A 645
SITE 1 AC7 5 PHE A 131 LYS A 135 ALA A 206 HOH A 532
SITE 2 AC7 5 HOH A 648
SITE 1 AC8 4 GLU A 27 ASP A 28 PHE A 29 HOH A 523
SITE 1 AC9 4 GLU A 144 ASN A 146 ASN B 197 PEG B 403
SITE 1 AD1 4 ARG A 48 GLN A 88 HOH A 501 GLU B 299
SITE 1 AD2 5 HIS A 334 PRO A 335 PRO A 337 GLY A 338
SITE 2 AD2 5 HOH A 630
SITE 1 AD3 6 SER B 233 ILE B 234 PHE B 235 GLU B 236
SITE 2 AD3 6 GLU B 237 GLN B 271
SITE 1 AD4 4 HIS B 334 PRO B 335 PRO B 337 GLY B 338
SITE 1 AD5 8 GLU A 144 EDO A 409 LEU B 142 GLY B 191
SITE 2 AD5 8 ARG B 192 LYS B 195 ASN B 197 PEG B 404
SITE 1 AD6 8 GLU B 33 VAL B 34 PHE B 112 GLU B 123
SITE 2 AD6 8 ARG B 192 LYS B 195 ARG B 370 PEG B 403
SITE 1 AD7 4 TYR B 166 LYS B 250 ARG B 252 HOH B 519
SITE 1 AD8 4 PRO A 37 GLU B 185 ASP B 186 ASN B 218
SITE 1 AD9 5 ASN A 197 PEG A 402 GLU B 144 ASN B 146
SITE 2 AD9 5 ARG B 157
SITE 1 AE1 5 ASP B 128 TYR B 357 ASN B 374 GLU B 375
SITE 2 AE1 5 HOH B 657
SITE 1 AE2 4 LEU B 203 HOH B 503 HOH B 511 HOH B 621
SITE 1 AE3 7 SER B 266 MSE B 267 ASN B 270 SER B 290
SITE 2 AE3 7 TYR B 295 PHE B 336 HOH B 501
CRYST1 116.703 126.553 110.260 90.00 90.00 90.00 C 2 2 21 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 0.008569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009069 0.00000
TER 5404 LYS A 382
TER 10903 LYS B 382
MASTER 472 0 42 21 45 0 36 6 6159 2 600 60
END |