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2FYD.pdb
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2FYD.pdb
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HEADER TRANSFERASE 07-FEB-06 2FYD
TITLE CATALYTIC DOMAIN OF BOVINE BETA 1, 4-GALACTOSYLTRANSFERASE IN COMPLEX
TITLE 2 WITH ALPHA-LACTALBUMIN, GLUCOSE, MN, AND UDP-N-ACETYLGALACTOSAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-LACTALBUMIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: LACTOSE SYNTHASE B PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-1,4-GALACTOSYLTRANSFERASE;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: RESIDUES 57-329;
COMPND 11 EC: 2.4.1.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: LALBA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17.1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 13 ORGANISM_COMMON: CATTLE;
SOURCE 14 ORGANISM_TAXID: 9913;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS LACTOSE SYTHASE, CATALYTIC INTERMEDIATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.RAMAKRISHNAN,V.RAMASAMY,P.K.QASBA
REVDAT 7 30-AUG-23 2FYD 1 REMARK
REVDAT 6 20-OCT-21 2FYD 1 REMARK SEQADV HETSYN
REVDAT 5 29-JUL-20 2FYD 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 25-AUG-09 2FYD 1 HET
REVDAT 3 24-FEB-09 2FYD 1 VERSN
REVDAT 2 11-APR-06 2FYD 1 JRNL
REVDAT 1 14-MAR-06 2FYD 0
JRNL AUTH B.RAMAKRISHNAN,V.RAMASAMY,P.K.QASBA
JRNL TITL STRUCTURAL SNAPSHOTS OF BETA-1,4-GALACTOSYLTRANSFERASE-I
JRNL TITL 2 ALONG THE KINETIC PATHWAY.
JRNL REF J.MOL.BIOL. V. 357 1619 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16497331
JRNL DOI 10.1016/J.JMB.2006.01.088
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1608743.440
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 68794
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6964
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10204
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1077
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 509
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.40000
REMARK 3 B22 (A**2) : 1.33000
REMARK 3 B33 (A**2) : -5.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.86000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.080
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.460 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.540 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.580 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 56.02
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : UD2GX1_PG.PAR
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : UD2GX1_PG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ALTHOUGH INTACT UDP-GALNAC WAS USED IN
REMARK 3 THE CRYSTALLIZATION, IN THE CRYSTAL STRUCTURE THE GALNAC MOIETY
REMARK 3 IS CLEAVED OFF FROM UDP-GALNAC. THIS CLEAVED OFF SUGAR EXISTS
REMARK 3 WITHOUT O1 OXYGEN ATOM SIMILAR TO AN OXOCARBENIUM ION OR A N-
REMARK 3 ACETYLGALACTAL FORM, WHICH CANNOT BE DISTINGUISHED AT THE
REMARK 3 PRESENT RESOLUTION
REMARK 4
REMARK 4 2FYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036457.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68901
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 32.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.56800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1OQM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES-NAOH, 6% PEG 4000, PH 6.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 47.68800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA B 117
REMARK 465 SER B 118
REMARK 465 MET B 119
REMARK 465 THR B 120
REMARK 465 GLY B 121
REMARK 465 GLY B 122
REMARK 465 GLN B 123
REMARK 465 GLN B 124
REMARK 465 MET B 125
REMARK 465 GLY B 126
REMARK 465 ARG B 127
REMARK 465 GLY B 128
REMARK 465 SER B 129
REMARK 465 SER B 130
REMARK 465 ALA D 117
REMARK 465 SER D 118
REMARK 465 MET D 119
REMARK 465 THR D 120
REMARK 465 GLY D 121
REMARK 465 GLY D 122
REMARK 465 GLN D 123
REMARK 465 GLN D 124
REMARK 465 MET D 125
REMARK 465 GLY D 126
REMARK 465 ARG D 127
REMARK 465 GLY D 128
REMARK 465 SER D 129
REMARK 465 SER D 130
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 CYS B 312 CB
REMARK 480 CYS B 401 CB
REMARK 480 CYS D 312 CB
REMARK 480 CYS D 401 CB
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 ASP C 87 CB - CG - OD1 ANGL. DEV. = 5.6 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 ASP A 14 7.19 -66.13
REMARK 500 ASN A 45 98.82 98.49
REMARK 500 ARG B 189 114.65 -174.27
REMARK 500 LYS B 352 9.07 81.97
REMARK 500 ILE C 15 -7.91 -59.75
REMARK 500 ASN C 45 98.45 69.09
REMARK 500 PHE C 59 -30.87 -132.00
REMARK 500 LYS C 122 103.68 -29.11
REMARK 500 ARG D 189 118.11 -170.27
REMARK 500 ASP D 260 1.31 -67.23
REMARK 500 GLU D 384 144.97 -172.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NGA B 404
REMARK 610 NGA D 529
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 CA A 124 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 79 O
REMARK 620 2 ASP A 82 OD1 92.8
REMARK 620 3 GLU A 84 O 165.1 83.0
REMARK 620 4 ASP A 87 OD1 92.7 143.2 82.5
REMARK 620 5 ASP A 88 OD2 101.5 143.9 90.1 69.6
REMARK 620 6 HOH A 901 O 86.1 73.3 106.1 143.3 74.8
REMARK 620 7 HOH A 910 O 78.5 69.9 86.6 75.6 145.2 139.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 405 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 254 OD2
REMARK 620 2 MET B 344 SD 96.8
REMARK 620 3 HIS B 347 NE2 84.8 93.1
REMARK 620 4 UDP B 406 O1A 98.1 164.8 85.5
REMARK 620 5 UDP B 406 O2B 177.4 84.4 97.6 80.9
REMARK 620 6 HOH B1008 O 86.2 89.8 170.8 94.0 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 526 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS C 79 O
REMARK 620 2 ASP C 82 OD1 89.7
REMARK 620 3 GLU C 84 O 167.4 81.7
REMARK 620 4 ASP C 87 OD1 93.8 147.9 88.7
REMARK 620 5 ASP C 88 OD2 104.2 140.7 88.2 68.8
REMARK 620 6 HOH C 919 O 86.6 71.4 99.3 140.6 73.0
REMARK 620 7 HOH C 924 O 85.0 75.3 83.9 73.2 141.3 145.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 527 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 254 OD2
REMARK 620 2 MET D 344 SD 100.1
REMARK 620 3 HIS D 347 NE2 80.1 97.9
REMARK 620 4 UDP D 528 O2B 174.6 82.9 104.1
REMARK 620 5 UDP D 528 O1A 96.9 163.0 85.3 80.1
REMARK 620 6 HOH D 911 O 86.3 79.7 165.5 89.8 101.2
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OQM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A 1:1 COMPLEX BETWEEN ALPHA-LACTALBUMIN AND
REMARK 900 BETA 1, 4-GALACTOSYLTRANSFERASE IN THE PRESENCE OF UDP-N-ACETYL-
REMARK 900 GALACTOSAMINE
DBREF 2FYD A 1 123 UNP P29752 LALBA_MOUSE 21 143
DBREF 2FYD C 1 123 UNP P29752 LALBA_MOUSE 21 143
DBREF 2FYD B 130 402 GB 21450879 AAM54035 57 329
DBREF 2FYD D 130 402 GB 21450879 AAM54035 57 329
SEQADV 2FYD ALA B 117 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD SER B 118 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD MET B 119 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD THR B 120 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY B 121 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY B 122 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLN B 123 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLN B 124 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD MET B 125 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY B 126 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD ARG B 127 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY B 128 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD SER B 129 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD CYS B 312 GB 21450879 TRP 239 ENGINEERED MUTATION
SEQADV 2FYD THR B 342 GB 21450879 CYS 269 ENGINEERED MUTATION
SEQADV 2FYD CYS B 401 GB 21450879 PRO 328 ENGINEERED MUTATION
SEQADV 2FYD ALA D 117 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD SER D 118 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD MET D 119 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD THR D 120 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY D 121 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY D 122 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLN D 123 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLN D 124 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD MET D 125 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY D 126 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD ARG D 127 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD GLY D 128 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD SER D 129 GB 21450879 CLONING ARTIFACT
SEQADV 2FYD CYS D 312 GB 21450879 TRP 239 ENGINEERED MUTATION
SEQADV 2FYD THR D 342 GB 21450879 CYS 269 ENGINEERED MUTATION
SEQADV 2FYD CYS D 401 GB 21450879 PRO 328 ENGINEERED MUTATION
SEQRES 1 A 123 THR GLU LEU THR LYS CYS LYS VAL SER HIS ALA ILE LYS
SEQRES 2 A 123 ASP ILE ASP GLY TYR GLN GLY ILE SER LEU LEU GLU TRP
SEQRES 3 A 123 ALA CYS VAL LEU PHE HIS THR SER GLY TYR ASP THR GLN
SEQRES 4 A 123 ALA VAL VAL ASN ASP ASN GLY SER THR GLU TYR GLY LEU
SEQRES 5 A 123 PHE GLN ILE SER ASP ARG PHE TRP CYS LYS SER SER GLU
SEQRES 6 A 123 PHE PRO GLU SER GLU ASN ILE CYS GLY ILE SER CYS ASP
SEQRES 7 A 123 LYS LEU LEU ASP ASP GLU LEU ASP ASP ASP ILE ALA CYS
SEQRES 8 A 123 ALA LYS LYS ILE LEU ALA ILE LYS GLY ILE ASP TYR TRP
SEQRES 9 A 123 LYS ALA TYR LYS PRO MET CYS SER GLU LYS LEU GLU GLN
SEQRES 10 A 123 TRP ARG CYS GLU LYS PRO
SEQRES 1 B 286 ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY SER
SEQRES 2 B 286 SER LEU THR ALA CYS PRO GLU GLU SER PRO LEU LEU VAL
SEQRES 3 B 286 GLY PRO MET LEU ILE GLU PHE ASN ILE PRO VAL ASP LEU
SEQRES 4 B 286 LYS LEU VAL GLU GLN GLN ASN PRO LYS VAL LYS LEU GLY
SEQRES 5 B 286 GLY ARG TYR THR PRO MET ASP CYS ILE SER PRO HIS LYS
SEQRES 6 B 286 VAL ALA ILE ILE ILE PRO PHE ARG ASN ARG GLN GLU HIS
SEQRES 7 B 286 LEU LYS TYR TRP LEU TYR TYR LEU HIS PRO ILE LEU GLN
SEQRES 8 B 286 ARG GLN GLN LEU ASP TYR GLY ILE TYR VAL ILE ASN GLN
SEQRES 9 B 286 ALA GLY GLU SER MET PHE ASN ARG ALA LYS LEU LEU ASN
SEQRES 10 B 286 VAL GLY PHE LYS GLU ALA LEU LYS ASP TYR ASP TYR ASN
SEQRES 11 B 286 CYS PHE VAL PHE SER ASP VAL ASP LEU ILE PRO MET ASN
SEQRES 12 B 286 ASP HIS ASN THR TYR ARG CYS PHE SER GLN PRO ARG HIS
SEQRES 13 B 286 ILE SER VAL ALA MET ASP LYS PHE GLY PHE SER LEU PRO
SEQRES 14 B 286 TYR VAL GLN TYR PHE GLY GLY VAL SER ALA LEU SER LYS
SEQRES 15 B 286 GLN GLN PHE LEU SER ILE ASN GLY PHE PRO ASN ASN TYR
SEQRES 16 B 286 CYS GLY TRP GLY GLY GLU ASP ASP ASP ILE TYR ASN ARG
SEQRES 17 B 286 LEU ALA PHE ARG GLY MET SER VAL SER ARG PRO ASN ALA
SEQRES 18 B 286 VAL ILE GLY LYS THR ARG MET ILE ARG HIS SER ARG ASP
SEQRES 19 B 286 LYS LYS ASN GLU PRO ASN PRO GLN ARG PHE ASP ARG ILE
SEQRES 20 B 286 ALA HIS THR LYS GLU THR MET LEU SER ASP GLY LEU ASN
SEQRES 21 B 286 SER LEU THR TYR MET VAL LEU GLU VAL GLN ARG TYR PRO
SEQRES 22 B 286 LEU TYR THR LYS ILE THR VAL ASP ILE GLY THR CYS SER
SEQRES 1 C 123 THR GLU LEU THR LYS CYS LYS VAL SER HIS ALA ILE LYS
SEQRES 2 C 123 ASP ILE ASP GLY TYR GLN GLY ILE SER LEU LEU GLU TRP
SEQRES 3 C 123 ALA CYS VAL LEU PHE HIS THR SER GLY TYR ASP THR GLN
SEQRES 4 C 123 ALA VAL VAL ASN ASP ASN GLY SER THR GLU TYR GLY LEU
SEQRES 5 C 123 PHE GLN ILE SER ASP ARG PHE TRP CYS LYS SER SER GLU
SEQRES 6 C 123 PHE PRO GLU SER GLU ASN ILE CYS GLY ILE SER CYS ASP
SEQRES 7 C 123 LYS LEU LEU ASP ASP GLU LEU ASP ASP ASP ILE ALA CYS
SEQRES 8 C 123 ALA LYS LYS ILE LEU ALA ILE LYS GLY ILE ASP TYR TRP
SEQRES 9 C 123 LYS ALA TYR LYS PRO MET CYS SER GLU LYS LEU GLU GLN
SEQRES 10 C 123 TRP ARG CYS GLU LYS PRO
SEQRES 1 D 286 ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY SER
SEQRES 2 D 286 SER LEU THR ALA CYS PRO GLU GLU SER PRO LEU LEU VAL
SEQRES 3 D 286 GLY PRO MET LEU ILE GLU PHE ASN ILE PRO VAL ASP LEU
SEQRES 4 D 286 LYS LEU VAL GLU GLN GLN ASN PRO LYS VAL LYS LEU GLY
SEQRES 5 D 286 GLY ARG TYR THR PRO MET ASP CYS ILE SER PRO HIS LYS
SEQRES 6 D 286 VAL ALA ILE ILE ILE PRO PHE ARG ASN ARG GLN GLU HIS
SEQRES 7 D 286 LEU LYS TYR TRP LEU TYR TYR LEU HIS PRO ILE LEU GLN
SEQRES 8 D 286 ARG GLN GLN LEU ASP TYR GLY ILE TYR VAL ILE ASN GLN
SEQRES 9 D 286 ALA GLY GLU SER MET PHE ASN ARG ALA LYS LEU LEU ASN
SEQRES 10 D 286 VAL GLY PHE LYS GLU ALA LEU LYS ASP TYR ASP TYR ASN
SEQRES 11 D 286 CYS PHE VAL PHE SER ASP VAL ASP LEU ILE PRO MET ASN
SEQRES 12 D 286 ASP HIS ASN THR TYR ARG CYS PHE SER GLN PRO ARG HIS
SEQRES 13 D 286 ILE SER VAL ALA MET ASP LYS PHE GLY PHE SER LEU PRO
SEQRES 14 D 286 TYR VAL GLN TYR PHE GLY GLY VAL SER ALA LEU SER LYS
SEQRES 15 D 286 GLN GLN PHE LEU SER ILE ASN GLY PHE PRO ASN ASN TYR
SEQRES 16 D 286 CYS GLY TRP GLY GLY GLU ASP ASP ASP ILE TYR ASN ARG
SEQRES 17 D 286 LEU ALA PHE ARG GLY MET SER VAL SER ARG PRO ASN ALA
SEQRES 18 D 286 VAL ILE GLY LYS THR ARG MET ILE ARG HIS SER ARG ASP
SEQRES 19 D 286 LYS LYS ASN GLU PRO ASN PRO GLN ARG PHE ASP ARG ILE
SEQRES 20 D 286 ALA HIS THR LYS GLU THR MET LEU SER ASP GLY LEU ASN
SEQRES 21 D 286 SER LEU THR TYR MET VAL LEU GLU VAL GLN ARG TYR PRO
SEQRES 22 D 286 LEU TYR THR LYS ILE THR VAL ASP ILE GLY THR CYS SER
HET CA A 124 1
HET PG4 A 850 13
HET MES A 805 12
HET BGC B 403 12
HET NGA B 404 14
HET MN B 405 1
HET UDP B 406 25
HET CA C 526 1
HET PG4 C 851 13
HET MES C 806 12
HET BGC D 530 12
HET NGA D 529 14
HET MN D 527 1
HET UDP D 528 25
HETNAM CA CALCIUM ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM NGA 2-ACETAMIDO-2-DEOXY-BETA-D-GALACTOPYRANOSE
HETNAM MN MANGANESE (II) ION
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN NGA N-ACETYL-BETA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 NGA BETA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2-
HETSYN 3 NGA ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-D-GALACTOSAMINE
FORMUL 5 CA 2(CA 2+)
FORMUL 6 PG4 2(C8 H18 O5)
FORMUL 7 MES 2(C6 H13 N O4 S)
FORMUL 8 BGC 2(C6 H12 O6)
FORMUL 9 NGA 2(C8 H15 N O6)
FORMUL 10 MN 2(MN 2+)
FORMUL 11 UDP 2(C9 H14 N2 O12 P2)
FORMUL 19 HOH *509(H2 O)
HELIX 1 1 THR A 4 ILE A 12 1 9
HELIX 2 2 LYS A 13 ASP A 16 5 4
HELIX 3 3 GLY A 17 ILE A 21 5 5
HELIX 4 4 SER A 22 GLY A 35 1 14
HELIX 5 5 SER A 76 LEU A 81 5 6
HELIX 6 6 LEU A 85 LYS A 99 1 15
HELIX 7 7 GLY A 100 TRP A 104 5 5
HELIX 8 8 ALA A 106 CYS A 111 1 6
HELIX 9 9 LEU A 115 ARG A 119 5 5
HELIX 10 10 ASP B 154 ASN B 162 1 9
HELIX 11 11 ARG B 191 GLN B 209 1 19
HELIX 12 12 ASN B 227 LEU B 240 1 14
HELIX 13 13 LYS B 279 GLY B 281 5 3
HELIX 14 14 LYS B 298 ILE B 304 1 7
HELIX 15 15 GLY B 316 ARG B 328 1 13
HELIX 16 16 GLN B 358 ALA B 364 1 7
HELIX 17 17 HIS B 365 MET B 370 1 6
HELIX 18 18 GLY B 374 LEU B 378 5 5
HELIX 19 19 THR C 4 ILE C 12 1 9
HELIX 20 20 LYS C 13 ASP C 16 5 4
HELIX 21 21 GLY C 17 ILE C 21 5 5
HELIX 22 22 SER C 22 GLY C 35 1 14
HELIX 23 23 SER C 76 LEU C 81 5 6
HELIX 24 24 LEU C 85 LYS C 99 1 15
HELIX 25 25 GLY C 100 TRP C 104 5 5
HELIX 26 26 ALA C 106 CYS C 111 1 6
HELIX 27 27 LEU C 115 ARG C 119 5 5
HELIX 28 28 ASP D 154 ASN D 162 1 9
HELIX 29 29 ARG D 191 GLN D 209 1 19
HELIX 30 30 ASN D 227 LEU D 240 1 14
HELIX 31 31 LYS D 279 GLY D 281 5 3
HELIX 32 32 LYS D 298 ILE D 304 1 7
HELIX 33 33 GLY D 316 ARG D 328 1 13
HELIX 34 34 GLN D 358 ALA D 364 1 7
HELIX 35 35 HIS D 365 MET D 370 1 6
HELIX 36 36 GLY D 374 LEU D 378 5 5
SHEET 1 A 3 VAL A 41 ASN A 43 0
SHEET 2 A 3 THR A 48 TYR A 50 -1 O GLU A 49 N VAL A 42
SHEET 3 A 3 ILE A 55 SER A 56 -1 O ILE A 55 N TYR A 50
SHEET 1 B 6 ARG B 170 TYR B 171 0
SHEET 2 B 6 ASP B 212 GLN B 220 -1 O TYR B 213 N TYR B 171
SHEET 3 B 6 LYS B 181 PHE B 188 1 N ILE B 186 O TYR B 216
SHEET 4 B 6 CYS B 247 SER B 251 1 O VAL B 249 N ILE B 185
SHEET 5 B 6 VAL B 293 SER B 297 -1 O SER B 294 N PHE B 250
SHEET 6 B 6 ARG B 271 HIS B 272 -1 N ARG B 271 O ALA B 295
SHEET 1 C 4 ARG B 170 TYR B 171 0
SHEET 2 C 4 ASP B 212 GLN B 220 -1 O TYR B 213 N TYR B 171
SHEET 3 C 4 THR B 392 ASP B 397 1 O THR B 392 N VAL B 217
SHEET 4 C 4 MET B 381 ARG B 387 -1 N GLN B 386 O LYS B 393
SHEET 1 D 3 LEU B 255 PRO B 257 0
SHEET 2 D 3 LYS B 341 MET B 344 -1 O ARG B 343 N ILE B 256
SHEET 3 D 3 ALA B 276 MET B 277 1 N ALA B 276 O THR B 342
SHEET 1 E 3 VAL C 41 ASN C 43 0
SHEET 2 E 3 THR C 48 TYR C 50 -1 O GLU C 49 N VAL C 42
SHEET 3 E 3 ILE C 55 SER C 56 -1 O ILE C 55 N TYR C 50
SHEET 1 F 6 ARG D 170 TYR D 171 0
SHEET 2 F 6 ASP D 212 GLN D 220 -1 O TYR D 213 N TYR D 171
SHEET 3 F 6 LYS D 181 PHE D 188 1 N ILE D 184 O TYR D 216
SHEET 4 F 6 CYS D 247 SER D 251 1 O VAL D 249 N ILE D 185
SHEET 5 F 6 VAL D 293 SER D 297 -1 O LEU D 296 N PHE D 248
SHEET 6 F 6 ARG D 271 HIS D 272 -1 N ARG D 271 O ALA D 295
SHEET 1 G 4 ARG D 170 TYR D 171 0
SHEET 2 G 4 ASP D 212 GLN D 220 -1 O TYR D 213 N TYR D 171
SHEET 3 G 4 THR D 392 ASP D 397 1 O THR D 392 N VAL D 217
SHEET 4 G 4 MET D 381 ARG D 387 -1 N GLN D 386 O LYS D 393
SHEET 1 H 3 LEU D 255 PRO D 257 0
SHEET 2 H 3 LYS D 341 MET D 344 -1 O ARG D 343 N ILE D 256
SHEET 3 H 3 ALA D 276 MET D 277 1 N ALA D 276 O THR D 342
SSBOND 1 CYS A 6 CYS A 120 1555 1555 2.04
SSBOND 2 CYS A 28 CYS A 111 1555 1555 2.03
SSBOND 3 CYS A 61 CYS A 77 1555 1555 2.04
SSBOND 4 CYS A 73 CYS A 91 1555 1555 2.05
SSBOND 5 CYS B 134 CYS B 176 1555 1555 2.04
SSBOND 6 CYS B 247 CYS B 266 1555 1555 2.03
SSBOND 7 CYS B 312 CYS B 401 1555 1555 2.05
SSBOND 8 CYS C 6 CYS C 120 1555 1555 2.03
SSBOND 9 CYS C 28 CYS C 111 1555 1555 2.04
SSBOND 10 CYS C 61 CYS C 77 1555 1555 2.04
SSBOND 11 CYS C 73 CYS C 91 1555 1555 2.03
SSBOND 12 CYS D 134 CYS D 176 1555 1555 2.03
SSBOND 13 CYS D 247 CYS D 266 1555 1555 2.03
SSBOND 14 CYS D 312 CYS D 401 1555 1555 2.03
LINK O LYS A 79 CA CA A 124 1555 1555 2.37
LINK OD1 ASP A 82 CA CA A 124 1555 1555 2.51
LINK O GLU A 84 CA CA A 124 1555 1555 2.25
LINK OD1 ASP A 87 CA CA A 124 1555 1555 2.41
LINK OD2 ASP A 88 CA CA A 124 1555 1555 2.45
LINK CA CA A 124 O HOH A 901 1555 1555 2.56
LINK CA CA A 124 O HOH A 910 1555 1555 2.53
LINK OD2 ASP B 254 MN MN B 405 1555 1555 2.25
LINK SD MET B 344 MN MN B 405 1555 1555 2.79
LINK NE2 HIS B 347 MN MN B 405 1555 1555 2.20
LINK MN MN B 405 O1A UDP B 406 1555 1555 1.97
LINK MN MN B 405 O2B UDP B 406 1555 1555 2.37
LINK MN MN B 405 O HOH B1008 1555 1555 2.37
LINK O LYS C 79 CA CA C 526 1555 1555 2.36
LINK OD1 ASP C 82 CA CA C 526 1555 1555 2.44
LINK O GLU C 84 CA CA C 526 1555 1555 2.22
LINK OD1 ASP C 87 CA CA C 526 1555 1555 2.28
LINK OD2 ASP C 88 CA CA C 526 1555 1555 2.44
LINK CA CA C 526 O HOH C 919 1555 1555 2.35
LINK CA CA C 526 O HOH C 924 1555 1555 2.54
LINK OD2 ASP D 254 MN MN D 527 1555 1555 2.33
LINK SD MET D 344 MN MN D 527 1555 1555 2.83
LINK NE2 HIS D 347 MN MN D 527 1555 1555 2.24
LINK MN MN D 527 O2B UDP D 528 1555 1555 2.31
LINK MN MN D 527 O1A UDP D 528 1555 1555 2.08
LINK MN MN D 527 O HOH D 911 1555 1555 2.04
CRYST1 58.068 95.376 100.389 90.00 101.33 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017221 0.000000 0.003451 0.00000
SCALE2 0.000000 0.010485 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010159 0.00000
ATOM 1 N THR A 1 17.634 -10.451 12.179 1.00 31.89 N
ATOM 2 CA THR A 1 18.193 -9.067 12.287 1.00 33.24 C
ATOM 3 C THR A 1 17.074 -8.032 12.277 1.00 33.34 C
ATOM 4 O THR A 1 16.144 -8.129 11.454 1.00 30.70 O
ATOM 5 CB THR A 1 19.089 -8.780 11.111 1.00 33.31 C
ATOM 6 OG1 THR A 1 20.026 -9.851 10.978 1.00 36.66 O
ATOM 7 CG2 THR A 1 19.807 -7.466 11.294 1.00 34.85 C
ATOM 8 N GLU A 2 17.164 -7.051 13.177 1.00 33.98 N
ATOM 9 CA GLU A 2 16.168 -5.976 13.239 1.00 35.90 C
ATOM 10 C GLU A 2 16.528 -4.925 12.205 1.00 35.20 C
ATOM 11 O GLU A 2 17.446 -4.140 12.413 1.00 34.02 O
ATOM 12 CB GLU A 2 16.135 -5.308 14.611 1.00 39.59 C
ATOM 13 CG GLU A 2 15.153 -4.126 14.646 1.00 46.02 C
ATOM 14 CD GLU A 2 15.281 -3.268 15.902 1.00 49.33 C
ATOM 15 OE1 GLU A 2 16.399 -3.189 16.463 1.00 50.98 O
ATOM 16 OE2 GLU A 2 14.268 -2.659 16.313 1.00 50.63 O
ATOM 17 N LEU A 3 15.792 -4.898 11.098 1.00 33.30 N
ATOM 18 CA LEU A 3 16.063 -3.959 10.010 1.00 32.92 C
ATOM 19 C LEU A 3 15.420 -2.589 10.258 1.00 33.39 C
ATOM 20 O LEU A 3 14.637 -2.423 11.196 1.00 34.34 O
ATOM 21 CB LEU A 3 15.541 -4.557 8.689 1.00 29.90 C
ATOM 22 CG LEU A 3 16.012 -5.990 8.371 1.00 30.77 C
ATOM 23 CD1 LEU A 3 15.298 -6.557 7.153 1.00 30.58 C
ATOM 24 CD2 LEU A 3 17.523 -5.969 8.133 1.00 30.94 C
ATOM 25 N THR A 4 15.749 -1.610 9.424 1.00 32.16 N
ATOM 26 CA THR A 4 15.154 -0.280 9.566 1.00 32.44 C
ATOM 27 C THR A 4 14.066 -0.153 8.490 1.00 32.74 C
ATOM 28 O THR A 4 13.994 -0.974 7.566 1.00 32.61 O
ATOM 29 CB THR A 4 16.176 0.855 9.316 1.00 32.03 C
ATOM 30 OG1 THR A 4 16.642 0.784 7.966 1.00 33.16 O
ATOM 31 CG2 THR A 4 17.349 0.758 10.262 1.00 32.84 C
ATOM 32 N LYS A 5 13.244 0.891 8.594 1.00 33.15 N
ATOM 33 CA LYS A 5 12.164 1.134 7.636 1.00 31.14 C
ATOM 34 C LYS A 5 12.690 1.243 6.207 1.00 31.19 C
ATOM 35 O LYS A 5 12.086 0.716 5.254 1.00 31.02 O
ATOM 36 CB LYS A 5 11.424 2.429 7.989 1.00 31.90 C
ATOM 37 CG LYS A 5 10.454 2.904 6.901 1.00 32.76 C
ATOM 38 CD LYS A 5 9.864 4.283 7.228 1.00 33.86 C
ATOM 39 CE LYS A 5 10.946 5.363 7.208 1.00 35.10 C
ATOM 40 NZ LYS A 5 10.409 6.676 7.656 1.00 36.86 N
ATOM 41 N CYS A 6 13.795 1.959 6.049 1.00 29.40 N
ATOM 42 CA CYS A 6 14.378 2.126 4.728 1.00 30.52 C
ATOM 43 C CYS A 6 15.053 0.868 4.211 1.00 30.27 C
ATOM 44 O CYS A 6 15.109 0.641 3.026 1.00 29.12 O
ATOM 45 CB CYS A 6 15.399 3.243 4.732 1.00 33.06 C
ATOM 46 SG CYS A 6 14.723 4.924 4.527 1.00 37.45 S
ATOM 47 N LYS A 7 15.605 0.063 5.104 1.00 32.25 N
ATOM 48 CA LYS A 7 16.252 -1.165 4.659 1.00 34.15 C
ATOM 49 C LYS A 7 15.133 -2.089 4.124 1.00 31.88 C
ATOM 50 O LYS A 7 15.250 -2.711 3.073 1.00 32.65 O
ATOM 51 CB LYS A 7 16.986 -1.782 5.842 1.00 36.72 C
ATOM 52 CG LYS A 7 18.343 -2.328 5.522 1.00 42.99 C
ATOM 53 CD LYS A 7 18.227 -3.547 4.610 1.00 46.56 C
ATOM 54 CE LYS A 7 19.566 -4.276 4.477 1.00 47.21 C
ATOM 55 NZ LYS A 7 19.349 -5.605 3.838 1.00 50.64 N
ATOM 56 N VAL A 8 14.031 -2.152 4.857 1.00 31.08 N
ATOM 57 CA VAL A 8 12.897 -2.959 4.443 1.00 28.02 C
ATOM 58 C VAL A 8 12.345 -2.416 3.138 1.00 27.03 C
ATOM 59 O VAL A 8 12.141 -3.165 2.175 1.00 26.60 O
ATOM 60 CB VAL A 8 11.778 -2.960 5.535 1.00 28.15 C
ATOM 61 CG1 VAL A 8 10.491 -3.587 4.983 1.00 27.40 C
ATOM 62 CG2 VAL A 8 12.252 -3.735 6.751 1.00 26.78 C
ATOM 63 N SER A 9 12.098 -1.110 3.089 1.00 27.42 N
ATOM 64 CA SER A 9 11.547 -0.515 1.878 1.00 28.33 C
ATOM 65 C SER A 9 12.363 -0.828 0.648 1.00 29.70 C
ATOM 66 O SER A 9 11.805 -1.188 -0.402 1.00 28.11 O
ATOM 67 CB SER A 9 11.405 1.010 2.013 1.00 29.37 C
ATOM 68 OG SER A 9 10.489 1.312 3.055 1.00 31.66 O
ATOM 69 N HIS A 10 13.679 -0.690 0.738 1.00 30.49 N
ATOM 70 CA HIS A 10 14.453 -1.000 -0.441 1.00 34.96 C
ATOM 71 C HIS A 10 14.351 -2.480 -0.783 1.00 34.45 C
ATOM 72 O HIS A 10 14.163 -2.841 -1.946 1.00 35.91 O
ATOM 73 CB HIS A 10 15.928 -0.621 -0.292 1.00 41.33 C
ATOM 74 CG HIS A 10 16.740 -1.026 -1.482 1.00 47.62 C
ATOM 75 ND1 HIS A 10 16.307 -0.805 -2.775 1.00 50.15 N
ATOM 76 CD2 HIS A 10 17.881 -1.749 -1.586 1.00 50.10 C
ATOM 77 CE1 HIS A 10 17.141 -1.382 -3.623 1.00 51.29 C
ATOM 78 NE2 HIS A 10 18.104 -1.963 -2.927 1.00 52.17 N
ATOM 79 N ALA A 11 14.455 -3.337 0.230 1.00 34.95 N
ATOM 80 CA ALA A 11 14.379 -4.784 0.007 1.00 36.63 C
ATOM 81 C ALA A 11 13.088 -5.234 -0.679 1.00 36.85 C
ATOM 82 O ALA A 11 13.136 -6.067 -1.589 1.00 38.25 O
ATOM 83 CB ALA A 11 14.574 -5.547 1.355 1.00 36.96 C
ATOM 84 N ILE A 12 11.942 -4.660 -0.302 1.00 35.41 N
ATOM 85 CA ILE A 12 10.678 -5.091 -0.905 1.00 34.36 C
ATOM 86 C ILE A 12 10.114 -4.222 -2.014 1.00 36.84 C
ATOM 87 O ILE A 12 8.921 -4.323 -2.335 1.00 34.56 O
ATOM 88 CB ILE A 12 9.583 -5.246 0.169 1.00 33.37 C
ATOM 89 CG1 ILE A 12 9.182 -3.871 0.727 1.00 32.41 C
ATOM 90 CG2 ILE A 12 10.105 -6.093 1.311 1.00 30.17 C
ATOM 91 CD1 ILE A 12 8.067 -3.941 1.764 1.00 33.17 C
ATOM 92 N LYS A 13 10.956 -3.372 -2.603 1.00 39.20 N
ATOM 93 CA LYS A 13 10.522 -2.469 -3.675 1.00 43.04 C
ATOM 94 C LYS A 13 9.677 -3.141 -4.757 1.00 43.59 C
ATOM 95 O LYS A 13 8.707 -2.549 -5.225 1.00 42.91 O
ATOM 96 CB LYS A 13 11.730 -1.795 -4.363 1.00 46.27 C
ATOM 97 CG LYS A 13 12.651 -0.942 -3.465 1.00 52.78 C
ATOM 98 CD LYS A 13 12.030 0.418 -3.036 1.00 55.78 C
ATOM 99 CE LYS A 13 13.072 1.318 -2.338 1.00 56.27 C
ATOM 100 NZ LYS A 13 12.511 2.587 -1.760 1.00 56.03 N
ATOM 101 N ASP A 14 10.063 -4.356 -5.163 1.00 45.92 N
ATOM 102 CA ASP A 14 9.357 -5.122 -6.209 1.00 47.40 C
ATOM 103 C ASP A 14 7.932 -5.574 -5.841 1.00 48.51 C
ATOM 104 O ASP A 14 7.305 -6.336 -6.586 1.00 48.93 O
ATOM 105 CB ASP A 14 10.175 -6.368 -6.597 1.00 48.76 C
ATOM 106 CG ASP A 14 9.386 -7.345 -7.490 1.00 49.51 C
ATOM 107 OD1 ASP A 14 9.046 -8.472 -7.032 1.00 48.51 O
ATOM 108 OD2 ASP A 14 9.092 -6.974 -8.646 1.00 48.56 O
ATOM 109 N ILE A 15 7.420 -5.118 -4.701 1.00 47.60 N
ATOM 110 CA ILE A 15 6.079 -5.499 -4.272 1.00 46.36 C
ATOM 111 C ILE A 15 5.179 -4.263 -4.268 1.00 45.52 C
ATOM 112 O ILE A 15 3.973 -4.368 -4.065 1.00 45.62 O
ATOM 113 CB ILE A 15 6.127 -6.142 -2.841 1.00 47.33 C
ATOM 114 CG1 ILE A 15 4.936 -7.061 -2.616 1.00 48.31 C
ATOM 115 CG2 ILE A 15 6.048 -5.078 -1.763 1.00 44.87 C
ATOM 116 CD1 ILE A 15 4.887 -7.618 -1.183 1.00 47.96 C
ATOM 117 N ASP A 16 5.771 -3.089 -4.496 1.00 44.29 N
ATOM 118 CA ASP A 16 5.014 -1.841 -4.502 1.00 43.29 C
ATOM 119 C ASP A 16 3.915 -1.852 -5.545 1.00 43.03 C
ATOM 120 O ASP A 16 4.172 -2.146 -6.713 1.00 43.75 O
ATOM 121 CB ASP A 16 5.945 -0.644 -4.746 1.00 43.03 C
ATOM 122 CG ASP A 16 5.199 0.685 -4.811 1.00 43.40 C
ATOM 123 OD1 ASP A 16 4.186 0.869 -4.097 1.00 41.17 O
ATOM 124 OD2 ASP A 16 5.635 1.570 -5.578 1.00 44.41 O
ATOM 125 N GLY A 17 2.691 -1.542 -5.112 1.00 41.09 N
ATOM 126 CA GLY A 17 1.554 -1.504 -6.017 1.00 40.79 C
ATOM 127 C GLY A 17 0.869 -2.820 -6.365 1.00 39.44 C
ATOM 128 O GLY A 17 -0.211 -2.809 -6.947 1.00 41.59 O
ATOM 129 N TYR A 18 1.474 -3.950 -6.027 1.00 38.74 N
ATOM 130 CA TYR A 18 0.877 -5.255 -6.322 1.00 38.81 C
ATOM 131 C TYR A 18 -0.425 -5.473 -5.538 1.00 38.04 C
ATOM 132 O TYR A 18 -0.479 -5.278 -4.317 1.00 35.03 O
ATOM 133 CB TYR A 18 1.874 -6.372 -6.001 1.00 38.93 C
ATOM 134 CG TYR A 18 1.411 -7.777 -6.376 1.00 40.58 C
ATOM 135 CD1 TYR A 18 1.108 -8.112 -7.701 1.00 41.27 C
ATOM 136 CD2 TYR A 18 1.306 -8.770 -5.410 1.00 38.86 C
ATOM 137 CE1 TYR A 18 0.716 -9.405 -8.049 1.00 41.35 C
ATOM 138 CE2 TYR A 18 0.914 -10.062 -5.740 1.00 40.54 C
ATOM 139 CZ TYR A 18 0.624 -10.380 -7.060 1.00 42.89 C
ATOM 140 OH TYR A 18 0.272 -11.677 -7.373 1.00 42.15 O
ATOM 141 N GLN A 19 -1.475 -5.870 -6.254 1.00 37.05 N
ATOM 142 CA GLN A 19 -2.772 -6.102 -5.633 1.00 35.90 C
ATOM 143 C GLN A 19 -3.249 -4.761 -5.038 1.00 34.95 C
ATOM 144 O GLN A 19 -4.099 -4.716 -4.165 1.00 33.89 O
ATOM 145 CB GLN A 19 -2.629 -7.184 -4.557 1.00 38.89 C
ATOM 146 CG GLN A 19 -3.564 -8.408 -4.654 1.00 41.07 C
ATOM 147 CD GLN A 19 -4.019 -8.777 -6.065 1.00 42.21 C
ATOM 148 OE1 GLN A 19 -3.308 -9.428 -6.832 1.00 42.98 O
ATOM 149 NE2 GLN A 19 -5.221 -8.354 -6.406 1.00 42.79 N
ATOM 150 N GLY A 20 -2.679 -3.665 -5.530 1.00 34.58 N
ATOM 151 CA GLY A 20 -3.075 -2.340 -5.075 1.00 34.04 C
ATOM 152 C GLY A 20 -2.509 -1.810 -3.760 1.00 34.71 C
ATOM 153 O GLY A 20 -2.884 -0.720 -3.332 1.00 35.72 O
ATOM 154 N ILE A 21 -1.614 -2.552 -3.120 1.00 31.58 N
ATOM 155 CA ILE A 21 -1.017 -2.115 -1.855 1.00 30.19 C
ATOM 156 C ILE A 21 0.300 -1.373 -2.111 1.00 29.76 C
ATOM 157 O ILE A 21 1.193 -1.903 -2.791 1.00 29.77 O
ATOM 158 CB ILE A 21 -0.716 -3.326 -0.931 1.00 29.96 C
ATOM 159 CG1 ILE A 21 -1.948 -4.230 -0.838 1.00 31.66 C
ATOM 160 CG2 ILE A 21 -0.303 -2.835 0.454 1.00 29.84 C
ATOM 161 CD1 ILE A 21 -3.198 -3.509 -0.298 1.00 32.21 C
ATOM 162 N SER A 22 0.434 -0.171 -1.550 1.00 28.79 N
ATOM 163 CA SER A 22 1.647 0.638 -1.735 1.00 29.31 C
ATOM 164 C SER A 22 2.787 0.312 -0.767 1.00 28.85 C
ATOM 165 O SER A 22 2.605 -0.387 0.241 1.00 28.63 O
ATOM 166 CB SER A 22 1.328 2.136 -1.610 1.00 29.54 C
ATOM 167 OG SER A 22 1.243 2.543 -0.242 1.00 29.90 O
ATOM 168 N LEU A 23 3.968 0.832 -1.088 1.00 29.13 N
ATOM 169 CA LEU A 23 5.154 0.645 -0.272 1.00 29.05 C
ATOM 170 C LEU A 23 4.984 1.339 1.078 1.00 28.13 C
ATOM 171 O LEU A 23 5.487 0.865 2.091 1.00 26.73 O
ATOM 172 CB LEU A 23 6.379 1.192 -1.009 1.00 31.62 C
ATOM 173 CG LEU A 23 7.763 1.034 -0.375 1.00 32.62 C
ATOM 174 CD1 LEU A 23 7.949 -0.364 0.201 1.00 32.39 C
ATOM 175 CD2 LEU A 23 8.812 1.327 -1.452 1.00 33.37 C
ATOM 176 N LEU A 24 4.275 2.465 1.096 1.00 27.32 N
ATOM 177 CA LEU A 24 4.043 3.153 2.364 1.00 26.00 C
ATOM 178 C LEU A 24 3.194 2.243 3.237 1.00 26.45 C
ATOM 179 O LEU A 24 3.513 2.013 4.416 1.00 26.70 O
ATOM 180 CB LEU A 24 3.312 4.482 2.140 1.00 27.55 C
ATOM 181 CG LEU A 24 4.025 5.521 1.266 1.00 27.98 C
ATOM 182 CD1 LEU A 24 3.287 6.859 1.420 1.00 29.92 C
ATOM 183 CD2 LEU A 24 5.484 5.697 1.675 1.00 25.65 C
ATOM 184 N GLU A 25 2.112 1.716 2.663 1.00 23.47 N
ATOM 185 CA GLU A 25 1.244 0.823 3.417 1.00 24.90 C
ATOM 186 C GLU A 25 2.007 -0.403 3.926 1.00 25.81 C
ATOM 187 O GLU A 25 1.802 -0.821 5.080 1.00 25.71 O
ATOM 188 CB GLU A 25 0.042 0.399 2.564 1.00 24.71 C
ATOM 189 CG GLU A 25 -0.969 1.511 2.343 1.00 25.85 C
ATOM 190 CD GLU A 25 -1.997 1.167 1.281 1.00 28.70 C
ATOM 191 OE1 GLU A 25 -1.594 0.806 0.156 1.00 29.11 O
ATOM 192 OE2 GLU A 25 -3.212 1.250 1.569 1.00 28.99 O
ATOM 193 N TRP A 26 2.869 -0.993 3.084 1.00 24.58 N
ATOM 194 CA TRP A 26 3.669 -2.152 3.528 1.00 25.56 C
ATOM 195 C TRP A 26 4.654 -1.769 4.647 1.00 24.88 C
ATOM 196 O TRP A 26 4.830 -2.512 5.634 1.00 24.62 O
ATOM 197 CB TRP A 26 4.445 -2.777 2.355 1.00 25.58 C
ATOM 198 CG TRP A 26 3.644 -3.838 1.650 1.00 24.40 C
ATOM 199 CD1 TRP A 26 3.200 -3.818 0.353 1.00 26.67 C
ATOM 200 CD2 TRP A 26 3.179 -5.070 2.214 1.00 24.27 C
ATOM 201 NE1 TRP A 26 2.494 -4.966 0.079 1.00 25.98 N
ATOM 202 CE2 TRP A 26 2.464 -5.750 1.204 1.00 24.50 C
ATOM 203 CE3 TRP A 26 3.299 -5.666 3.479 1.00 23.14 C
ATOM 204 CZ2 TRP A 26 1.872 -7.000 1.415 1.00 24.47 C
ATOM 205 CZ3 TRP A 26 2.711 -6.914 3.693 1.00 23.95 C
ATOM 206 CH2 TRP A 26 2.005 -7.565 2.657 1.00 22.99 C
ATOM 207 N ALA A 27 5.297 -0.616 4.512 1.00 23.07 N
ATOM 208 CA ALA A 27 6.222 -0.191 5.574 1.00 24.15 C
ATOM 209 C ALA A 27 5.464 -0.150 6.911 1.00 24.38 C
ATOM 210 O ALA A 27 5.947 -0.639 7.925 1.00 24.54 O
ATOM 211 CB ALA A 27 6.793 1.172 5.253 1.00 25.24 C
ATOM 212 N CYS A 28 4.263 0.427 6.894 1.00 25.10 N
ATOM 213 CA CYS A 28 3.415 0.525 8.077 1.00 24.06 C
ATOM 214 C CYS A 28 3.022 -0.865 8.574 1.00 24.06 C
ATOM 215 O CYS A 28 3.156 -1.163 9.754 1.00 23.49 O
ATOM 216 CB CYS A 28 2.147 1.314 7.742 1.00 24.34 C
ATOM 217 SG CYS A 28 0.972 1.453 9.132 1.00 25.46 S
ATOM 218 N VAL A 29 2.504 -1.700 7.670 1.00 22.24 N
ATOM 219 CA VAL A 29 2.104 -3.068 8.009 1.00 22.47 C
ATOM 220 C VAL A 29 3.193 -3.928 8.683 1.00 21.32 C
ATOM 221 O VAL A 29 2.947 -4.544 9.729 1.00 19.33 O
ATOM 222 CB VAL A 29 1.600 -3.821 6.740 1.00 22.11 C
ATOM 223 CG1 VAL A 29 1.524 -5.356 7.003 1.00 20.23 C
ATOM 224 CG2 VAL A 29 0.220 -3.282 6.334 1.00 21.52 C
ATOM 225 N LEU A 30 4.392 -3.952 8.094 1.00 20.91 N
ATOM 226 CA LEU A 30 5.466 -4.793 8.630 1.00 19.68 C
ATOM 227 C LEU A 30 6.032 -4.322 9.971 1.00 19.86 C
ATOM 228 O LEU A 30 6.493 -5.149 10.761 1.00 19.75 O
ATOM 229 CB LEU A 30 6.573 -4.950 7.592 1.00 21.38 C
ATOM 230 CG LEU A 30 6.096 -5.560 6.254 1.00 25.20 C
ATOM 231 CD1 LEU A 30 7.261 -5.580 5.272 1.00 22.76 C
ATOM 232 CD2 LEU A 30 5.532 -6.986 6.472 1.00 22.55 C
ATOM 233 N PHE A 31 5.988 -3.018 10.255 1.00 17.41 N
ATOM 234 CA PHE A 31 6.468 -2.574 11.567 1.00 18.72 C
ATOM 235 C PHE A 31 5.558 -3.150 12.654 1.00 20.71 C
ATOM 236 O PHE A 31 6.037 -3.700 13.646 1.00 21.44 O
ATOM 237 CB PHE A 31 6.493 -1.033 11.720 1.00 20.75 C
ATOM 238 CG PHE A 31 6.848 -0.592 13.131 1.00 20.51 C
ATOM 239 CD1 PHE A 31 8.161 -0.664 13.582 1.00 20.28 C
ATOM 240 CD2 PHE A 31 5.844 -0.299 14.054 1.00 23.32 C
ATOM 241 CE1 PHE A 31 8.476 -0.464 14.950 1.00 21.77 C
ATOM 242 CE2 PHE A 31 6.139 -0.096 15.417 1.00 21.74 C
ATOM 243 CZ PHE A 31 7.457 -0.184 15.858 1.00 21.54 C
ATOM 244 N HIS A 32 4.240 -3.055 12.473 1.00 20.53 N
ATOM 245 CA HIS A 32 3.321 -3.565 13.492 1.00 21.23 C
ATOM 246 C HIS A 32 3.209 -5.089 13.526 1.00 23.31 C
ATOM 247 O HIS A 32 2.789 -5.671 14.539 1.00 24.61 O
ATOM 248 CB HIS A 32 1.924 -2.948 13.302 1.00 21.36 C
ATOM 249 CG HIS A 32 1.882 -1.466 13.526 1.00 21.03 C
ATOM 250 ND1 HIS A 32 2.063 -0.893 14.770 1.00 22.56 N
ATOM 251 CD2 HIS A 32 1.750 -0.438 12.654 1.00 20.07 C
ATOM 252 CE1 HIS A 32 2.047 0.424 14.652 1.00 22.52 C
ATOM 253 NE2 HIS A 32 1.858 0.727 13.376 1.00 21.68 N
ATOM 254 N THR A 33 3.595 -5.739 12.431 1.00 22.19 N
ATOM 255 CA THR A 33 3.527 -7.196 12.337 1.00 21.36 C
ATOM 256 C THR A 33 4.721 -7.924 12.993 1.00 21.61 C
ATOM 257 O THR A 33 4.541 -8.848 13.776 1.00 20.85 O
ATOM 258 CB THR A 33 3.426 -7.610 10.847 1.00 22.61 C
ATOM 259 OG1 THR A 33 2.239 -7.033 10.280 1.00 22.64 O
ATOM 260 CG2 THR A 33 3.399 -9.164 10.687 1.00 21.98 C
ATOM 261 N SER A 34 5.933 -7.466 12.704 1.00 21.76 N
ATOM 262 CA SER A 34 7.147 -8.120 13.209 1.00 22.84 C
ATOM 263 C SER A 34 8.201 -7.174 13.781 1.00 25.07 C
ATOM 264 O SER A 34 9.263 -7.634 14.193 1.00 25.22 O
ATOM 265 CB SER A 34 7.813 -8.882 12.069 1.00 19.44 C
ATOM 266 OG SER A 34 8.205 -7.956 11.072 1.00 20.54 O
ATOM 267 N GLY A 35 7.925 -5.864 13.777 1.00 26.41 N
ATOM 268 CA GLY A 35 8.895 -4.895 14.264 1.00 25.07 C
ATOM 269 C GLY A 35 10.100 -4.878 13.350 1.00 27.79 C
ATOM 270 O GLY A 35 11.183 -4.465 13.762 1.00 27.67 O
ATOM 271 N TYR A 36 9.908 -5.322 12.099 1.00 26.07 N
ATOM 272 CA TYR A 36 10.977 -5.386 11.085 1.00 25.15 C
ATOM 273 C TYR A 36 12.068 -6.418 11.463 1.00 24.91 C
ATOM 274 O TYR A 36 13.195 -6.338 10.963 1.00 23.31 O
ATOM 275 CB TYR A 36 11.670 -4.010 10.862 1.00 26.35 C
ATOM 276 CG TYR A 36 10.812 -2.864 10.302 1.00 25.04 C
ATOM 277 CD1 TYR A 36 9.711 -3.106 9.482 1.00 26.21 C
ATOM 278 CD2 TYR A 36 11.110 -1.539 10.614 1.00 24.83 C
ATOM 279 CE1 TYR A 36 8.915 -2.037 8.990 1.00 24.41 C
ATOM 280 CE2 TYR A 36 10.333 -0.482 10.140 1.00 24.69 C
ATOM 281 CZ TYR A 36 9.234 -0.731 9.332 1.00 25.96 C
ATOM 282 OH TYR A 36 8.435 0.329 8.922 1.00 25.73 O
ATOM 283 N ASP A 37 11.742 -7.360 12.347 1.00 23.31 N
ATOM 284 CA ASP A 37 12.699 -8.408 12.779 1.00 24.78 C
ATOM 285 C ASP A 37 12.578 -9.648 11.881 1.00 23.80 C
ATOM 286 O ASP A 37 11.588 -10.364 11.937 1.00 22.02 O
ATOM 287 CB ASP A 37 12.406 -8.817 14.232 1.00 25.52 C
ATOM 288 CG ASP A 37 13.372 -9.881 14.757 1.00 29.17 C
ATOM 289 OD1 ASP A 37 14.157 -10.447 13.972 1.00 27.28 O
ATOM 290 OD2 ASP A 37 13.333 -10.164 15.969 1.00 29.48 O
ATOM 291 N THR A 38 13.592 -9.908 11.072 1.00 23.22 N
ATOM 292 CA THR A 38 13.582 -11.049 10.162 1.00 24.17 C
ATOM 293 C THR A 38 13.595 -12.410 10.859 1.00 24.55 C
ATOM 294 O THR A 38 13.380 -13.427 10.213 1.00 23.90 O
ATOM 295 CB THR A 38 14.767 -10.967 9.157 1.00 24.92 C
ATOM 296 OG1 THR A 38 16.009 -11.161 9.845 1.00 27.37 O
ATOM 297 CG2 THR A 38 14.793 -9.607 8.497 1.00 22.10 C
ATOM 298 N GLN A 39 13.829 -12.437 12.175 1.00 23.69 N
ATOM 299 CA GLN A 39 13.836 -13.704 12.892 1.00 23.84 C
ATOM 300 C GLN A 39 12.608 -13.832 13.797 1.00 23.92 C
ATOM 301 O GLN A 39 12.537 -14.747 14.607 1.00 22.09 O
ATOM 302 CB GLN A 39 15.107 -13.855 13.752 1.00 26.04 C
ATOM 303 CG GLN A 39 16.404 -14.018 12.968 1.00 31.12 C
ATOM 304 CD GLN A 39 17.622 -14.304 13.863 1.00 36.93 C
ATOM 305 OE1 GLN A 39 18.501 -15.066 13.482 1.00 39.90 O
ATOM 306 NE2 GLN A 39 17.679 -13.679 15.042 1.00 39.08 N
ATOM 307 N ALA A 40 11.644 -12.928 13.652 1.00 21.86 N
ATOM 308 CA ALA A 40 10.439 -12.978 14.492 1.00 23.77 C
ATOM 309 C ALA A 40 9.700 -14.335 14.439 1.00 22.24 C
ATOM 310 O ALA A 40 9.444 -14.879 13.374 1.00 20.47 O
ATOM 311 CB ALA A 40 9.478 -11.833 14.082 1.00 22.90 C
ATOM 312 N VAL A 41 9.391 -14.898 15.596 1.00 23.58 N
ATOM 313 CA VAL A 41 8.659 -16.155 15.642 1.00 25.78 C
ATOM 314 C VAL A 41 7.542 -15.954 16.648 1.00 27.26 C
ATOM 315 O VAL A 41 7.799 -15.703 17.832 1.00 28.53 O
ATOM 316 CB VAL A 41 9.534 -17.331 16.091 1.00 28.98 C
ATOM 317 CG1 VAL A 41 8.655 -18.560 16.310 1.00 27.35 C
ATOM 318 CG2 VAL A 41 10.612 -17.635 15.032 1.00 27.47 C
ATOM 319 N VAL A 42 6.296 -16.068 16.201 1.00 25.61 N
ATOM 320 CA VAL A 42 5.191 -15.840 17.117 1.00 27.42 C
ATOM 321 C VAL A 42 4.144 -16.929 17.099 1.00 31.14 C