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HEADER HYDROLASE 29-NOV-00 1GA2
TITLE THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM
TITLE 2 CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE
CAVEAT 1GA2 THERE IS A CHIRALITY ERROR IN RESIDUE ILE A454
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE 9G;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.2.1.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM CELLULOLYTICUM;
SOURCE 3 ORGANISM_TAXID: 1521;
SOURCE 4 GENE: CELCCG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-5X-2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS ENDOGLUCANASE, CELLULASE 9G, CELLOBIOSE COMPLEX, CELLULOSE BINDING
KEYWDS 2 DOMAIN, (ALPHA-ALPHA)6-BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MANDELMAN,A.BELAICH,J.P.BELAICH,N.AGHAJARI,H.DRIGUEZ,R.HASER
REVDAT 4 13-JUL-11 1GA2 1 VERSN
REVDAT 3 28-JUL-09 1GA2 1 HET HETATM
REVDAT 2 24-FEB-09 1GA2 1 VERSN
REVDAT 1 22-JUL-03 1GA2 0
JRNL AUTH D.MANDELMAN,A.BELAICH,J.P.BELAICH,N.AGHAJARI,H.DRIGUEZ,
JRNL AUTH 2 R.HASER
JRNL TITL X-RAY CRYSTAL STRUCTURE OF THE MULTIDOMAIN ENDOGLUCANASE
JRNL TITL 2 CEL9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH NATURAL
JRNL TITL 3 AND SYNTHETIC CELLO-OLIGOSACCHARIDES
JRNL REF J.BACTERIOL. V. 185 4127 2003
JRNL REFN ISSN 0021-9193
JRNL PMID 12837787
JRNL DOI 10.1128/JB.185.14.4127-4135.2003
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1342846.540
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 104781
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) : 0.170
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5290
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6932
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 353
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9558
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 125
REMARK 3 SOLVENT ATOMS : 757
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.55000
REMARK 3 B22 (A**2) : 4.08000
REMARK 3 B33 (A**2) : -3.53000
REMARK 3 B12 (A**2) : 2.54000
REMARK 3 B13 (A**2) : -2.01000
REMARK 3 B23 (A**2) : -0.81000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.11
REMARK 3 LOW RESOLUTION CUTOFF (A) : 50.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
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) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.570 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.670 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 46.84
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : LIGAND.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GA2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-00.
REMARK 100 THE RCSB ID CODE IS RCSB012421.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR571
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119438
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1G87
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS, MG ACETATE,
REMARK 280 ISOPROPANOL, GLYCEROL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 A 1
REMARK 465 GLY A 2
REMARK 465 THR A 3
REMARK 465 ALA B 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 86 CG CD CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 ASP A 248 CG OD1 OD2
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 HIS A 439 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 454 CD1
REMARK 470 GLN A 572 CB CG CD OE1 NE2
REMARK 470 THR A 590 OG1 CG2
REMARK 470 ASP B 248 CG OD1 OD2
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 O THR B 591 N THR B 593 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 -117.00 -138.98
REMARK 500 ASP A 58 -168.29 -112.43
REMARK 500 GLN A 246 17.77 57.51
REMARK 500 TYR A 252 -2.98 -141.44
REMARK 500 TRP A 254 -149.59 -116.37
REMARK 500 THR A 290 -85.90 -121.32
REMARK 500 SER A 521 135.80 -174.02
REMARK 500 TRP A 534 -55.20 -127.81
REMARK 500 THR A 590 2.41 -61.72
REMARK 500 ALA B 56 -117.47 -135.50
REMARK 500 SER B 209 148.84 -170.36
REMARK 500 GLN B 246 -34.44 78.76
REMARK 500 TYR B 252 -0.68 -141.75
REMARK 500 TRP B 254 -144.52 -117.98
REMARK 500 THR B 290 -81.17 -121.39
REMARK 500 TYR B 416 3.96 -61.65
REMARK 500 VAL B 417 -75.73 -106.35
REMARK 500 THR B 591 67.19 -103.50
REMARK 500 SER B 592 -11.70 24.56
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 ILE A 454 -34.8 S R CBETA WRONG HAND
REMARK 500
REMARK 500 REMARK: NULL
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 780 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 792 O
REMARK 620 2 SER A 209 O 71.1
REMARK 620 3 ASP A 213 OD2 101.4 76.3
REMARK 620 4 ASP A 259 O 75.7 122.6 156.8
REMARK 620 5 SER A 209 OG 98.7 72.5 134.6 68.0
REMARK 620 6 ASP A 212 OD1 151.2 80.3 74.1 119.4 68.9
REMARK 620 7 ASP A 212 OD2 156.9 131.5 90.5 85.6 86.3 51.3
REMARK 620 8 HOH A1107 O 79.3 136.9 79.7 77.2 144.3 126.2 83.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 781 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 503 OE1
REMARK 620 2 GLU A 503 OE2 46.4
REMARK 620 3 HOH A 844 O 81.6 123.4
REMARK 620 4 ASN A 578 O 84.6 103.9 88.8
REMARK 620 5 ASN A 581 OD1 116.8 84.4 149.1 69.9
REMARK 620 6 ASP A 582 OD1 157.3 150.0 76.1 98.7 85.1
REMARK 620 7 ASP A 500 O 102.4 72.5 106.3 164.1 94.2 80.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 782 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1182 O
REMARK 620 2 HOH A1183 O 96.8
REMARK 620 3 HOH B1015 O 77.7 87.9
REMARK 620 4 HIS A 371 NE2 91.3 91.4 168.8
REMARK 620 5 HOH A1184 O 174.9 87.3 99.4 91.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 783 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 500 OD2
REMARK 620 2 HOH A 920 O 102.4
REMARK 620 3 HOH A 953 O 88.8 95.3
REMARK 620 4 HOH A 975 O 95.2 90.0 172.6
REMARK 620 5 HOH A1122 O 100.6 154.1 96.7 76.4
REMARK 620 6 HOH A1120 O 170.7 86.1 86.8 88.3 71.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 784 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1148 O
REMARK 620 2 ASP A 24 OD1 87.8
REMARK 620 3 HOH A 859 O 88.5 75.5
REMARK 620 4 HOH A 967 O 165.6 77.8 86.7
REMARK 620 5 HOH A1149 O 90.6 86.6 162.1 89.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 785 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1142 O
REMARK 620 2 HOH A1141 O 91.3
REMARK 620 3 HOH A1143 O 91.8 81.8
REMARK 620 4 HOH A1151 O 87.7 90.1 171.9
REMARK 620 5 HOH A1140 O 173.8 93.7 92.5 88.6
REMARK 620 6 BGC A 778 O4 90.2 176.0 101.8 86.3 84.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 782 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1131 O
REMARK 620 2 ASP B 212 OD2 80.6
REMARK 620 3 SER B 209 OG 143.1 84.0
REMARK 620 4 ASP B 213 OD1 79.1 89.2 134.2
REMARK 620 5 ASP B 212 OD1 121.5 50.7 69.6 71.2
REMARK 620 6 SER B 209 O 139.1 132.4 73.6 78.3 81.9
REMARK 620 7 HOH B1130 O 81.1 156.1 102.0 102.2 153.0 71.1
REMARK 620 8 ASP B 259 O 76.5 82.7 68.4 155.2 119.0 124.0 78.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 783 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1132 O
REMARK 620 2 ASN B 578 O 86.0
REMARK 620 3 GLU B 503 OE2 83.5 82.5
REMARK 620 4 ASP B 582 OD1 75.1 95.6 158.5
REMARK 620 5 GLU B 503 OE1 125.8 106.4 48.1 150.0
REMARK 620 6 ASP B 500 O 103.4 169.1 103.9 81.7 72.9
REMARK 620 7 ASN B 581 OD1 148.5 77.2 119.8 80.2 84.8 91.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 784 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 861 O
REMARK 620 2 HOH B 905 O 82.9
REMARK 620 3 HOH B 938 O 88.3 91.9
REMARK 620 4 HOH B1020 O 86.4 86.6 174.7
REMARK 620 5 HOH B1134 O 91.9 172.5 93.4 87.7
REMARK 620 6 HIS B 371 NE2 174.3 93.6 87.3 97.9 92.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 785 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 856 O
REMARK 620 2 HOH B 857 O 99.6
REMARK 620 3 HOH B 872 O 98.1 89.4
REMARK 620 4 HOH B 940 O 85.2 93.4 175.3
REMARK 620 5 HOH B1138 O 88.2 172.2 88.8 87.9
REMARK 620 6 ASP B 24 OD1 179.2 80.3 81.1 95.6 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 786 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1143 O
REMARK 620 2 GLU B 79 O 172.8
REMARK 620 3 HOH B1012 O 86.1 98.2
REMARK 620 4 HOH B1139 O 90.5 95.1 91.6
REMARK 620 5 HOH B 999 O 86.5 89.3 172.4 86.7
REMARK 620 6 HOH B 979 O 87.7 86.3 92.9 175.1 88.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 775
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 776
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 778
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 779
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 780
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 781
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 782
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 783
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 784
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 785
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 786
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 787
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 788
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 789
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 790
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 780
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 781
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 782
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 783
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 784
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 785
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 786
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 787
DBREF 1GA2 A 1 614 UNP P37700 GUNG_CLOCE 36 649
DBREF 1GA2 B 1 614 UNP P37700 GUNG_CLOCE 36 649
SEQADV 1GA2 THR A 574 UNP P37700 ARG 609 CONFLICT
SEQADV 1GA2 THR A 575 UNP P37700 ARG 610 CONFLICT
SEQADV 1GA2 THR B 574 UNP P37700 ARG 609 CONFLICT
SEQADV 1GA2 THR B 575 UNP P37700 ARG 610 CONFLICT
SEQRES 1 A 614 ALA GLY THR TYR ASN TYR GLY GLU ALA LEU GLN LYS SER
SEQRES 2 A 614 ILE MET PHE TYR GLU PHE GLN ARG SER GLY ASP LEU PRO
SEQRES 3 A 614 ALA ASP LYS ARG ASP ASN TRP ARG ASP ASP SER GLY MET
SEQRES 4 A 614 LYS ASP GLY SER ASP VAL GLY VAL ASP LEU THR GLY GLY
SEQRES 5 A 614 TRP TYR ASP ALA GLY ASP HIS VAL LYS PHE ASN LEU PRO
SEQRES 6 A 614 MET SER TYR THR SER ALA MET LEU ALA TRP SER LEU TYR
SEQRES 7 A 614 GLU ASP LYS ASP ALA TYR ASP LYS SER GLY GLN THR LYS
SEQRES 8 A 614 TYR ILE MET ASP GLY ILE LYS TRP ALA ASN ASP TYR PHE
SEQRES 9 A 614 ILE LYS CYS ASN PRO THR PRO GLY VAL TYR TYR TYR GLN
SEQRES 10 A 614 VAL GLY ASP GLY GLY LYS ASP HIS SER TRP TRP GLY PRO
SEQRES 11 A 614 ALA GLU VAL MET GLN MET GLU ARG PRO SER PHE LYS VAL
SEQRES 12 A 614 ASP ALA SER LYS PRO GLY SER ALA VAL CYS ALA SER THR
SEQRES 13 A 614 ALA ALA SER LEU ALA SER ALA ALA VAL VAL PHE LYS SER
SEQRES 14 A 614 SER ASP PRO THR TYR ALA GLU LYS CYS ILE SER HIS ALA
SEQRES 15 A 614 LYS ASN LEU PHE ASP MET ALA ASP LYS ALA LYS SER ASP
SEQRES 16 A 614 ALA GLY TYR THR ALA ALA SER GLY TYR TYR SER SER SER
SEQRES 17 A 614 SER PHE TYR ASP ASP LEU SER TRP ALA ALA VAL TRP LEU
SEQRES 18 A 614 TYR LEU ALA THR ASN ASP SER THR TYR LEU ASP LYS ALA
SEQRES 19 A 614 GLU SER TYR VAL PRO ASN TRP GLY LYS GLU GLN GLN THR
SEQRES 20 A 614 ASP ILE ILE ALA TYR LYS TRP GLY GLN CYS TRP ASP ASP
SEQRES 21 A 614 VAL HIS TYR GLY ALA GLU LEU LEU LEU ALA LYS LEU THR
SEQRES 22 A 614 ASN LYS GLN LEU TYR LYS ASP SER ILE GLU MET ASN LEU
SEQRES 23 A 614 ASP PHE TRP THR THR GLY VAL ASN GLY THR ARG VAL SER
SEQRES 24 A 614 TYR THR PRO LYS GLY LEU ALA TRP LEU PHE GLN TRP GLY
SEQRES 25 A 614 SER LEU ARG HIS ALA THR THR GLN ALA PHE LEU ALA GLY
SEQRES 26 A 614 VAL TYR ALA GLU TRP GLU GLY CYS THR PRO SER LYS VAL
SEQRES 27 A 614 SER VAL TYR LYS ASP PHE LEU LYS SER GLN ILE ASP TYR
SEQRES 28 A 614 ALA LEU GLY SER THR GLY ARG SER PHE VAL VAL GLY TYR
SEQRES 29 A 614 GLY VAL ASN PRO PRO GLN HIS PRO HIS HIS ARG THR ALA
SEQRES 30 A 614 HIS GLY SER TRP THR ASP GLN MET THR SER PRO THR TYR
SEQRES 31 A 614 HIS ARG HIS THR ILE TYR GLY ALA LEU VAL GLY GLY PRO
SEQRES 32 A 614 ASP ASN ALA ASP GLY TYR THR ASP GLU ILE ASN ASN TYR
SEQRES 33 A 614 VAL ASN ASN GLU ILE ALA CYS ASP TYR ASN ALA GLY PHE
SEQRES 34 A 614 THR GLY ALA LEU ALA LYS MET TYR LYS HIS SER GLY GLY
SEQRES 35 A 614 ASP PRO ILE PRO ASN PHE LYS ALA ILE GLU LYS ILE THR
SEQRES 36 A 614 ASN ASP GLU VAL ILE ILE LYS ALA GLY LEU ASN SER THR
SEQRES 37 A 614 GLY PRO ASN TYR THR GLU ILE LYS ALA VAL VAL TYR ASN
SEQRES 38 A 614 GLN THR GLY TRP PRO ALA ARG VAL THR ASP LYS ILE SER
SEQRES 39 A 614 PHE LYS TYR PHE MET ASP LEU SER GLU ILE VAL ALA ALA
SEQRES 40 A 614 GLY ILE ASP PRO LEU SER LEU VAL THR SER SER ASN TYR
SEQRES 41 A 614 SER GLU GLY LYS ASN THR LYS VAL SER GLY VAL LEU PRO
SEQRES 42 A 614 TRP ASP VAL SER ASN ASN VAL TYR TYR VAL ASN VAL ASP
SEQRES 43 A 614 LEU THR GLY GLU ASN ILE TYR PRO GLY GLY GLN SER ALA
SEQRES 44 A 614 CYS ARG ARG GLU VAL GLN PHE ARG ILE ALA ALA PRO GLN
SEQRES 45 A 614 GLY THR THR TYR TRP ASN PRO LYS ASN ASP PHE SER TYR
SEQRES 46 A 614 ASP GLY LEU PRO THR THR SER THR VAL ASN THR VAL THR
SEQRES 47 A 614 ASN ILE PRO VAL TYR ASP ASN GLY VAL LYS VAL PHE GLY
SEQRES 48 A 614 ASN GLU PRO
SEQRES 1 B 614 ALA GLY THR TYR ASN TYR GLY GLU ALA LEU GLN LYS SER
SEQRES 2 B 614 ILE MET PHE TYR GLU PHE GLN ARG SER GLY ASP LEU PRO
SEQRES 3 B 614 ALA ASP LYS ARG ASP ASN TRP ARG ASP ASP SER GLY MET
SEQRES 4 B 614 LYS ASP GLY SER ASP VAL GLY VAL ASP LEU THR GLY GLY
SEQRES 5 B 614 TRP TYR ASP ALA GLY ASP HIS VAL LYS PHE ASN LEU PRO
SEQRES 6 B 614 MET SER TYR THR SER ALA MET LEU ALA TRP SER LEU TYR
SEQRES 7 B 614 GLU ASP LYS ASP ALA TYR ASP LYS SER GLY GLN THR LYS
SEQRES 8 B 614 TYR ILE MET ASP GLY ILE LYS TRP ALA ASN ASP TYR PHE
SEQRES 9 B 614 ILE LYS CYS ASN PRO THR PRO GLY VAL TYR TYR TYR GLN
SEQRES 10 B 614 VAL GLY ASP GLY GLY LYS ASP HIS SER TRP TRP GLY PRO
SEQRES 11 B 614 ALA GLU VAL MET GLN MET GLU ARG PRO SER PHE LYS VAL
SEQRES 12 B 614 ASP ALA SER LYS PRO GLY SER ALA VAL CYS ALA SER THR
SEQRES 13 B 614 ALA ALA SER LEU ALA SER ALA ALA VAL VAL PHE LYS SER
SEQRES 14 B 614 SER ASP PRO THR TYR ALA GLU LYS CYS ILE SER HIS ALA
SEQRES 15 B 614 LYS ASN LEU PHE ASP MET ALA ASP LYS ALA LYS SER ASP
SEQRES 16 B 614 ALA GLY TYR THR ALA ALA SER GLY TYR TYR SER SER SER
SEQRES 17 B 614 SER PHE TYR ASP ASP LEU SER TRP ALA ALA VAL TRP LEU
SEQRES 18 B 614 TYR LEU ALA THR ASN ASP SER THR TYR LEU ASP LYS ALA
SEQRES 19 B 614 GLU SER TYR VAL PRO ASN TRP GLY LYS GLU GLN GLN THR
SEQRES 20 B 614 ASP ILE ILE ALA TYR LYS TRP GLY GLN CYS TRP ASP ASP
SEQRES 21 B 614 VAL HIS TYR GLY ALA GLU LEU LEU LEU ALA LYS LEU THR
SEQRES 22 B 614 ASN LYS GLN LEU TYR LYS ASP SER ILE GLU MET ASN LEU
SEQRES 23 B 614 ASP PHE TRP THR THR GLY VAL ASN GLY THR ARG VAL SER
SEQRES 24 B 614 TYR THR PRO LYS GLY LEU ALA TRP LEU PHE GLN TRP GLY
SEQRES 25 B 614 SER LEU ARG HIS ALA THR THR GLN ALA PHE LEU ALA GLY
SEQRES 26 B 614 VAL TYR ALA GLU TRP GLU GLY CYS THR PRO SER LYS VAL
SEQRES 27 B 614 SER VAL TYR LYS ASP PHE LEU LYS SER GLN ILE ASP TYR
SEQRES 28 B 614 ALA LEU GLY SER THR GLY ARG SER PHE VAL VAL GLY TYR
SEQRES 29 B 614 GLY VAL ASN PRO PRO GLN HIS PRO HIS HIS ARG THR ALA
SEQRES 30 B 614 HIS GLY SER TRP THR ASP GLN MET THR SER PRO THR TYR
SEQRES 31 B 614 HIS ARG HIS THR ILE TYR GLY ALA LEU VAL GLY GLY PRO
SEQRES 32 B 614 ASP ASN ALA ASP GLY TYR THR ASP GLU ILE ASN ASN TYR
SEQRES 33 B 614 VAL ASN ASN GLU ILE ALA CYS ASP TYR ASN ALA GLY PHE
SEQRES 34 B 614 THR GLY ALA LEU ALA LYS MET TYR LYS HIS SER GLY GLY
SEQRES 35 B 614 ASP PRO ILE PRO ASN PHE LYS ALA ILE GLU LYS ILE THR
SEQRES 36 B 614 ASN ASP GLU VAL ILE ILE LYS ALA GLY LEU ASN SER THR
SEQRES 37 B 614 GLY PRO ASN TYR THR GLU ILE LYS ALA VAL VAL TYR ASN
SEQRES 38 B 614 GLN THR GLY TRP PRO ALA ARG VAL THR ASP LYS ILE SER
SEQRES 39 B 614 PHE LYS TYR PHE MET ASP LEU SER GLU ILE VAL ALA ALA
SEQRES 40 B 614 GLY ILE ASP PRO LEU SER LEU VAL THR SER SER ASN TYR
SEQRES 41 B 614 SER GLU GLY LYS ASN THR LYS VAL SER GLY VAL LEU PRO
SEQRES 42 B 614 TRP ASP VAL SER ASN ASN VAL TYR TYR VAL ASN VAL ASP
SEQRES 43 B 614 LEU THR GLY GLU ASN ILE TYR PRO GLY GLY GLN SER ALA
SEQRES 44 B 614 CYS ARG ARG GLU VAL GLN PHE ARG ILE ALA ALA PRO GLN
SEQRES 45 B 614 GLY THR THR TYR TRP ASN PRO LYS ASN ASP PHE SER TYR
SEQRES 46 B 614 ASP GLY LEU PRO THR THR SER THR VAL ASN THR VAL THR
SEQRES 47 B 614 ASN ILE PRO VAL TYR ASP ASN GLY VAL LYS VAL PHE GLY
SEQRES 48 B 614 ASN GLU PRO
HET BGC A 775 11
HET BGC A 776 11
HET BGC A 777 12
HET BGC A 778 11
HET BGC A 779 12
HET CA A 780 1
HET CA A 781 1
HET MG A 782 1
HET MG A 783 1
HET MG A 784 1
HET MG A 785 1
HET GOL A 786 6
HET GOL A 787 6
HET GOL A 788 6
HET GOL A 789 6
HET ACY A 790 4
HET BGC B 780 11
HET BGC B 781 12
HET CA B 782 1
HET CA B 783 1
HET MG B 784 1
HET MG B 785 1
HET MG B 786 1
HET GOL B 787 6
HETNAM BGC BETA-D-GLUCOSE
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM ACY ACETIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BGC 7(C6 H12 O6)
FORMUL 5 CA 4(CA 2+)
FORMUL 7 MG 7(MG 2+)
FORMUL 11 GOL 5(C3 H8 O3)
FORMUL 15 ACY C2 H4 O2
FORMUL 23 HOH *757(H2 O)
HELIX 1 1 ASN A 5 ARG A 21 1 17
HELIX 2 2 ASN A 63 LYS A 81 1 19
HELIX 3 3 ASP A 80 SER A 87 1 8
HELIX 4 4 GLN A 89 CYS A 107 1 19
HELIX 5 5 ASP A 120 SER A 126 1 7
HELIX 6 6 PRO A 130 MET A 134 5 5
HELIX 7 7 GLY A 149 LYS A 168 1 20
HELIX 8 8 ASP A 171 LYS A 193 1 23
HELIX 9 9 PHE A 210 ASN A 226 1 17
HELIX 10 10 ASP A 227 TYR A 237 1 11
HELIX 11 11 VAL A 238 TRP A 241 5 4
HELIX 12 12 VAL A 261 ASN A 274 1 14
HELIX 13 13 LYS A 275 THR A 290 1 16
HELIX 14 14 GLY A 312 TRP A 330 1 19
HELIX 15 15 THR A 334 SER A 336 5 3
HELIX 16 16 LYS A 337 GLY A 354 1 18
HELIX 17 17 HIS A 374 GLY A 379 1 6
HELIX 18 18 ASN A 415 GLU A 420 1 6
HELIX 19 19 ALA A 422 GLY A 441 1 20
HELIX 20 20 LEU A 501 ALA A 507 1 7
HELIX 21 21 ASP A 510 LEU A 514 5 5
HELIX 22 22 VAL A 536 ASN A 538 5 3
HELIX 23 23 ASN A 578 ASP A 582 5 5
HELIX 24 24 ASP A 582 ASP A 586 5 5
HELIX 25 25 ASN B 5 GLN B 20 1 16
HELIX 26 26 GLY B 42 GLY B 46 5 5
HELIX 27 27 ASN B 63 ASP B 80 1 18
HELIX 28 28 ASP B 80 SER B 87 1 8
HELIX 29 29 GLN B 89 CYS B 107 1 19
HELIX 30 30 ASP B 120 SER B 126 1 7
HELIX 31 31 PRO B 130 MET B 134 5 5
HELIX 32 32 GLY B 149 LYS B 168 1 20
HELIX 33 33 ASP B 171 LYS B 193 1 23
HELIX 34 34 PHE B 210 ASN B 226 1 17
HELIX 35 35 ASP B 227 TYR B 237 1 11
HELIX 36 36 VAL B 238 TRP B 241 5 4
HELIX 37 37 VAL B 261 ASN B 274 1 14
HELIX 38 38 LYS B 275 THR B 290 1 16
HELIX 39 39 GLY B 312 TRP B 330 1 19
HELIX 40 40 THR B 334 SER B 336 5 3
HELIX 41 41 LYS B 337 GLY B 354 1 18
HELIX 42 42 HIS B 374 GLY B 379 1 6
HELIX 43 43 ALA B 422 GLY B 441 1 20
HELIX 44 44 LEU B 501 ALA B 507 1 7
HELIX 45 45 ASP B 510 LEU B 514 5 5
HELIX 46 46 VAL B 536 ASN B 538 5 3
HELIX 47 47 ASN B 578 ASP B 582 5 5
HELIX 48 48 ASP B 582 ASP B 586 5 5
SHEET 1 A 3 LYS A 61 PHE A 62 0
SHEET 2 A 3 TYR A 114 VAL A 118 -1 O VAL A 118 N LYS A 61
SHEET 3 A 3 SER A 140 VAL A 143 -1 N PHE A 141 O GLN A 117
SHEET 1 B 2 SER A 299 TYR A 300 0
SHEET 2 B 2 ALA A 306 TRP A 307 -1 N TRP A 307 O SER A 299
SHEET 1 C 5 VAL A 515 SER A 521 0
SHEET 2 C 5 ARG A 561 ALA A 569 -1 N GLN A 565 O TYR A 520
SHEET 3 C 5 TYR A 472 ASN A 481 -1 O THR A 473 N ILE A 568
SHEET 4 C 5 VAL A 459 GLY A 469 -1 O ILE A 460 N TYR A 480
SHEET 5 C 5 ASN A 595 THR A 596 -1 O ASN A 595 N ALA A 463
SHEET 1 D 5 VAL A 607 PHE A 610 0
SHEET 2 D 5 VAL A 602 ASP A 604 -1 O VAL A 602 N VAL A 609
SHEET 3 D 5 ILE A 493 ASP A 500 -1 O SER A 494 N TYR A 603
SHEET 4 D 5 VAL A 540 ASP A 546 -1 O TYR A 541 N MET A 499
SHEET 5 D 5 LYS A 527 VAL A 528 -1 O LYS A 527 N ASP A 546
SHEET 1 E 5 VAL A 607 PHE A 610 0
SHEET 2 E 5 VAL A 602 ASP A 604 -1 O VAL A 602 N VAL A 609
SHEET 3 E 5 ILE A 493 ASP A 500 -1 O SER A 494 N TYR A 603
SHEET 4 E 5 VAL A 540 ASP A 546 -1 O TYR A 541 N MET A 499
SHEET 5 E 5 LEU A 532 ASP A 535 -1 N LEU A 532 O TYR A 542
SHEET 1 F 3 LYS B 61 PHE B 62 0
SHEET 2 F 3 TYR B 114 VAL B 118 -1 O VAL B 118 N LYS B 61
SHEET 3 F 3 SER B 140 VAL B 143 -1 N PHE B 141 O GLN B 117
SHEET 1 G 2 SER B 299 TYR B 300 0
SHEET 2 G 2 ALA B 306 TRP B 307 -1 N TRP B 307 O SER B 299
SHEET 1 H 5 VAL B 515 SER B 521 0
SHEET 2 H 5 ARG B 561 ALA B 569 -1 N GLN B 565 O TYR B 520
SHEET 3 H 5 TYR B 472 ASN B 481 -1 O THR B 473 N ILE B 568
SHEET 4 H 5 VAL B 459 GLY B 469 -1 O ILE B 460 N TYR B 480
SHEET 5 H 5 ASN B 595 THR B 596 -1 O ASN B 595 N ALA B 463
SHEET 1 I 5 VAL B 607 PHE B 610 0
SHEET 2 I 5 VAL B 602 ASP B 604 -1 O VAL B 602 N VAL B 609
SHEET 3 I 5 ILE B 493 ASP B 500 -1 O SER B 494 N TYR B 603
SHEET 4 I 5 VAL B 540 ASP B 546 -1 O TYR B 541 N MET B 499
SHEET 5 I 5 LYS B 527 VAL B 528 -1 O LYS B 527 N ASP B 546
SHEET 1 J 5 VAL B 607 PHE B 610 0
SHEET 2 J 5 VAL B 602 ASP B 604 -1 O VAL B 602 N VAL B 609
SHEET 3 J 5 ILE B 493 ASP B 500 -1 O SER B 494 N TYR B 603
SHEET 4 J 5 VAL B 540 ASP B 546 -1 O TYR B 541 N MET B 499
SHEET 5 J 5 LEU B 532 ASP B 535 -1 N LEU B 532 O TYR B 542
LINK C1 BGC A 775 O4 BGC A 776 1555 1555 1.39
LINK CA CA A 780 O HOH A 792 1555 1555 2.49
LINK CA CA A 780 O SER A 209 1555 1555 2.48
LINK CA CA A 780 OD2 ASP A 213 1555 1555 2.33
LINK CA CA A 780 O ASP A 259 1555 1555 2.50
LINK CA CA A 780 OG SER A 209 1555 1555 2.56
LINK CA CA A 780 OD1 ASP A 212 1555 1555 2.59
LINK CA CA A 780 OD2 ASP A 212 1555 1555 2.40
LINK CA CA A 780 O HOH A1107 1555 1555 2.37
LINK CA CA A 781 OE1 GLU A 503 1555 1555 2.31
LINK CA CA A 781 OE2 GLU A 503 1555 1555 3.02
LINK CA CA A 781 O HOH A 844 1555 1555 2.48
LINK CA CA A 781 O ASN A 578 1555 1555 2.33
LINK CA CA A 781 OD1 ASN A 581 1555 1555 2.31
LINK CA CA A 781 OD1 ASP A 582 1555 1555 2.43
LINK CA CA A 781 O ASP A 500 1555 1555 2.37
LINK MG MG A 782 O HOH A1182 1555 1555 2.14
LINK MG MG A 782 O HOH A1183 1555 1555 2.04
LINK MG MG A 782 O HOH B1015 1555 1555 2.21
LINK MG MG A 782 NE2 HIS A 371 1555 1555 2.21
LINK MG MG A 782 O HOH A1184 1555 1555 2.03
LINK MG MG A 783 OD2 ASP A 500 1555 1555 1.99
LINK MG MG A 783 O HOH A 920 1555 1555 2.11
LINK MG MG A 783 O HOH A 953 1555 1555 2.24
LINK MG MG A 783 O HOH A 975 1555 1555 2.11
LINK MG MG A 783 O HOH A1122 1555 1555 2.33
LINK MG MG A 783 O HOH A1120 1555 1555 2.19
LINK MG MG A 784 O HOH A1148 1555 1555 2.20
LINK MG MG A 784 OD1 ASP A 24 1555 1555 2.14
LINK MG MG A 784 O HOH A 859 1555 1555 2.47
LINK MG MG A 784 O HOH A 967 1555 1555 2.37
LINK MG MG A 784 O HOH A1149 1555 1555 2.00
LINK MG MG A 785 O HOH A1142 1555 1555 2.00
LINK MG MG A 785 O HOH A1141 1555 1555 2.01
LINK MG MG A 785 O HOH A1143 1555 1555 2.06
LINK MG MG A 785 O HOH A1151 1555 1555 2.04
LINK MG MG A 785 O HOH A1140 1555 1555 2.08
LINK CA CA B 782 O HOH B1131 1555 1555 2.41
LINK CA CA B 782 OD2 ASP B 212 1555 1555 2.48
LINK CA CA B 782 OG SER B 209 1555 1555 2.60
LINK CA CA B 782 OD1 ASP B 213 1555 1555 2.27
LINK CA CA B 782 OD1 ASP B 212 1555 1555 2.61
LINK CA CA B 782 O SER B 209 1555 1555 2.45
LINK CA CA B 782 O HOH B1130 1555 1555 2.40
LINK CA CA B 782 O ASP B 259 1555 1555 2.57
LINK CA CA B 783 O HOH B1132 1555 1555 2.41
LINK CA CA B 783 O ASN B 578 1555 1555 2.22
LINK CA CA B 783 OE2 GLU B 503 1555 1555 2.25
LINK CA CA B 783 OD1 ASP B 582 1555 1555 2.40
LINK CA CA B 783 OE1 GLU B 503 1555 1555 2.90
LINK CA CA B 783 O ASP B 500 1555 1555 2.33
LINK CA CA B 783 OD1 ASN B 581 1555 1555 2.32
LINK MG MG B 784 O HOH B 861 1555 1555 2.20
LINK MG MG B 784 O HOH B 905 1555 1555 2.21
LINK MG MG B 784 O HOH B 938 1555 1555 2.16
LINK MG MG B 784 O HOH B1020 1555 1555 2.00
LINK MG MG B 784 O HOH B1134 1555 1555 2.06
LINK MG MG B 784 NE2 HIS B 371 1555 1555 2.22
LINK MG MG B 785 O HOH B 856 1555 1555 1.99
LINK MG MG B 785 O HOH B 857 1555 1555 2.11
LINK MG MG B 785 O HOH B 872 1555 1555 2.25
LINK MG MG B 785 O HOH B 940 1555 1555 2.06
LINK MG MG B 785 O HOH B1138 1555 1555 2.02
LINK MG MG B 785 OD1 ASP B 24 1555 1555 2.05
LINK MG MG B 786 O HOH B1143 1555 1555 2.20
LINK MG MG B 786 O GLU B 79 1555 1555 2.07
LINK MG MG B 786 O HOH B1012 1555 1555 2.37
LINK MG MG B 786 O HOH B1139 1555 1555 2.06
LINK MG MG B 786 O HOH B 999 1555 1555 2.05
LINK MG MG B 786 O HOH B 979 1555 1555 2.24
LINK C1 BGC A 776 O4 BGC A 777 1555 1555 1.39
LINK C1 BGC A 778 O4 BGC A 779 1555 1555 1.39
LINK O4 BGC A 778 MG MG A 785 1555 1555 2.20
LINK C1 BGC B 780 O4 BGC B 781 1555 1555 1.39
CISPEP 1 SER A 387 PRO A 388 0 1.09
CISPEP 2 TRP A 485 PRO A 486 0 -0.62
CISPEP 3 SER B 387 PRO B 388 0 -0.07
CISPEP 4 TRP B 485 PRO B 486 0 -0.63
SITE 1 AC1 6 TRP A 254 ASP A 259 ASP A 260 BGC A 776
SITE 2 AC1 6 HOH A 851 LYS B 123
SITE 1 AC2 6 TRP A 254 CYS A 257 ASP A 259 BGC A 775
SITE 2 AC2 6 BGC A 777 HOH A1007
SITE 1 AC3 13 TRP A 258 PHE A 309 TRP A 311 ARG A 315
SITE 2 AC3 13 BGC A 776 MG A 785 HOH A 821 HOH A1007
SITE 3 AC3 13 HOH A1071 HOH A1141 HOH A1142 HOH A1145
SITE 4 AC3 13 HOH A1147
SITE 1 AC4 11 HIS A 373 ARG A 375 TYR A 416 GLU A 420
SITE 2 AC4 11 BGC A 779 MG A 785 HOH A1140 HOH A1142
SITE 3 AC4 11 HOH A1143 HOH A1151 HOH B1058
SITE 1 AC5 7 HIS A 373 MET A 385 BGC A 778 GLU B 522
SITE 2 AC5 7 SER B 558 ARG B 561 HOH B1098
SITE 1 AC6 6 SER A 209 ASP A 212 ASP A 213 ASP A 259
SITE 2 AC6 6 HOH A 792 HOH A1107
SITE 1 AC7 6 ASP A 500 GLU A 503 ASN A 578 ASN A 581
SITE 2 AC7 6 ASP A 582 HOH A 844
SITE 1 AC8 5 HIS A 371 HOH A1182 HOH A1183 HOH A1184
SITE 2 AC8 5 HOH B1015
SITE 1 AC9 6 ASP A 500 HOH A 920 HOH A 953 HOH A 975
SITE 2 AC9 6 HOH A1120 HOH A1122
SITE 1 BC1 5 ASP A 24 HOH A 859 HOH A 967 HOH A1148
SITE 2 BC1 5 HOH A1149
SITE 1 BC2 7 BGC A 777 BGC A 778 HOH A1140 HOH A1141
SITE 2 BC2 7 HOH A1142 HOH A1143 HOH A1151
SITE 1 BC3 4 TRP A 534 LYS B 86 ASP B 510 SER B 513
SITE 1 BC4 5 ASP A 195 ALA A 196 TYR A 198 SER A 206
SITE 2 BC4 5 SER A 207
SITE 1 BC5 9 HIS A 371 THR A 386 THR A 389 GLU A 412
SITE 2 BC5 9 ILE A 413 HOH A 941 HOH A1118 HOH A1182
SITE 3 BC5 9 SER B 336
SITE 1 BC6 8 THR A 110 HOH A 909 ASP B 24 THR B 50
SITE 2 BC6 8 TRP B 99 LYS B 106 HOH B 826 HOH B1023
SITE 1 BC7 5 ASP A 404 TYR A 409 THR A 410 ASN A 415
SITE 2 BC7 5 ASN A 418
SITE 1 BC8 6 SER B 208 TRP B 254 ASP B 259 ASP B 260
SITE 2 BC8 6 BGC B 781 HOH B 915
SITE 1 BC9 4 TRP B 254 CYS B 257 ASP B 259 BGC B 780
SITE 1 CC1 6 SER B 209 ASP B 212 ASP B 213 ASP B 259
SITE 2 CC1 6 HOH B1130 HOH B1131
SITE 1 CC2 6 ASP B 500 GLU B 503 ASN B 578 ASN B 581
SITE 2 CC2 6 ASP B 582 HOH B1132
SITE 1 CC3 6 HIS B 371 HOH B 861 HOH B 905 HOH B 938
SITE 2 CC3 6 HOH B1020 HOH B1134
SITE 1 CC4 6 ASP B 24 HOH B 856 HOH B 857 HOH B 872
SITE 2 CC4 6 HOH B 940 HOH B1138
SITE 1 CC5 7 GLU B 79 ASP B 80 HOH B 979 HOH B 999
SITE 2 CC5 7 HOH B1012 HOH B1139 HOH B1143
SITE 1 CC6 9 THR A 334 SER A 336 HOH A1133 HIS B 371
SITE 2 CC6 9 THR B 389 GLU B 412 ILE B 413 HOH B 816
SITE 3 CC6 9 HOH B 938
CRYST1 56.850 57.670 86.580 93.82 100.86 99.46 P 1 2
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 0.017590 0.002931 0.003689 0.00000
SCALE2 0.000000 0.017579 0.001780 0.00000
SCALE3 0.000000 0.000000 0.011821 0.00000
ATOM 1 N TYR A 4 19.718 18.002 49.301 1.00 22.58 N
ATOM 2 CA TYR A 4 18.297 18.418 49.091 1.00 21.76 C
ATOM 3 C TYR A 4 18.098 19.869 49.487 1.00 21.19 C
ATOM 4 O TYR A 4 18.842 20.396 50.313 1.00 20.75 O
ATOM 5 CB TYR A 4 17.356 17.539 49.920 1.00 22.91 C
ATOM 6 CG TYR A 4 17.502 16.082 49.585 1.00 23.76 C
ATOM 7 CD1 TYR A 4 18.346 15.260 50.325 1.00 24.46 C
ATOM 8 CD2 TYR A 4 16.885 15.551 48.457 1.00 25.85 C
ATOM 9 CE1 TYR A 4 18.582 13.941 49.946 1.00 25.63 C
ATOM 10 CE2 TYR A 4 17.112 14.238 48.068 1.00 27.25 C
ATOM 11 CZ TYR A 4 17.963 13.439 48.812 1.00 26.45 C
ATOM 12 OH TYR A 4 18.216 12.155 48.396 1.00 29.85 O
ATOM 13 N ASN A 5 17.098 20.516 48.895 1.00 20.87 N
ATOM 14 CA ASN A 5 16.814 21.900 49.234 1.00 20.06 C
ATOM 15 C ASN A 5 15.947 21.891 50.493 1.00 20.16 C
ATOM 16 O ASN A 5 14.725 21.722 50.417 1.00 19.96 O
ATOM 17 CB ASN A 5 16.063 22.605 48.107 1.00 19.76 C
ATOM 18 CG ASN A 5 15.949 24.081 48.357 1.00 19.30 C
ATOM 19 OD1 ASN A 5 15.821 24.505 49.512 1.00 17.85 O
ATOM 20 ND2 ASN A 5 16.003 24.881 47.292 1.00 17.05 N
ATOM 21 N TYR A 6 16.580 22.082 51.643 1.00 19.35 N
ATOM 22 CA TYR A 6 15.869 22.061 52.912 1.00 18.15 C
ATOM 23 C TYR A 6 15.036 23.314 53.168 1.00 17.73 C
ATOM 24 O TYR A 6 14.005 23.241 53.840 1.00 16.07 O
ATOM 25 CB TYR A 6 16.859 21.841 54.060 1.00 16.50 C
ATOM 26 CG TYR A 6 17.635 20.552 53.934 1.00 17.66 C
ATOM 27 CD1 TYR A 6 17.001 19.315 54.083 1.00 15.26 C
ATOM 28 CD2 TYR A 6 19.000 20.566 53.630 1.00 18.25 C
ATOM 29 CE1 TYR A 6 17.716 18.115 53.927 1.00 17.90 C
ATOM 30 CE2 TYR A 6 19.717 19.387 53.474 1.00 19.73 C
ATOM 31 CZ TYR A 6 19.073 18.167 53.623 1.00 19.42 C
ATOM 32 OH TYR A 6 19.792 17.008 53.476 1.00 16.91 O
ATOM 33 N GLY A 7 15.471 24.454 52.631 1.00 18.11 N
ATOM 34 CA GLY A 7 14.721 25.684 52.822 1.00 16.64 C
ATOM 35 C GLY A 7 13.367 25.615 52.137 1.00 16.43 C
ATOM 36 O GLY A 7 12.341 26.056 52.684 1.00 15.23 O
ATOM 37 N GLU A 8 13.360 25.060 50.928 1.00 16.12 N
ATOM 38 CA GLU A 8 12.131 24.920 50.164 1.00 15.86 C
ATOM 39 C GLU A 8 11.217 23.927 50.871 1.00 15.02 C
ATOM 40 O GLU A 8 10.004 24.124 50.936 1.00 13.67 O
ATOM 41 CB GLU A 8 12.436 24.419 48.759 1.00 17.34 C
ATOM 42 CG GLU A 8 11.217 24.318 47.851 1.00 19.26 C
ATOM 43 CD GLU A 8 11.516 23.550 46.568 1.00 22.84 C
ATOM 44 OE1 GLU A 8 12.689 23.560 46.137 1.00 26.00 O
ATOM 45 OE2 GLU A 8 10.585 22.946 45.990 1.00 20.36 O
ATOM 46 N ALA A 9 11.801 22.860 51.400 1.00 15.06 N
ATOM 47 CA ALA A 9 11.005 21.857 52.100 1.00 15.42 C
ATOM 48 C ALA A 9 10.378 22.515 53.327 1.00 14.55 C
ATOM 49 O ALA A 9 9.195 22.329 53.603 1.00 14.94 O
ATOM 50 CB ALA A 9 11.889 20.667 52.513 1.00 16.23 C
ATOM 51 N LEU A 10 11.170 23.308 54.047 1.00 14.96 N
ATOM 52 CA LEU A 10 10.687 23.991 55.254 1.00 14.26 C
ATOM 53 C LEU A 10 9.520 24.903 54.902 1.00 15.25 C
ATOM 54 O LEU A 10 8.489 24.923 55.569 1.00 16.56 O
ATOM 55 CB LEU A 10 11.809 24.832 55.870 1.00 14.58 C
ATOM 56 CG LEU A 10 11.458 25.643 57.125 1.00 13.68 C
ATOM 57 CD1 LEU A 10 11.094 24.684 58.253 1.00 16.11 C
ATOM 58 CD2 LEU A 10 12.650 26.527 57.545 1.00 14.85 C
ATOM 59 N GLN A 11 9.727 25.683 53.855 1.00 14.61 N
ATOM 60 CA GLN A 11 8.735 26.615 53.357 1.00 15.61 C
ATOM 61 C GLN A 11 7.429 25.896 53.034 1.00 15.31 C
ATOM 62 O GLN A 11 6.356 26.339 53.440 1.00 13.88 O
ATOM 63 CB GLN A 11 9.317 27.299 52.117 1.00 15.71 C
ATOM 64 CG GLN A 11 8.340 27.875 51.138 1.00 18.99 C
ATOM 65 CD GLN A 11 9.061 28.477 49.938 1.00 17.91 C
ATOM 66 OE1 GLN A 11 9.808 27.792 49.233 1.00 20.34 O
ATOM 67 NE2 GLN A 11 8.846 29.758 49.711 1.00 18.31 N
ATOM 68 N LYS A 12 7.516 24.776 52.320 1.00 14.40 N
ATOM 69 CA LYS A 12 6.308 24.043 51.959 1.00 13.40 C
ATOM 70 C LYS A 12 5.647 23.325 53.137 1.00 13.55 C
ATOM 71 O LYS A 12 4.421 23.231 53.187 1.00 15.02 O
ATOM 72 CB LYS A 12 6.613 23.074 50.810 1.00 12.78 C
ATOM 73 CG LYS A 12 6.780 23.843 49.491 1.00 13.27 C