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1fat.pdb
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HEADER LECTIN 12-JUN-96 1FAT
TITLE PHYTOHEMAGGLUTININ-L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHYTOHEMAGGLUTININ-L;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: LEUCOAGGLUTINATING PHYTOHEMAGGLUTININ, PHA-L
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHASEOLUS VULGARIS;
SOURCE 3 ORGANISM_TAXID: 3885;
SOURCE 4 ORGAN: SEED;
SOURCE 5 OTHER_DETAILS: PURIFIED PHA-L WAS PURCHASED FROM SIGMA
KEYWDS GLYCOPROTEIN, PLANT DEFENSE PROTEIN, LECTIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HAMELRYCK,R.LORIS
REVDAT 3 13-JUL-11 1FAT 1 VERSN
REVDAT 2 24-FEB-09 1FAT 1 VERSN
REVDAT 1 23-DEC-96 1FAT 0
JRNL AUTH T.W.HAMELRYCK,M.H.DAO-THI,F.POORTMANS,M.J.CHRISPEELS,L.WYNS,
JRNL AUTH 2 R.LORIS
JRNL TITL THE CRYSTALLOGRAPHIC STRUCTURE OF PHYTOHEMAGGLUTININ-L.
JRNL REF J.BIOL.CHEM. V. 271 20479 1996
JRNL REFN ISSN 0021-9258
JRNL PMID 8702788
JRNL DOI 10.1074/JBC.271.34.20479
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.H.DAO-THI,T.W.HAMELRYCK,F.POORTMANS,T.A.VOELKER,
REMARK 1 AUTH 2 M.J.CHRISPEELS,L.WYNS
REMARK 1 TITL CRYSTALLIZATION OF GLYCOSYLATED AND NONGLYCOSYLATED
REMARK 1 TITL 2 PHYTOHEMAGGLUTININ-L
REMARK 1 REF PROTEINS V. 24 134 1996
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.J.CHRISPEELS,N.V.RAIKHEL
REMARK 1 TITL LECTINS, LECTIN GENES, AND THEIR ROLE IN PLANT DEFENSE
REMARK 1 REF PLANT CELL V. 3 1 1991
REMARK 1 REFN ISSN 1040-4651
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.M.HOFFMAN,D.D.DONALDSON
REMARK 1 TITL CHARACTERIZATION OF TWO PHASEOLUS VULGARIS
REMARK 1 TITL 2 PHYTOHEMAGGLUTININ GENES CLOSELY LINKED ON THE CHROMOSOME
REMARK 1 REF EMBO J. V. 4 883 1985
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 67416
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : A POSTERIORI R-FREE FACTOR
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2758
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.94
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1832
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 299
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7168
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.34
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.01
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.16
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.71
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : MONOMERS A, B, C, D
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; 300
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; 1.0
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FAT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 53.15000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.15000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 60.60000
REMARK 290 SMTRY3 4 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 300 REMARK: PHYTOHEMAGGLUTININ-L IS A HOMOTETRAMER WITH 222 SYMMETRY.
REMARK 300 EACH SUBUNIT CONSISTS OF 252 RESIDUES. THE FOUR SUBUNITS
REMARK 300 HAVE CHAIN IDENTIFIERS A, B, C, AND D IN THIS ENTRY.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A 37
REMARK 465 ASP A 234
REMARK 465 GLU A 235
REMARK 465 THR A 236
REMARK 465 THR A 237
REMARK 465 SER A 238
REMARK 465 GLU A 239
REMARK 465 GLY A 240
REMARK 465 LEU A 241
REMARK 465 ASN A 242
REMARK 465 LEU A 243
REMARK 465 ALA A 244
REMARK 465 ASN A 245
REMARK 465 LEU A 246
REMARK 465 VAL A 247
REMARK 465 LEU A 248
REMARK 465 ASN A 249
REMARK 465 LYS A 250
REMARK 465 ILE A 251
REMARK 465 LEU A 252
REMARK 465 ASP B 234
REMARK 465 GLU B 235
REMARK 465 THR B 236
REMARK 465 THR B 237
REMARK 465 SER B 238
REMARK 465 GLU B 239
REMARK 465 GLY B 240
REMARK 465 LEU B 241
REMARK 465 ASN B 242
REMARK 465 LEU B 243
REMARK 465 ALA B 244
REMARK 465 ASN B 245
REMARK 465 LEU B 246
REMARK 465 VAL B 247
REMARK 465 LEU B 248
REMARK 465 ASN B 249
REMARK 465 LYS B 250
REMARK 465 ILE B 251
REMARK 465 LEU B 252
REMARK 465 GLY C 37
REMARK 465 ASP C 234
REMARK 465 GLU C 235
REMARK 465 THR C 236
REMARK 465 THR C 237
REMARK 465 SER C 238
REMARK 465 GLU C 239
REMARK 465 GLY C 240
REMARK 465 LEU C 241
REMARK 465 ASN C 242
REMARK 465 LEU C 243
REMARK 465 ALA C 244
REMARK 465 ASN C 245
REMARK 465 LEU C 246
REMARK 465 VAL C 247
REMARK 465 LEU C 248
REMARK 465 ASN C 249
REMARK 465 LYS C 250
REMARK 465 ILE C 251
REMARK 465 LEU C 252
REMARK 465 ASN D 36
REMARK 465 GLY D 37
REMARK 465 ASP D 234
REMARK 465 GLU D 235
REMARK 465 THR D 236
REMARK 465 THR D 237
REMARK 465 SER D 238
REMARK 465 GLU D 239
REMARK 465 GLY D 240
REMARK 465 LEU D 241
REMARK 465 ASN D 242
REMARK 465 LEU D 243
REMARK 465 ALA D 244
REMARK 465 ASN D 245
REMARK 465 LEU D 246
REMARK 465 VAL D 247
REMARK 465 LEU D 248
REMARK 465 ASN D 249
REMARK 465 LYS D 250
REMARK 465 ILE D 251
REMARK 465 LEU D 252
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 10 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 LYS B 215 CD - CE - NZ ANGL. DEV. = -15.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 2 70.07 -152.06
REMARK 500 ARG A 20 -126.28 60.15
REMARK 500 ASN A 34 176.60 -60.00
REMARK 500 ALA A 85 141.88 -179.15
REMARK 500 SER A 97 131.27 -38.16
REMARK 500 LYS A 100 -141.34 -110.59
REMARK 500 LEU A 106 16.82 53.38
REMARK 500 TRP A 131 -13.44 -153.34
REMARK 500 ASN A 172 19.10 54.63
REMARK 500 LYS A 215 -69.06 -9.15
REMARK 500 ASN B 2 70.36 -153.90
REMARK 500 ARG B 20 -129.23 56.93
REMARK 500 ALA B 85 140.59 -179.40
REMARK 500 LYS B 100 -139.09 -110.78
REMARK 500 LEU B 106 18.09 53.74
REMARK 500 LYS B 129 -50.19 -29.68
REMARK 500 TRP B 131 -15.86 -154.61
REMARK 500 LYS B 215 -71.27 -8.61
REMARK 500 ASN C 2 72.18 -151.83
REMARK 500 ARG C 20 -124.91 57.00
REMARK 500 ASN C 34 178.01 -59.96
REMARK 500 ALA C 85 142.65 179.74
REMARK 500 SER C 97 131.04 -39.31
REMARK 500 LYS C 100 -138.88 -109.65
REMARK 500 LEU C 106 12.11 54.35
REMARK 500 TRP C 131 -17.98 -151.79
REMARK 500 ASN C 172 18.01 58.36
REMARK 500 LYS C 215 -63.60 -9.03
REMARK 500 ASN D 2 73.57 -152.64
REMARK 500 ARG D 20 -125.78 58.72
REMARK 500 ALA D 85 141.76 -179.14
REMARK 500 LYS D 100 -141.37 -111.48
REMARK 500 LEU D 106 13.27 54.12
REMARK 500 TRP D 131 -19.05 -152.38
REMARK 500 LYS D 215 -64.88 -7.76
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 THR A 14 24.0 L L OUTSIDE RANGE
REMARK 500 VAL A 95 21.9 L L OUTSIDE RANGE
REMARK 500 VAL B 95 21.9 L L OUTSIDE RANGE
REMARK 500 THR C 14 24.4 L L OUTSIDE RANGE
REMARK 500 SER C 52 24.3 L L OUTSIDE RANGE
REMARK 500 VAL C 95 22.3 L L OUTSIDE RANGE
REMARK 500 THR D 14 24.7 L L OUTSIDE RANGE
REMARK 500 VAL D 95 22.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 PHYTOHEMAGGLUTININ-L IS A GLYCOPROTEIN. IT CONTAINS ONE HI
REMARK 600 MANNOSE TYPE AND ONE COMPLEX TYPE SUGAR PER MONOMER. ONLY
REMARK 600 GLCNAC RESIDUE OF THE MANNOSE TYPE SUGAR ATTACHED TO ASN 12
REMARK 600 IS VISIBLE IN THE ELECTRON DENSITY. NO INTERPRETABLE
REMARK 600 DENSITY IS OBSERVED FOR THE COMPLEX TYPE SUGAR ATTACHED TO
REMARK 600 ASN 60.
REMARK 600
REMARK 600 EACH MONOMER HAS A BOUND CALCIUM AND MANGANESE
REMARK 600 ATOM. THE CALCIUM AND MANGANESE IONS ARE ESSENTIAL FOR
REMARK 600 STABILIZING AN UNUSUAL ALA-ASP CIS PEPTIDE BOND THAT IS AN
REMARK 600 ESSENTIAL FEATURE OF THE CARBOHYDRATE RECOGNITION SITE OF
REMARK 600 THIS LECTIN. THESE SITES ARE PRESENTED ON *SITE* RECORDS
REMARK 600 BELOW.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 254 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 122 OE2
REMARK 620 2 ASP A 124 OD2 91.1
REMARK 620 3 HIS A 137 NE2 96.0 78.9
REMARK 620 4 ASP A 132 OD1 170.6 83.0 90.1
REMARK 620 5 HOH A 307 O 85.9 81.9 160.8 86.1
REMARK 620 6 HOH A 308 O 97.5 169.7 94.5 89.1 104.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 255 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 124 OD1
REMARK 620 2 ASN A 128 OD1 158.0
REMARK 620 3 LEU A 126 O 71.7 87.1
REMARK 620 4 ASP A 124 OD2 55.0 129.4 105.9
REMARK 620 5 ASP A 132 OD2 91.2 75.2 68.7 65.6
REMARK 620 6 HOH A 306 O 75.6 107.5 81.0 122.6 149.5
REMARK 620 7 HOH A 305 O 110.2 88.6 164.4 65.8 95.7 114.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 254 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 122 OE2
REMARK 620 2 ASP B 132 OD1 158.3
REMARK 620 3 HIS B 137 NE2 98.9 94.6
REMARK 620 4 ASP B 124 OD2 83.5 81.0 84.5
REMARK 620 5 HOH B 304 O 95.8 97.3 103.8 171.7
REMARK 620 6 HOH B 303 O 84.2 76.5 155.0 71.2 100.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 255 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 124 OD1
REMARK 620 2 LEU B 126 O 75.7
REMARK 620 3 ASN B 128 OD1 165.9 90.3
REMARK 620 4 ASP B 132 OD2 100.0 76.0 77.0
REMARK 620 5 HOH B 302 O 112.3 167.4 81.7 92.7
REMARK 620 6 HOH B 301 O 70.3 81.9 107.4 157.6 109.6
REMARK 620 7 ASP B 124 OD2 54.1 113.2 135.5 73.3 67.6 112.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 254 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 122 OE2
REMARK 620 2 ASP C 124 OD2 91.1
REMARK 620 3 HIS C 137 NE2 102.6 90.3
REMARK 620 4 ASP C 132 OD1 155.0 84.3 102.0
REMARK 620 5 HOH C 315 O 72.2 90.1 174.8 83.2
REMARK 620 6 HOH C 316 O 98.2 156.5 108.4 78.1 72.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 255 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 128 OD1
REMARK 620 2 ASP C 124 OD2 133.9
REMARK 620 3 HOH C 313 O 85.5 63.0
REMARK 620 4 LEU C 126 O 92.3 100.1 151.3
REMARK 620 5 ASP C 132 OD2 78.4 65.9 83.2 68.3
REMARK 620 6 HOH C 314 O 126.7 94.1 102.4 101.9 154.4
REMARK 620 7 ASP C 124 OD1 163.7 49.3 106.7 71.8 92.0 62.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 254 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 122 OE2
REMARK 620 2 ASP D 124 OD2 88.0
REMARK 620 3 ASP D 132 OD1 173.4 88.8
REMARK 620 4 HIS D 137 NE2 86.0 77.9 87.6
REMARK 620 5 HOH D 312 O 94.3 153.1 85.9 75.5
REMARK 620 6 HOH D 311 O 87.5 75.2 97.3 152.5 131.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 255 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 124 OD2
REMARK 620 2 ASN D 128 OD1 141.0
REMARK 620 3 ASP D 132 OD2 72.1 77.9
REMARK 620 4 HOH D 309 O 110.9 105.3 162.2
REMARK 620 5 HOH D 310 O 79.2 76.5 90.4 107.4
REMARK 620 6 LEU D 126 O 108.5 84.7 71.9 90.8 156.6
REMARK 620 7 ASP D 124 OD1 55.4 155.5 97.5 72.2 127.9 71.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE IN CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: MNA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MANGANESE BINDING SITE IN CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE IN CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: MNB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MANGANESE BINDING SITE IN CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE IN CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: MNC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MANGANESE BINDING SITE IN CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE IN CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: MND
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MANGANESE BINDING SITE IN CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 255
DBREF 1FAT A 1 252 UNP P05087 PHAL_PHAVU 21 272
DBREF 1FAT B 1 252 UNP P05087 PHAL_PHAVU 21 272
DBREF 1FAT C 1 252 UNP P05087 PHAL_PHAVU 21 272
DBREF 1FAT D 1 252 UNP P05087 PHAL_PHAVU 21 272
SEQADV 1FAT GLU A 235 UNP P05087 GLY 255 CONFLICT
SEQADV 1FAT GLU B 235 UNP P05087 GLY 255 CONFLICT
SEQADV 1FAT GLU C 235 UNP P05087 GLY 255 CONFLICT
SEQADV 1FAT GLU D 235 UNP P05087 GLY 255 CONFLICT
SEQRES 1 A 252 SER ASN ASP ILE TYR PHE ASN PHE GLN ARG PHE ASN GLU
SEQRES 2 A 252 THR ASN LEU ILE LEU GLN ARG ASP ALA SER VAL SER SER
SEQRES 3 A 252 SER GLY GLN LEU ARG LEU THR ASN LEU ASN GLY ASN GLY
SEQRES 4 A 252 GLU PRO ARG VAL GLY SER LEU GLY ARG ALA PHE TYR SER
SEQRES 5 A 252 ALA PRO ILE GLN ILE TRP ASP ASN THR THR GLY THR VAL
SEQRES 6 A 252 ALA SER PHE ALA THR SER PHE THR PHE ASN ILE GLN VAL
SEQRES 7 A 252 PRO ASN ASN ALA GLY PRO ALA ASP GLY LEU ALA PHE ALA
SEQRES 8 A 252 LEU VAL PRO VAL GLY SER GLN PRO LYS ASP LYS GLY GLY
SEQRES 9 A 252 PHE LEU GLY LEU PHE ASP GLY SER ASN SER ASN PHE HIS
SEQRES 10 A 252 THR VAL ALA VAL GLU PHE ASP THR LEU TYR ASN LYS ASP
SEQRES 11 A 252 TRP ASP PRO THR GLU ARG HIS ILE GLY ILE ASP VAL ASN
SEQRES 12 A 252 SER ILE ARG SER ILE LYS THR THR ARG TRP ASP PHE VAL
SEQRES 13 A 252 ASN GLY GLU ASN ALA GLU VAL LEU ILE THR TYR ASP SER
SEQRES 14 A 252 SER THR ASN LEU LEU VAL ALA SER LEU VAL TYR PRO SER
SEQRES 15 A 252 GLN LYS THR SER PHE ILE VAL SER ASP THR VAL ASP LEU
SEQRES 16 A 252 LYS SER VAL LEU PRO GLU TRP VAL SER VAL GLY PHE SER
SEQRES 17 A 252 ALA THR THR GLY ILE ASN LYS GLY ASN VAL GLU THR ASN
SEQRES 18 A 252 ASP VAL LEU SER TRP SER PHE ALA SER LYS LEU SER ASP
SEQRES 19 A 252 GLU THR THR SER GLU GLY LEU ASN LEU ALA ASN LEU VAL
SEQRES 20 A 252 LEU ASN LYS ILE LEU
SEQRES 1 B 252 SER ASN ASP ILE TYR PHE ASN PHE GLN ARG PHE ASN GLU
SEQRES 2 B 252 THR ASN LEU ILE LEU GLN ARG ASP ALA SER VAL SER SER
SEQRES 3 B 252 SER GLY GLN LEU ARG LEU THR ASN LEU ASN GLY ASN GLY
SEQRES 4 B 252 GLU PRO ARG VAL GLY SER LEU GLY ARG ALA PHE TYR SER
SEQRES 5 B 252 ALA PRO ILE GLN ILE TRP ASP ASN THR THR GLY THR VAL
SEQRES 6 B 252 ALA SER PHE ALA THR SER PHE THR PHE ASN ILE GLN VAL
SEQRES 7 B 252 PRO ASN ASN ALA GLY PRO ALA ASP GLY LEU ALA PHE ALA
SEQRES 8 B 252 LEU VAL PRO VAL GLY SER GLN PRO LYS ASP LYS GLY GLY
SEQRES 9 B 252 PHE LEU GLY LEU PHE ASP GLY SER ASN SER ASN PHE HIS
SEQRES 10 B 252 THR VAL ALA VAL GLU PHE ASP THR LEU TYR ASN LYS ASP
SEQRES 11 B 252 TRP ASP PRO THR GLU ARG HIS ILE GLY ILE ASP VAL ASN
SEQRES 12 B 252 SER ILE ARG SER ILE LYS THR THR ARG TRP ASP PHE VAL
SEQRES 13 B 252 ASN GLY GLU ASN ALA GLU VAL LEU ILE THR TYR ASP SER
SEQRES 14 B 252 SER THR ASN LEU LEU VAL ALA SER LEU VAL TYR PRO SER
SEQRES 15 B 252 GLN LYS THR SER PHE ILE VAL SER ASP THR VAL ASP LEU
SEQRES 16 B 252 LYS SER VAL LEU PRO GLU TRP VAL SER VAL GLY PHE SER
SEQRES 17 B 252 ALA THR THR GLY ILE ASN LYS GLY ASN VAL GLU THR ASN
SEQRES 18 B 252 ASP VAL LEU SER TRP SER PHE ALA SER LYS LEU SER ASP
SEQRES 19 B 252 GLU THR THR SER GLU GLY LEU ASN LEU ALA ASN LEU VAL
SEQRES 20 B 252 LEU ASN LYS ILE LEU
SEQRES 1 C 252 SER ASN ASP ILE TYR PHE ASN PHE GLN ARG PHE ASN GLU
SEQRES 2 C 252 THR ASN LEU ILE LEU GLN ARG ASP ALA SER VAL SER SER
SEQRES 3 C 252 SER GLY GLN LEU ARG LEU THR ASN LEU ASN GLY ASN GLY
SEQRES 4 C 252 GLU PRO ARG VAL GLY SER LEU GLY ARG ALA PHE TYR SER
SEQRES 5 C 252 ALA PRO ILE GLN ILE TRP ASP ASN THR THR GLY THR VAL
SEQRES 6 C 252 ALA SER PHE ALA THR SER PHE THR PHE ASN ILE GLN VAL
SEQRES 7 C 252 PRO ASN ASN ALA GLY PRO ALA ASP GLY LEU ALA PHE ALA
SEQRES 8 C 252 LEU VAL PRO VAL GLY SER GLN PRO LYS ASP LYS GLY GLY
SEQRES 9 C 252 PHE LEU GLY LEU PHE ASP GLY SER ASN SER ASN PHE HIS
SEQRES 10 C 252 THR VAL ALA VAL GLU PHE ASP THR LEU TYR ASN LYS ASP
SEQRES 11 C 252 TRP ASP PRO THR GLU ARG HIS ILE GLY ILE ASP VAL ASN
SEQRES 12 C 252 SER ILE ARG SER ILE LYS THR THR ARG TRP ASP PHE VAL
SEQRES 13 C 252 ASN GLY GLU ASN ALA GLU VAL LEU ILE THR TYR ASP SER
SEQRES 14 C 252 SER THR ASN LEU LEU VAL ALA SER LEU VAL TYR PRO SER
SEQRES 15 C 252 GLN LYS THR SER PHE ILE VAL SER ASP THR VAL ASP LEU
SEQRES 16 C 252 LYS SER VAL LEU PRO GLU TRP VAL SER VAL GLY PHE SER
SEQRES 17 C 252 ALA THR THR GLY ILE ASN LYS GLY ASN VAL GLU THR ASN
SEQRES 18 C 252 ASP VAL LEU SER TRP SER PHE ALA SER LYS LEU SER ASP
SEQRES 19 C 252 GLU THR THR SER GLU GLY LEU ASN LEU ALA ASN LEU VAL
SEQRES 20 C 252 LEU ASN LYS ILE LEU
SEQRES 1 D 252 SER ASN ASP ILE TYR PHE ASN PHE GLN ARG PHE ASN GLU
SEQRES 2 D 252 THR ASN LEU ILE LEU GLN ARG ASP ALA SER VAL SER SER
SEQRES 3 D 252 SER GLY GLN LEU ARG LEU THR ASN LEU ASN GLY ASN GLY
SEQRES 4 D 252 GLU PRO ARG VAL GLY SER LEU GLY ARG ALA PHE TYR SER
SEQRES 5 D 252 ALA PRO ILE GLN ILE TRP ASP ASN THR THR GLY THR VAL
SEQRES 6 D 252 ALA SER PHE ALA THR SER PHE THR PHE ASN ILE GLN VAL
SEQRES 7 D 252 PRO ASN ASN ALA GLY PRO ALA ASP GLY LEU ALA PHE ALA
SEQRES 8 D 252 LEU VAL PRO VAL GLY SER GLN PRO LYS ASP LYS GLY GLY
SEQRES 9 D 252 PHE LEU GLY LEU PHE ASP GLY SER ASN SER ASN PHE HIS
SEQRES 10 D 252 THR VAL ALA VAL GLU PHE ASP THR LEU TYR ASN LYS ASP
SEQRES 11 D 252 TRP ASP PRO THR GLU ARG HIS ILE GLY ILE ASP VAL ASN
SEQRES 12 D 252 SER ILE ARG SER ILE LYS THR THR ARG TRP ASP PHE VAL
SEQRES 13 D 252 ASN GLY GLU ASN ALA GLU VAL LEU ILE THR TYR ASP SER
SEQRES 14 D 252 SER THR ASN LEU LEU VAL ALA SER LEU VAL TYR PRO SER
SEQRES 15 D 252 GLN LYS THR SER PHE ILE VAL SER ASP THR VAL ASP LEU
SEQRES 16 D 252 LYS SER VAL LEU PRO GLU TRP VAL SER VAL GLY PHE SER
SEQRES 17 D 252 ALA THR THR GLY ILE ASN LYS GLY ASN VAL GLU THR ASN
SEQRES 18 D 252 ASP VAL LEU SER TRP SER PHE ALA SER LYS LEU SER ASP
SEQRES 19 D 252 GLU THR THR SER GLU GLY LEU ASN LEU ALA ASN LEU VAL
SEQRES 20 D 252 LEU ASN LYS ILE LEU
MODRES 1FAT ASN A 12 ASN GLYCOSYLATION SITE
MODRES 1FAT ASN B 12 ASN GLYCOSYLATION SITE
MODRES 1FAT ASN C 12 ASN GLYCOSYLATION SITE
MODRES 1FAT ASN D 12 ASN GLYCOSYLATION SITE
HET NAG A 253 14
HET NAG B 253 14
HET NAG C 253 14
HET NAG D 253 14
HET MN A 254 1
HET CA A 255 1
HET MN B 254 1
HET CA B 255 1
HET MN C 254 1
HET CA C 255 1
HET MN D 254 1
HET CA D 255 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MN MANGANESE (II) ION
HETNAM CA CALCIUM ION
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 9 MN 4(MN 2+)
FORMUL 10 CA 4(CA 2+)
FORMUL 17 HOH *16(H2 O)
HELIX 1 1 GLU A 13 ASN A 15 5 3
HELIX 2 2 GLY A 103 PHE A 105 5 3
HELIX 3 3 LEU A 195 VAL A 198 1 4
HELIX 4 4 GLU B 13 ASN B 15 5 3
HELIX 5 5 GLY B 103 PHE B 105 5 3
HELIX 6 6 LEU B 195 VAL B 198 1 4
HELIX 7 7 GLU C 13 ASN C 15 5 3
HELIX 8 8 GLY C 103 PHE C 105 5 3
HELIX 9 9 LEU C 195 VAL C 198 1 4
HELIX 10 10 GLU D 13 ASN D 15 5 3
HELIX 11 11 GLY D 103 PHE D 105 5 3
HELIX 12 12 LEU D 195 VAL D 198 1 4
SHEET 1 A12 THR A 185 THR A 192 0
SHEET 2 A12 LEU A 173 TYR A 180 -1 N TYR A 180 O THR A 185
SHEET 3 A12 ASN A 160 ASP A 168 -1 N ASP A 168 O LEU A 173
SHEET 4 A12 ALA A 66 GLN A 77 -1 N PHE A 74 O ALA A 161
SHEET 5 A12 THR A 220 LEU A 232 -1 N LYS A 231 O SER A 67
SHEET 6 A12 ASN A 2 PHE A 8 -1 N PHE A 8 O TRP A 226
SHEET 7 A12 ASN B 2 PHE B 8 -1 N ASN B 7 O ASP A 3
SHEET 8 A12 ASP B 222 LEU B 232 -1 N SER B 230 O ILE B 4
SHEET 9 A12 ALA B 66 ASN B 75 -1 N ASN B 75 O ASP B 222
SHEET 10 A12 ASN B 160 ASP B 168 -1 N TYR B 167 O PHE B 68
SHEET 11 A12 LEU B 173 TYR B 180 -1 N VAL B 179 O GLU B 162
SHEET 12 A12 THR B 185 THR B 192 -1 N ASP B 191 O LEU B 174
SHEET 1 B 7 LEU A 16 ARG A 20 0
SHEET 2 B 7 LEU A 46 TYR A 51 -1 N PHE A 50 O ILE A 17
SHEET 3 B 7 VAL A 203 THR A 211 -1 N ALA A 209 O GLY A 47
SHEET 4 B 7 ASP A 86 PRO A 94 -1 N VAL A 93 O SER A 204
SHEET 5 B 7 VAL A 119 ASP A 124 -1 N PHE A 123 O LEU A 88
SHEET 6 B 7 HIS A 137 VAL A 142 -1 N ASP A 141 O ALA A 120
SHEET 7 B 7 LYS A 149 ARG A 152 -1 N THR A 151 O ILE A 138
SHEET 1 C 7 LEU B 16 ARG B 20 0
SHEET 2 C 7 LEU B 46 TYR B 51 -1 N PHE B 50 O ILE B 17
SHEET 3 C 7 VAL B 203 THR B 211 -1 N ALA B 209 O GLY B 47
SHEET 4 C 7 ASP B 86 PRO B 94 -1 N VAL B 93 O SER B 204
SHEET 5 C 7 VAL B 119 ASP B 124 -1 N PHE B 123 O LEU B 88
SHEET 6 C 7 HIS B 137 VAL B 142 -1 N ASP B 141 O ALA B 120
SHEET 7 C 7 LYS B 149 ARG B 152 -1 N THR B 151 O ILE B 138
SHEET 1 D12 THR D 185 THR D 192 0
SHEET 2 D12 LEU D 173 TYR D 180 -1 N TYR D 180 O THR D 185
SHEET 3 D12 ASN D 160 ASP D 168 -1 N ASP D 168 O LEU D 173
SHEET 4 D12 SER D 67 ASN D 75 -1 N PHE D 74 O ALA D 161
SHEET 5 D12 ASP D 222 LYS D 231 -1 N LYS D 231 O SER D 67
SHEET 6 D12 ASN D 2 PHE D 8 -1 N PHE D 8 O TRP D 226
SHEET 7 D12 ASP C 3 PHE C 8 -1 N ASN C 7 O ASP D 3
SHEET 8 D12 THR C 220 LEU C 232 -1 N SER C 230 O ILE C 4
SHEET 9 D12 ALA C 66 GLN C 77 -1 N GLN C 77 O THR C 220
SHEET 10 D12 ASN C 160 ASP C 168 -1 N TYR C 167 O PHE C 68
SHEET 11 D12 LEU C 173 TYR C 180 -1 N VAL C 179 O GLU C 162
SHEET 12 D12 THR C 185 THR C 192 -1 N ASP C 191 O LEU C 174
SHEET 1 E 7 LEU C 16 ARG C 20 0
SHEET 2 E 7 LEU C 46 TYR C 51 -1 N PHE C 50 O ILE C 17
SHEET 3 E 7 VAL C 203 THR C 211 -1 N ALA C 209 O GLY C 47
SHEET 4 E 7 ASP C 86 PRO C 94 -1 N VAL C 93 O SER C 204
SHEET 5 E 7 VAL C 119 ASP C 124 -1 N PHE C 123 O LEU C 88
SHEET 6 E 7 HIS C 137 VAL C 142 -1 N ASP C 141 O ALA C 120
SHEET 7 E 7 LYS C 149 ARG C 152 -1 N THR C 151 O ILE C 138
SHEET 1 F 7 LEU D 16 ARG D 20 0
SHEET 2 F 7 LEU D 46 TYR D 51 -1 N PHE D 50 O ILE D 17
SHEET 3 F 7 VAL D 203 THR D 211 -1 N ALA D 209 O GLY D 47
SHEET 4 F 7 ASP D 86 PRO D 94 -1 N VAL D 93 O SER D 204
SHEET 5 F 7 VAL D 119 ASP D 124 -1 N PHE D 123 O LEU D 88
SHEET 6 F 7 HIS D 137 VAL D 142 -1 N ASP D 141 O ALA D 120
SHEET 7 F 7 LYS D 149 ARG D 152 -1 N THR D 151 O ILE D 138
LINK C1 NAG A 253 ND2 ASN A 12 1555 1555 1.45
LINK MN MN A 254 OE2 GLU A 122 1555 1555 2.05
LINK MN MN A 254 OD2 ASP A 124 1555 1555 2.30
LINK MN MN A 254 NE2 HIS A 137 1555 1555 2.14
LINK CA CA A 255 OD1 ASP A 124 1555 1555 2.32
LINK CA CA A 255 OD1 ASN A 128 1555 1555 2.21
LINK C1 NAG B 253 ND2 ASN B 12 1555 1555 1.48
LINK MN MN B 254 OE2 GLU B 122 1555 1555 2.15
LINK MN MN B 254 OD1 ASP B 132 1555 1555 2.33
LINK MN MN B 254 NE2 HIS B 137 1555 1555 2.01
LINK CA CA B 255 OD1 ASP B 124 1555 1555 2.38
LINK CA CA B 255 O LEU B 126 1555 1555 2.31
LINK CA CA B 255 OD1 ASN B 128 1555 1555 2.09
LINK CA CA B 255 OD2 ASP B 132 1555 1555 2.31
LINK C1 NAG C 253 ND2 ASN C 12 1555 1555 1.45
LINK MN MN C 254 OE2 GLU C 122 1555 1555 2.22
LINK MN MN C 254 OD2 ASP C 124 1555 1555 2.25
LINK MN MN C 254 NE2 HIS C 137 1555 1555 1.82
LINK CA CA C 255 OD1 ASN C 128 1555 1555 1.87
LINK C1 NAG D 253 ND2 ASN D 12 1555 1555 1.43
LINK MN MN D 254 OE2 GLU D 122 1555 1555 2.20
LINK MN MN D 254 OD2 ASP D 124 1555 1555 2.28
LINK MN MN D 254 OD1 ASP D 132 1555 1555 2.32
LINK CA CA D 255 OD2 ASP D 124 1555 1555 2.40
LINK CA CA D 255 OD1 ASN D 128 1555 1555 2.13
LINK CA CA D 255 OD2 ASP D 132 1555 1555 2.39
LINK MN MN A 254 OD1 ASP A 132 1555 1555 2.44
LINK MN MN A 254 O HOH A 307 1555 1555 1.70
LINK MN MN A 254 O HOH A 308 1555 1555 1.46
LINK CA CA A 255 O LEU A 126 1555 1555 2.45
LINK CA CA A 255 OD2 ASP A 124 1555 1555 2.49
LINK CA CA A 255 OD2 ASP A 132 1555 1555 2.55
LINK CA CA A 255 O HOH A 306 1555 1555 1.99
LINK CA CA A 255 O HOH A 305 1555 1555 2.43
LINK MN MN B 254 OD2 ASP B 124 1555 1555 2.49
LINK MN MN B 254 O HOH B 304 1555 1555 1.46
LINK MN MN B 254 O HOH B 303 1555 1555 2.01
LINK CA CA B 255 O HOH B 302 1555 1555 2.33
LINK CA CA B 255 O HOH B 301 1555 1555 1.69
LINK CA CA B 255 OD2 ASP B 124 1555 1555 2.49
LINK MN MN C 254 OD1 ASP C 132 1555 1555 2.42
LINK MN MN C 254 O HOH C 315 1555 1555 2.39
LINK MN MN C 254 O HOH C 316 1555 1555 1.55
LINK CA CA C 255 OD2 ASP C 124 1555 1555 2.66
LINK CA CA C 255 O HOH C 313 1555 1555 2.68
LINK CA CA C 255 O LEU C 126 1555 1555 2.49
LINK CA CA C 255 OD2 ASP C 132 1555 1555 2.45
LINK CA CA C 255 O HOH C 314 1555 1555 2.00
LINK CA CA C 255 OD1 ASP C 124 1555 1555 2.66
LINK MN MN D 254 NE2 HIS D 137 1555 1555 2.41
LINK MN MN D 254 O HOH D 312 1555 1555 1.52
LINK MN MN D 254 O HOH D 311 1555 1555 1.50
LINK CA CA D 255 O HOH D 309 1555 1555 2.05
LINK CA CA D 255 O HOH D 310 1555 1555 2.66
LINK CA CA D 255 O LEU D 126 1555 1555 2.53
LINK CA CA D 255 OD1 ASP D 124 1555 1555 2.45
CISPEP 1 ALA A 85 ASP A 86 0 -0.04
CISPEP 2 ALA B 85 ASP B 86 0 0.19
CISPEP 3 ALA C 85 ASP C 86 0 -0.14
CISPEP 4 ALA D 85 ASP D 86 0 0.24
SITE 1 CAA 4 ASP A 124 LEU A 126 ASN A 128 ASP A 132
SITE 1 MNA 4 GLU A 122 ASP A 124 ASP A 132 HIS A 137
SITE 1 CAB 4 ASP B 124 LEU B 126 ASN B 128 ASP B 132
SITE 1 MNB 4 GLU B 122 ASP B 124 ASP B 132 HIS B 137
SITE 1 CAC 4 ASP C 124 LEU C 126 ASN C 128 ASP C 132
SITE 1 MNC 4 GLU C 122 ASP C 124 ASP C 132 HIS C 137
SITE 1 CAD 4 ASP D 124 LEU D 126 ASN D 128 ASP D 132
SITE 1 MND 4 GLU D 122 ASP D 124 ASP D 132 HIS D 137
SITE 1 AC1 6 ARG A 10 ASN A 12 GLU A 13 VAL A 24
SITE 2 AC1 6 SER A 25 TRP B 202
SITE 1 AC2 5 ARG B 10 ASN B 12 GLU B 13 VAL B 24
SITE 2 AC2 5 SER B 25
SITE 1 AC3 7 ARG C 10 ASN C 12 GLU C 13 VAL C 24
SITE 2 AC3 7 SER C 25 GLU D 201 TRP D 202
SITE 1 AC4 7 GLU C 201 TRP C 202 ARG D 10 ASN D 12
SITE 2 AC4 7 GLU D 13 VAL D 24 SER D 25
SITE 1 AC5 7 GLU A 122 ASP A 124 ASP A 132 HIS A 137
SITE 2 AC5 7 SER A 147 HOH A 307 HOH A 308
SITE 1 AC6 6 ASP A 124 LEU A 126 ASN A 128 ASP A 132
SITE 2 AC6 6 HOH A 305 HOH A 306
SITE 1 AC7 7 GLU B 122 ASP B 124 ASP B 132 HIS B 137
SITE 2 AC7 7 SER B 147 HOH B 303 HOH B 304
SITE 1 AC8 6 ASP B 124 LEU B 126 ASN B 128 ASP B 132
SITE 2 AC8 6 HOH B 301 HOH B 302
SITE 1 AC9 6 GLU C 122 ASP C 124 ASP C 132 HIS C 137
SITE 2 AC9 6 HOH C 315 HOH C 316
SITE 1 BC1 6 ASP C 124 LEU C 126 ASN C 128 ASP C 132
SITE 2 BC1 6 HOH C 313 HOH C 314
SITE 1 BC2 6 GLU D 122 ASP D 124 ASP D 132 HIS D 137
SITE 2 BC2 6 HOH D 311 HOH D 312
SITE 1 BC3 6 ASP D 124 LEU D 126 ASN D 128 ASP D 132
SITE 2 BC3 6 HOH D 309 HOH D 310
CRYST1 106.300 121.200 90.800 90.00 93.70 90.00 C 1 2 1 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 0.009407 0.000000 0.000608 0.00000
SCALE2 0.000000 0.008251 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011036 0.00000
ATOM 1 N SER A 1 22.898 12.385 31.874 1.00 45.32 N
ATOM 2 CA SER A 1 23.460 11.023 31.698 1.00 45.32 C
ATOM 3 C SER A 1 24.830 10.878 32.348 1.00 46.11 C
ATOM 4 O SER A 1 25.682 11.751 32.260 1.00 44.95 O
ATOM 5 CB SER A 1 23.580 10.684 30.209 1.00 48.73 C
ATOM 6 OG SER A 1 22.315 10.721 29.557 1.00 55.63 O
ATOM 7 N ASN A 2 25.018 9.773 33.046 1.00 46.57 N
ATOM 8 CA ASN A 2 26.289 9.459 33.687 1.00 41.77 C
ATOM 9 C ASN A 2 26.230 7.970 33.685 1.00 38.13 C
ATOM 10 O ASN A 2 26.061 7.319 34.712 1.00 40.44 O
ATOM 11 CB ASN A 2 26.356 9.984 35.084 1.00 40.18 C
ATOM 12 CG ASN A 2 27.480 10.900 35.260 1.00 41.42 C
ATOM 13 OD1 ASN A 2 28.334 10.684 36.112 1.00 52.28 O
ATOM 14 ND2 ASN A 2 27.530 11.930 34.438 1.00 36.53 N
ATOM 15 N ASP A 3 26.353 7.479 32.461 1.00 27.99 N
ATOM 16 CA ASP A 3 26.244 6.108 32.102 1.00 21.75 C
ATOM 17 C ASP A 3 27.438 5.208 32.343 1.00 18.49 C
ATOM 18 O ASP A 3 28.568 5.646 32.511 1.00 19.81 O
ATOM 19 CB ASP A 3 25.825 6.079 30.647 1.00 28.09 C
ATOM 20 CG ASP A 3 24.899 7.244 30.285 1.00 36.64 C
ATOM 21 OD1 ASP A 3 24.254 7.802 31.215 1.00 40.99 O
ATOM 22 OD2 ASP A 3 24.823 7.605 29.079 1.00 40.03 O
ATOM 23 N ILE A 4 27.133 3.927 32.383 1.00 14.48 N
ATOM 24 CA ILE A 4 28.097 2.868 32.556 1.00 15.10 C
ATOM 25 C ILE A 4 27.462 1.642 31.887 1.00 15.99 C
ATOM 26 O ILE A 4 26.236 1.523 31.785 1.00 15.24 O
ATOM 27 CB ILE A 4 28.345 2.558 34.033 1.00 16.00 C
ATOM 28 CG1 ILE A 4 29.190 1.288 34.213 1.00 16.95 C
ATOM 29 CG2 ILE A 4 27.037 2.283 34.694 1.00 27.77 C
ATOM 30 CD1 ILE A 4 30.657 1.437 33.885 1.00 19.99 C
ATOM 31 N TYR A 5 28.315 0.788 31.355 1.00 17.13 N
ATOM 32 CA TYR A 5 27.883 -0.407 30.702 1.00 11.97 C
ATOM 33 C TYR A 5 29.061 -1.316 30.541 1.00 13.22 C
ATOM 34 O TYR A 5 30.145 -0.860 30.212 1.00 18.21 O
ATOM 35 CB TYR A 5 27.381 -0.106 29.334 1.00 2.63 C
ATOM 36 CG TYR A 5 27.313 -1.367 28.517 1.00 19.99 C
ATOM 37 CD1 TYR A 5 26.211 -2.206 28.587 1.00 27.62 C
ATOM 38 CD2 TYR A 5 28.343 -1.732 27.675 1.00 26.38 C
ATOM 39 CE1 TYR A 5 26.128 -3.377 27.839 1.00 30.31 C
ATOM 40 CE2 TYR A 5 28.266 -2.911 26.916 1.00 33.70 C
ATOM 41 CZ TYR A 5 27.145 -3.726 27.011 1.00 32.96 C
ATOM 42 OH TYR A 5 27.007 -4.882 26.267 1.00 38.31 O
ATOM 43 N PHE A 6 28.845 -2.599 30.761 1.00 8.61 N
ATOM 44 CA PHE A 6 29.894 -3.537 30.575 1.00 8.68 C
ATOM 45 C PHE A 6 29.279 -4.843 30.301 1.00 12.96 C
ATOM 46 O PHE A 6 28.101 -5.030 30.541 1.00 17.37 O
ATOM 47 CB PHE A 6 30.843 -3.599 31.726 1.00 2.00 C
ATOM 48 CG PHE A 6 30.232 -3.962 32.985 1.00 8.38 C
ATOM 49 CD1 PHE A 6 29.918 -5.291 33.263 1.00 9.95 C
ATOM 50 CD2 PHE A 6 30.156 -3.011 34.009 1.00 12.14 C
ATOM 51 CE1 PHE A 6 29.560 -5.690 34.557 1.00 2.00 C
ATOM 52 CE2 PHE A 6 29.796 -3.376 35.314 1.00 2.00 C
ATOM 53 CZ PHE A 6 29.501 -4.734 35.583 1.00 6.40 C
ATOM 54 N ASN A 7 30.075 -5.751 29.770 1.00 14.63 N
ATOM 55 CA ASN A 7 29.564 -7.037 29.405 1.00 10.78 C
ATOM 56 C ASN A 7 30.688 -8.019 29.323 1.00 12.65 C
ATOM 57 O ASN A 7 31.553 -7.890 28.490 1.00 19.40 O
ATOM 58 CB ASN A 7 28.929 -6.915 28.056 1.00 7.89 C
ATOM 59 CG ASN A 7 28.651 -8.244 27.455 1.00 19.38 C
ATOM 60 OD1 ASN A 7 28.107 -9.116 28.113 1.00 35.58 O
ATOM 61 ND2 ASN A 7 29.047 -8.434 26.209 1.00 25.59 N
ATOM 62 N PHE A 8 30.692 -8.990 30.211 1.00 13.05 N
ATOM 63 CA PHE A 8 31.728 -9.982 30.214 1.00 10.35 C
ATOM 64 C PHE A 8 31.204 -11.294 29.718 1.00 15.18 C
ATOM 65 O PHE A 8 30.279 -11.835 30.302 1.00 18.09 O
ATOM 66 CB PHE A 8 32.221 -10.206 31.611 1.00 12.83 C
ATOM 67 CG PHE A 8 32.606 -8.974 32.294 1.00 22.58 C
ATOM 68 CD1 PHE A 8 33.167 -7.928 31.580 1.00 25.73 C
ATOM 69 CD2 PHE A 8 32.375 -8.829 33.659 1.00 27.40 C
ATOM 70 CE1 PHE A 8 33.493 -6.743 32.217 1.00 28.60 C
ATOM 71 CE2 PHE A 8 32.693 -7.649 34.315 1.00 27.39 C
ATOM 72 CZ PHE A 8 33.252 -6.601 33.597 1.00 28.82 C
ATOM 73 N GLN A 9 31.742 -11.795 28.616 1.00 18.08 N
ATOM 74 CA GLN A 9 31.324 -13.104 28.164 1.00 19.71 C
ATOM 75 C GLN A 9 32.293 -14.140 28.696 1.00 16.38 C
ATOM 76 O GLN A 9 32.120 -15.326 28.450 1.00 14.28 O
ATOM 77 CB GLN A 9 31.174 -13.162 26.667 1.00 23.21 C
ATOM 78 CG GLN A 9 29.781 -12.810 26.267 1.00 44.25 C
ATOM 79 CD GLN A 9 29.698 -12.188 24.890 1.00 66.36 C
ATOM 80 OE1 GLN A 9 30.648 -12.265 24.094 1.00 80.37 O
ATOM 81 NE2 GLN A 9 28.568 -11.531 24.603 1.00 73.38 N
ATOM 82 N ARG A 10 33.286 -13.673 29.457 1.00 14.88 N
ATOM 83 CA ARG A 10 34.261 -14.546 30.080 1.00 21.09 C
ATOM 84 C ARG A 10 34.966 -13.705 31.130 1.00 16.78 C
ATOM 85 O ARG A 10 35.356 -12.576 30.865 1.00 24.20 O
ATOM 86 CB ARG A 10 35.215 -15.123 29.052 1.00 30.30 C
ATOM 87 CG ARG A 10 36.557 -14.445 28.958 1.00 58.94 C
ATOM 88 CD ARG A 10 37.717 -15.475 28.967 1.00 79.34 C
ATOM 89 NE ARG A 10 38.907 -14.918 29.639 1.00 99.34 N
ATOM 90 CZ ARG A 10 40.039 -15.574 29.908 1.00106.23 C
ATOM 91 NH1 ARG A 10 40.195 -16.853 29.562 1.00109.44 N
ATOM 92 NH2 ARG A 10 41.013 -14.925 30.547 1.00107.02 N
ATOM 93 N PHE A 11 35.069 -14.248 32.334 1.00 13.80 N
ATOM 94 CA PHE A 11 35.629 -13.554 33.492 1.00 14.69 C
ATOM 95 C PHE A 11 37.133 -13.631 33.670 1.00 16.73 C
ATOM 96 O PHE A 11 37.753 -14.659 33.409 1.00 17.66 O
ATOM 97 CB PHE A 11 34.960 -14.042 34.806 1.00 11.14 C
ATOM 98 CG PHE A 11 33.477 -13.798 34.865 1.00 12.52 C
ATOM 99 CD1 PHE A 11 32.593 -14.677 34.218 1.00 17.84 C
ATOM 100 CD2 PHE A 11 32.965 -12.644 35.460 1.00 15.26 C
ATOM 101 CE1 PHE A 11 31.231 -14.416 34.141 1.00 11.90 C
ATOM 102 CE2 PHE A 11 31.596 -12.351 35.401 1.00 13.84 C
ATOM 103 CZ PHE A 11 30.727 -13.249 34.732 1.00 21.56 C
ATOM 104 N ASN A 12 37.677 -12.579 34.271 1.00 15.71 N
ATOM 105 CA ASN A 12 39.088 -12.475 34.565 1.00 12.34 C