HEADER TRANSCRIPTION 19-MAR-07 2P6T
TITLE CRYSTAL STRUCTURE OF TRANSCRIPTIONAL REGULATOR NMB0573 AND L-LEUCINE
TITLE 2 COMPLEX FROM NEISSERIA MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, LRP/ASNC FAMILY;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 122586;
SOURCE 4 STRAIN: MC58;
SOURCE 5 GENE: NMB0573;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: OPPF2146
KEYWDS NMB0573, TRANSCRIPTIONAL REGULATOR, LRP/ASNC-FAMILY, N.
KEYWDS 2 MENINIGITIDIS, STRUCTURAL GENOMICS, STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSIS OF N. MENINIGITIDIS TRANSCRIPTIONAL REGULATORS, OXFORD
KEYWDS 4 PROTEIN PRODUCTION FACILITY, OPPF, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.REN,S.SAINSBURY,R.J.OWENS,OXFORD PROTEIN PRODUCTION FACILITY (OPPF)
REVDAT 6 15-NOV-23 2P6T 1 REMARK
REVDAT 5 30-AUG-23 2P6T 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2P6T 1 VERSN
REVDAT 3 24-FEB-09 2P6T 1 VERSN
REVDAT 2 29-MAY-07 2P6T 1 JRNL
REVDAT 1 03-APR-07 2P6T 0
JRNL AUTH J.REN,S.SAINSBURY,S.E.COMBS,R.G.CAPPER,P.W.JORDAN,
JRNL AUTH 2 N.S.BERROW,D.K.STAMMERS,N.J.SAUNDERS,R.J.OWENS
JRNL TITL THE STRUCTURE AND TRANSCRIPTIONAL ANALYSIS OF A GLOBAL
JRNL TITL 2 REGULATOR FROM NEISSERIA MENINGITIDIS.
JRNL REF J.BIOL.CHEM. V. 282 14655 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17374605
JRNL DOI 10.1074/JBC.M701082200
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 28166
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 + TEST SET) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1454
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1490
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.4450
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.4570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 119
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.30000
REMARK 3 B22 (A**2) : -2.29000
REMARK 3 B33 (A**2) : 4.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 11.39000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.544
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.483
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.650
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.872
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10115 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6852 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13686 ; 1.054 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16763 ; 0.798 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1236 ; 4.825 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 452 ;38.370 ;23.982
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1825 ;16.131 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;15.649 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1633 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11021 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1987 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2559 ; 0.218 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7740 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4881 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5641 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 321 ; 0.161 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.048 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.157 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 35 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 88 ; 0.275 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.239 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6516 ; 3.576 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2487 ; 0.888 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10107 ; 5.791 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4065 ; 6.150 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3579 ; 9.229 ;10.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 158 5
REMARK 3 1 B 5 B 158 5
REMARK 3 1 C 5 C 158 5
REMARK 3 1 D 5 D 158 5
REMARK 3 1 E 5 E 158 5
REMARK 3 1 F 5 F 158 5
REMARK 3 1 G 5 G 158 5
REMARK 3 1 H 5 H 158 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 913 ; 0.44 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 913 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 913 ; 0.40 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 913 ; 0.60 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 913 ; 0.35 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 F (A): 913 ; 0.28 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 G (A): 913 ; 0.43 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 H (A): 913 ; 0.40 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1144 ; 1.19 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1144 ; 1.08 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1144 ; 1.03 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 1144 ; 1.27 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 E (A): 1144 ; 1.12 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 F (A): 1144 ; 0.93 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 G (A): 1144 ; 1.07 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 H (A): 1144 ; 1.09 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 913 ; 7.05 ; 20.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 913 ; 6.93 ; 20.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 913 ; 6.47 ; 20.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 913 ; 9.72 ; 20.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 913 ; 6.68 ; 20.00
REMARK 3 MEDIUM THERMAL 1 F (A**2): 913 ; 8.06 ; 20.00
REMARK 3 MEDIUM THERMAL 1 G (A**2): 913 ; 7.63 ; 20.00
REMARK 3 MEDIUM THERMAL 1 H (A**2): 913 ; 5.94 ; 20.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1144 ; 7.93 ; 30.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1144 ; 9.74 ; 30.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1144 ; 7.59 ; 30.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 1144 ; 10.86 ; 30.00
REMARK 3 LOOSE THERMAL 1 E (A**2): 1144 ; 8.86 ; 30.00
REMARK 3 LOOSE THERMAL 1 F (A**2): 1144 ; 9.80 ; 30.00
REMARK 3 LOOSE THERMAL 1 G (A**2): 1144 ; 9.48 ; 30.00
REMARK 3 LOOSE THERMAL 1 H (A**2): 1144 ; 7.99 ; 30.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1160 A 1160 4
REMARK 3 1 B 1160 B 1160 4
REMARK 3 1 C 1160 C 1160 4
REMARK 3 1 D 1160 D 1160 4
REMARK 3 1 E 1160 E 1160 4
REMARK 3 1 F 1160 F 1160 4
REMARK 3 1 G 1160 G 1160 4
REMARK 3 1 H 1160 H 1160 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 13 ; 0.16 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 13 ; 0.09 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 13 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 13 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 E (A): 13 ; 0.20 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 F (A): 13 ; 0.12 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 G (A): 13 ; 0.15 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 H (A): 13 ; 0.06 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 13 ; 2.89 ; 20.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 13 ; 2.44 ; 20.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 13 ; 8.61 ; 20.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 13 ; 3.59 ; 20.00
REMARK 3 MEDIUM THERMAL 2 E (A**2): 13 ; 11.24 ; 20.00
REMARK 3 MEDIUM THERMAL 2 F (A**2): 13 ; 5.97 ; 20.00
REMARK 3 MEDIUM THERMAL 2 G (A**2): 13 ; 4.51 ; 20.00
REMARK 3 MEDIUM THERMAL 2 H (A**2): 13 ; 3.87 ; 20.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2P6T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042038.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28887
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2P5V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 95 MM HEPES-NA, 190 MM CALCIUM
REMARK 280 CHLORIDE, 26.6% PEG 400, 5% GLYCEROL, PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 74.88550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 37810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -306.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 -1
REMARK 465 PRO A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 LYS A 159
REMARK 465 GLU A 160
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 160
REMARK 465 GLY C -1
REMARK 465 PRO C 0
REMARK 465 MSE C 1
REMARK 465 PRO C 2
REMARK 465 GLN C 3
REMARK 465 LEU C 4
REMARK 465 LYS C 159
REMARK 465 GLU C 160
REMARK 465 GLY D -1
REMARK 465 PRO D 0
REMARK 465 MSE D 1
REMARK 465 PRO D 2
REMARK 465 LYS D 159
REMARK 465 GLU D 160
REMARK 465 GLY E -1
REMARK 465 PRO E 0
REMARK 465 MSE E 1
REMARK 465 PRO E 2
REMARK 465 GLN E 3
REMARK 465 LEU E 4
REMARK 465 LYS E 159
REMARK 465 GLU E 160
REMARK 465 GLY F -1
REMARK 465 PRO F 0
REMARK 465 MSE F 1
REMARK 465 PRO F 2
REMARK 465 GLN F 3
REMARK 465 LYS F 159
REMARK 465 GLU F 160
REMARK 465 GLY G -1
REMARK 465 PRO G 0
REMARK 465 LYS G 159
REMARK 465 GLU G 160
REMARK 465 GLY H -1
REMARK 465 PRO H 0
REMARK 465 MSE H 1
REMARK 465 PRO H 2
REMARK 465 GLN H 3
REMARK 465 LEU H 4
REMARK 465 LYS H 159
REMARK 465 GLU H 160
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 82 -81.88 -88.19
REMARK 500 THR A 127 -45.49 -136.65
REMARK 500 ASN B 20 71.12 -118.42
REMARK 500 GLN B 54 143.17 -173.17
REMARK 500 ASN B 65 7.03 55.88
REMARK 500 ALA B 79 -154.40 -130.45
REMARK 500 THR B 127 -55.06 -134.68
REMARK 500 LEU C 6 53.38 82.26
REMARK 500 ASN C 20 65.03 -114.35
REMARK 500 ARG C 22 44.15 -103.27
REMARK 500 GLN C 54 147.84 -172.82
REMARK 500 ASP C 81 53.98 -151.89
REMARK 500 THR C 127 -53.34 -128.55
REMARK 500 THR D 5 61.69 -163.02
REMARK 500 LEU D 23 151.19 -48.27
REMARK 500 ASP D 48 45.31 -79.38
REMARK 500 ALA D 49 -56.73 -144.59
REMARK 500 ASN D 65 3.50 81.35
REMARK 500 LYS D 78 48.11 -86.47
REMARK 500 ALA D 79 -122.99 -96.44
REMARK 500 ASP D 81 15.97 54.20
REMARK 500 THR D 127 -63.64 -131.99
REMARK 500 HIS D 148 114.15 -161.29
REMARK 500 VAL E 32 0.21 -68.27
REMARK 500 GLN E 54 148.32 -178.20
REMARK 500 ASN E 65 -5.68 73.96
REMARK 500 THR E 127 -52.10 -143.82
REMARK 500 ALA F 49 33.23 -69.15
REMARK 500 GLN F 54 145.73 -173.43
REMARK 500 THR F 127 -54.67 -152.33
REMARK 500 PRO G 2 -7.87 -52.09
REMARK 500 LYS G 8 -63.83 -24.87
REMARK 500 LEU G 23 -144.15 -101.91
REMARK 500 GLU G 30 5.95 -69.10
REMARK 500 ALA G 33 70.84 71.57
REMARK 500 LEU G 34 -152.15 -150.78
REMARK 500 PRO G 36 -9.11 -56.29
REMARK 500 ALA G 79 -112.63 -89.77
REMARK 500 LYS G 80 -79.86 -133.12
REMARK 500 ALA H 33 72.13 51.97
REMARK 500 GLN H 54 149.45 -173.26
REMARK 500 LYS H 78 47.92 -87.72
REMARK 500 THR H 127 -53.68 -124.88
REMARK 500 LYS H 147 144.19 -170.09
REMARK 500 HIS H 148 106.94 -163.52
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 B 162 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 107 OD1
REMARK 620 2 LEU B1160 N 104.9
REMARK 620 3 ASP D 136 OD1 90.5 132.9
REMARK 620 4 HOH D1170 O 142.1 112.9 65.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 118 OD1
REMARK 620 2 GLY G 67 O 101.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1162 O
REMARK 620 2 HOH B1163 O 58.9
REMARK 620 3 ASN G 118 OD1 106.6 164.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 67 O
REMARK 620 2 HOH C1161 O 84.4
REMARK 620 3 HOH C1162 O 68.9 60.2
REMARK 620 4 HOH F1163 O 156.1 83.7 121.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 162 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 136 OD2
REMARK 620 2 GLU E 105 O 121.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 118 OD1
REMARK 620 2 ASN D 118 ND2 41.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 67 O
REMARK 620 2 HOH E1162 O 97.8
REMARK 620 3 HOH E1164 O 54.3 130.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 162 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 136 OD1
REMARK 620 2 ASP E 136 OD2 40.4
REMARK 620 3 GLU G 105 O 175.2 142.2
REMARK 620 4 ASP G 107 OD1 91.4 73.7 86.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 163 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E1179 O
REMARK 620 2 HOH H1161 O 97.7
REMARK 620 3 HOH H1171 O 110.0 81.4
REMARK 620 4 HOH H1172 O 97.5 67.5 140.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY F 104 O
REMARK 620 2 GLU F 105 O 67.8
REMARK 620 3 ASP F 107 OD1 119.3 85.3
REMARK 620 4 ASP H 136 OD1 124.2 123.5 116.1
REMARK 620 5 ASP H 136 OD2 163.4 113.9 77.1 40.1
REMARK 620 6 ALA H 137 O 77.0 140.8 128.4 64.3 95.1
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 CA D 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU A 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU B 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU C 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU D 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU E 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU F 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU G 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU H 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 809
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: OPTIC224 RELATED DB: TARGETDB
DBREF 2P6T A 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T B 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T C 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T D 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T E 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T F 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T G 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
DBREF 2P6T H 1 160 UNP Q9K0L9 Q9K0L9_NEIMB 28 187
SEQADV 2P6T GLY A -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO A 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE A 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE A 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY B -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO B 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE B 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE B 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY C -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO C 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE C 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE C 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY D -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO D 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE D 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE D 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY E -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO E 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE E 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE E 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY F -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO F 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE F 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE F 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY G -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO G 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE G 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE G 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQADV 2P6T GLY H -1 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T PRO H 0 UNP Q9K0L9 CLONING ARTIFACT
SEQADV 2P6T MSE H 1 UNP Q9K0L9 MET 28 MODIFIED RESIDUE
SEQADV 2P6T MSE H 117 UNP Q9K0L9 MET 144 MODIFIED RESIDUE
SEQRES 1 A 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 A 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 A 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 A 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 A 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 A 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 A 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 A 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 A 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 A 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 A 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 A 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 A 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 B 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 B 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 B 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 B 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 B 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 B 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 B 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 B 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 B 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 B 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 B 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 B 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 B 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 C 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 C 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 C 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 C 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 C 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 C 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 C 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 C 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 C 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 C 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 C 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 C 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 C 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 D 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 D 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 D 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 D 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 D 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 D 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 D 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 D 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 D 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 D 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 D 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 D 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 D 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 E 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 E 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 E 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 E 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 E 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 E 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 E 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 E 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 E 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 E 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 E 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 E 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 E 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 F 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 F 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 F 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 F 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 F 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 F 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 F 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 F 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 F 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 F 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 F 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 F 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 F 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 G 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 G 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 G 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 G 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 G 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 G 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 G 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 G 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 G 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 G 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 G 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 G 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 G 162 ASN HIS LEU LEU LYS GLU
SEQRES 1 H 162 GLY PRO MSE PRO GLN LEU THR LEU ASP LYS THR ASP ILE
SEQRES 2 H 162 LYS ILE LEU GLN VAL LEU GLN GLU ASN GLY ARG LEU THR
SEQRES 3 H 162 ASN VAL GLU LEU SER GLU ARG VAL ALA LEU SER PRO SER
SEQRES 4 H 162 PRO CYS LEU ARG ARG LEU LYS GLN LEU GLU ASP ALA GLY
SEQRES 5 H 162 ILE VAL ARG GLN TYR ALA ALA LEU LEU SER PRO GLU SER
SEQRES 6 H 162 VAL ASN LEU GLY LEU GLN ALA PHE ILE ARG VAL SER ILE
SEQRES 7 H 162 ARG LYS ALA LYS ASP ALA ARG GLU ASP PHE ALA ALA SER
SEQRES 8 H 162 VAL ARG LYS TRP PRO GLU VAL LEU SER CYS PHE ALA LEU
SEQRES 9 H 162 THR GLY GLU THR ASP TYR LEU LEU GLN ALA PHE PHE THR
SEQRES 10 H 162 ASP MSE ASN ALA PHE SER HIS PHE VAL LEU ASP THR LEU
SEQRES 11 H 162 LEU SER HIS HIS GLY VAL GLN ASP ALA GLN SER SER PHE
SEQRES 12 H 162 VAL LEU LYS GLU ILE LYS HIS THR THR SER LEU PRO LEU
SEQRES 13 H 162 ASN HIS LEU LEU LYS GLU
MODRES 2P6T MSE A 117 MET SELENOMETHIONINE
MODRES 2P6T MSE B 117 MET SELENOMETHIONINE
MODRES 2P6T MSE C 117 MET SELENOMETHIONINE
MODRES 2P6T MSE D 117 MET SELENOMETHIONINE
MODRES 2P6T MSE E 117 MET SELENOMETHIONINE
MODRES 2P6T MSE F 117 MET SELENOMETHIONINE
MODRES 2P6T MSE G 1 MET SELENOMETHIONINE
MODRES 2P6T MSE G 117 MET SELENOMETHIONINE
MODRES 2P6T MSE H 117 MET SELENOMETHIONINE
HET MSE A 117 8
HET MSE B 117 8
HET MSE C 117 8
HET MSE D 117 8
HET MSE E 117 8
HET MSE F 117 8
HET MSE G 1 8
HET MSE G 117 8
HET MSE H 117 8
HET LEU A1160 9
HET GOL A 904 6
HET CA B 161 1
HET CA B 162 1
HET LEU B1160 9
HET CA C 161 1
HET CA C 162 1
HET LEU C1160 9
HET GOL C 908 6
HET CA D 161 1
HET LEU D1160 9
HET GOL D 901 6
HET GOL D 803 6
HET CA E 161 1
HET CA E 162 1
HET LEU E1160 9
HET GOL E 907 6
HET GOL E 809 6
HET LEU F1160 9
HET CA G 161 1
HET LEU G1160 9
HET CA H 161 1
HET CA H 162 1
HET CA H 163 1
HET LEU H1160 9
HETNAM MSE SELENOMETHIONINE
HETNAM LEU LEUCINE
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 9 LEU 8(C6 H13 N O2)
FORMUL 10 GOL 6(C3 H8 O3)
FORMUL 11 CA 11(CA 2+)
FORMUL 34 HOH *132(H2 O)
HELIX 1 1 ASP A 7 ASN A 20 1 14
HELIX 2 2 THR A 24 ALA A 33 1 10
HELIX 3 3 SER A 35 ALA A 49 1 15
HELIX 4 4 PRO A 61 ASN A 65 5 5
HELIX 5 5 ASP A 81 ARG A 91 1 11
HELIX 6 6 ASP A 116 THR A 127 1 12
HELIX 7 7 LEU A 154 LEU A 158 5 5
HELIX 8 8 ASP B 7 ASN B 20 1 14
HELIX 9 9 THR B 24 VAL B 32 1 9
HELIX 10 10 SER B 35 ALA B 49 1 15
HELIX 11 11 PRO B 61 ASN B 65 5 5
HELIX 12 12 ASP B 81 ARG B 91 1 11
HELIX 13 13 ASP B 116 THR B 127 1 12
HELIX 14 14 LEU B 154 LEU B 158 5 5
HELIX 15 15 ASP C 7 ASN C 20 1 14
HELIX 16 16 THR C 24 VAL C 32 1 9
HELIX 17 17 SER C 35 GLY C 50 1 16
HELIX 18 18 PRO C 61 ASN C 65 5 5
HELIX 19 19 ASP C 81 TRP C 93 1 13
HELIX 20 20 ASP C 116 THR C 127 1 12
HELIX 21 21 LEU C 154 LEU C 158 5 5
HELIX 22 22 THR D 9 ASN D 20 1 12
HELIX 23 23 THR D 24 ALA D 33 1 10
HELIX 24 24 PRO D 38 ASP D 48 1 11
HELIX 25 25 PRO D 61 ASN D 65 5 5
HELIX 26 26 ASP D 81 TRP D 93 1 13
HELIX 27 27 ASP D 116 THR D 127 1 12
HELIX 28 28 LEU D 154 LEU D 158 5 5
HELIX 29 29 ASP E 7 ASN E 20 1 14
HELIX 30 30 THR E 24 VAL E 32 1 9
HELIX 31 31 SER E 35 GLY E 50 1 16
HELIX 32 32 PRO E 61 ASN E 65 5 5
HELIX 33 33 ALA E 79 ARG E 91 1 13
HELIX 34 34 ASP E 116 THR E 127 1 12
HELIX 35 35 LEU E 154 LEU E 158 5 5
HELIX 36 36 ASP F 7 ASN F 20 1 14
HELIX 37 37 THR F 24 GLU F 30 1 7
HELIX 38 38 SER F 35 ALA F 49 1 15
HELIX 39 39 PRO F 61 ASN F 65 5 5
HELIX 40 40 ASP F 81 ARG F 91 1 11
HELIX 41 41 ASP F 116 THR F 127 1 12
HELIX 42 42 LEU F 154 LEU F 158 5 5
HELIX 43 43 ASP G 7 ASN G 20 1 14
HELIX 44 44 THR G 24 ALA G 33 1 10
HELIX 45 45 SER G 37 GLU G 47 1 11
HELIX 46 46 ASP G 81 ARG G 91 1 11
HELIX 47 47 ASP G 116 THR G 127 1 12
HELIX 48 48 LEU G 154 LEU G 158 5 5
HELIX 49 49 ASP H 7 ASN H 20 1 14
HELIX 50 50 THR H 24 VAL H 32 1 9
HELIX 51 51 SER H 35 GLY H 50 1 16
HELIX 52 52 PRO H 61 ASN H 65 5 5
HELIX 53 53 ASP H 81 TRP H 93 1 13
HELIX 54 54 ASP H 116 THR H 127 1 12
HELIX 55 55 LEU H 154 LEU H 158 5 5
SHEET 1 A 2 VAL A 52 LEU A 59 0
SHEET 2 A 2 VAL B 52 LEU B 59 -1 O GLN B 54 N LEU A 58
SHEET 1 B 9 LEU A 68 ILE A 76 0
SHEET 2 B 9 TYR A 108 PHE A 114 -1 O ALA A 112 N ALA A 70
SHEET 3 B 9 VAL A 96 LEU A 102 -1 N PHE A 100 O LEU A 109
SHEET 4 B 9 VAL B 134 LYS B 147 -1 O LYS B 144 N ALA A 101
SHEET 5 B 9 LEU B 68 ILE B 76 -1 N SER B 75 O ASP B 136
SHEET 6 B 9 TYR B 108 PHE B 114 -1 O ALA B 112 N ALA B 70
SHEET 7 B 9 VAL B 96 LEU B 102 -1 N PHE B 100 O LEU B 109
SHEET 8 B 9 VAL A 134 HIS A 148 -1 N LEU A 143 O ALA B 101
SHEET 9 B 9 LEU A 68 ILE A 76 -1 N SER A 75 O GLN A 135
SHEET 1 C 2 VAL C 52 LEU C 59 0
SHEET 2 C 2 VAL D 52 LEU D 59 -1 O LEU D 58 N GLN C 54
SHEET 1 D 9 LEU C 68 ILE C 76 0
SHEET 2 D 9 TYR C 108 PHE C 114 -1 O ALA C 112 N ALA C 70
SHEET 3 D 9 VAL C 96 LEU C 102 -1 N PHE C 100 O LEU C 109
SHEET 4 D 9 VAL D 134 HIS D 148 -1 O LYS D 147 N CYS C 99
SHEET 5 D 9 LEU D 68 ILE D 76 -1 N PHE D 71 O SER D 140
SHEET 6 D 9 TYR D 108 PHE D 114 -1 O LEU D 110 N ILE D 72
SHEET 7 D 9 VAL D 96 LEU D 102 -1 N PHE D 100 O LEU D 109
SHEET 8 D 9 VAL C 134 HIS C 148 -1 N LYS C 147 O CYS D 99
SHEET 9 D 9 LEU C 68 ILE C 76 -1 N ARG C 73 O GLN C 138
SHEET 1 E 2 VAL E 52 LEU E 59 0
SHEET 2 E 2 VAL F 52 LEU F 59 -1 O GLN F 54 N LEU E 58
SHEET 1 F 9 LEU E 68 ILE E 76 0
SHEET 2 F 9 TYR E 108 PHE E 114 -1 O LEU E 110 N ILE E 72
SHEET 3 F 9 VAL E 96 LEU E 102 -1 N PHE E 100 O LEU E 109
SHEET 4 F 9 VAL F 134 HIS F 148 -1 O LYS F 144 N ALA E 101
SHEET 5 F 9 LEU F 68 ILE F 76 -1 N ARG F 73 O GLN F 138
SHEET 6 F 9 TYR F 108 PHE F 114 -1 O ALA F 112 N ALA F 70
SHEET 7 F 9 VAL F 96 LEU F 102 -1 N PHE F 100 O LEU F 109
SHEET 8 F 9 VAL E 134 HIS E 148 -1 N LEU E 143 O ALA F 101
SHEET 9 F 9 LEU E 68 ILE E 76 -1 N ARG E 73 O GLN E 138
SHEET 1 G 2 VAL G 52 LEU G 59 0
SHEET 2 G 2 VAL H 52 LEU H 59 -1 O GLN H 54 N LEU G 58
SHEET 1 H 9 LEU G 68 ILE G 76 0
SHEET 2 H 9 TYR G 108 PHE G 114 -1 O LEU G 110 N ILE G 72
SHEET 3 H 9 VAL G 96 LEU G 102 -1 N PHE G 100 O LEU G 109
SHEET 4 H 9 VAL H 134 HIS H 148 -1 O LYS H 147 N CYS G 99
SHEET 5 H 9 LEU H 68 ILE H 76 -1 N PHE H 71 O SER H 140
SHEET 6 H 9 TYR H 108 PHE H 114 -1 O ALA H 112 N ALA H 70
SHEET 7 H 9 VAL H 96 LEU H 102 -1 N PHE H 100 O LEU H 109
SHEET 8 H 9 VAL G 134 HIS G 148 -1 N LEU G 143 O ALA H 101
SHEET 9 H 9 LEU G 68 ILE G 76 -1 N PHE G 71 O SER G 140
LINK C ASP A 116 N MSE A 117 1555 1555 1.34
LINK C MSE A 117 N ASN A 118 1555 1555 1.33
LINK C ASP B 116 N MSE B 117 1555 1555 1.33
LINK C MSE B 117 N ASN B 118 1555 1555 1.34
LINK C ASP C 116 N MSE C 117 1555 1555 1.33
LINK C MSE C 117 N ASN C 118 1555 1555 1.33
LINK C ASP D 116 N MSE D 117 1555 1555 1.33
LINK C MSE D 117 N ASN D 118 1555 1555 1.33
LINK C ASP E 116 N MSE E 117 1555 1555 1.33
LINK C MSE E 117 N ASN E 118 1555 1555 1.33
LINK C ASP F 116 N MSE F 117 1555 1555 1.33
LINK C MSE F 117 N ASN F 118 1555 1555 1.33
LINK C MSE G 1 N PRO G 2 1555 1555 1.35
LINK C ASP G 116 N MSE G 117 1555 1555 1.33
LINK C MSE G 117 N ASN G 118 1555 1555 1.33
LINK C ASP H 116 N MSE H 117 1555 1555 1.34
LINK C MSE H 117 N ASN H 118 1555 1555 1.33
LINK OD1 ASP B 107 CA CA B 162 1555 1555 2.28
LINK OD1 ASN B 118 CA CA B 161 1555 1555 2.78
LINK CA CA B 161 O GLY G 67 1555 1555 3.03
LINK CA CA B 162 N LEU B1160 1555 1555 3.19
LINK CA CA B 162 OD1 ASP D 136 1555 1555 3.09
LINK CA CA B 162 O HOH D1170 1555 1555 3.31
LINK O HOH B1162 CA CA G 161 1555 1555 2.21
LINK O HOH B1163 CA CA G 161 1555 1555 2.71
LINK O GLY C 67 CA CA C 161 1555 1555 2.30
LINK OD2 ASP C 136 CA CA C 162 1555 1555 3.22
LINK CA CA C 161 O HOH C1161 1555 1555 2.85
LINK CA CA C 161 O HOH C1162 1555 1555 3.29
LINK CA CA C 161 O HOH F1163 1555 1555 2.72
LINK CA CA C 162 O GLU E 105 1555 1555 2.89
LINK OD1 ASN D 118 CA CA D 161 1555 1555 2.11
LINK ND2 ASN D 118 CA CA D 161 1555 1555 3.34
LINK O GLY E 67 CA CA E 161 1555 1555 3.33
LINK OD1 ASP E 136 CA CA E 162 1555 1555 2.98
LINK OD2 ASP E 136 CA CA E 162 1555 1555 3.32
LINK CA CA E 161 O HOH E1162 1555 1555 2.34
LINK CA CA E 161 O HOH E1164 1555 1555 2.48
LINK CA CA E 162 O GLU G 105 1555 1555 2.47
LINK CA CA E 162 OD1 ASP G 107 1555 1555 3.18
LINK O HOH E1179 CA CA H 163 1555 1555 2.99
LINK O GLY F 104 CA CA H 161 1555 1555 3.30
LINK O GLU F 105 CA CA H 161 1555 1555 2.94
LINK OD1 ASP F 107 CA CA H 161 1555 1555 2.42
LINK OD1 ASN G 118 CA CA G 161 1555 1555 2.36
LINK O GLU H 105 CA CA H 162 1555 1555 2.39
LINK OD1 ASP H 136 CA CA H 161 1555 1555 2.77
LINK OD2 ASP H 136 CA CA H 161 1555 1555 3.40
LINK O ALA H 137 CA CA H 161 1555 1555 3.34
LINK CA CA H 163 O HOH H1161 1555 1555 2.31
LINK CA CA H 163 O HOH H1171 1555 1555 2.46
LINK CA CA H 163 O HOH H1172 1555 1555 2.68
SITE 1 AC1 2 GLY A 67 ASN D 118
SITE 1 AC2 4 GLY B 67 HOH B1162 HOH B1163 ASN G 118
SITE 1 AC3 4 GLY C 67 HOH C1161 ASN F 118 HOH F1163
SITE 1 AC4 3 GLY E 67 HOH E1162 HOH E1164
SITE 1 AC5 6 GLY F 104 GLU F 105 ASP F 107 LEU F1160
SITE 2 AC5 6 ASP H 136 ALA H 137
SITE 1 AC6 2 ASN B 118 GLY G 67
SITE 1 AC7 3 ASP E 136 GLU G 105 ASP G 107
SITE 1 AC8 1 GLU H 105
SITE 1 AC9 5 GLY B 104 ASP B 107 LEU B1160 ASP D 136
SITE 2 AC9 5 ALA D 137
SITE 1 BC1 2 ASP C 136 GLU E 105
SITE 1 BC2 5 HOH E1179 GLY H 67 HOH H1161 HOH H1171
SITE 2 BC2 5 HOH H1172
SITE 1 BC3 11 LEU A 102 THR A 103 GLY A 104 THR A 106
SITE 2 BC3 11 ASP A 107 HOH A1165 LEU G 125 LEU G 129
SITE 3 BC3 11 ALA G 137 GLN G 138 SER G 139
SITE 1 BC4 9 LEU B 102 THR B 103 GLY B 104 ASP B 107
SITE 2 BC4 9 CA B 162 LEU D 129 ALA D 137 GLN D 138
SITE 3 BC4 9 SER D 139
SITE 1 BC5 9 LEU A 129 ALA A 137 GLN A 138 SER A 139
SITE 2 BC5 9 LEU C 102 THR C 103 GLY C 104 THR C 106
SITE 3 BC5 9 ASP C 107
SITE 1 BC6 10 LEU C 143 ARG D 83 LEU D 102 THR D 103
SITE 2 BC6 10 GLY D 104 ASP D 107 LEU F 129 ALA F 137
SITE 3 BC6 10 GLN F 138 SER F 139
SITE 1 BC7 10 LEU C 125 LEU C 129 ALA C 137 GLN C 138
SITE 2 BC7 10 SER C 139 LEU E 102 THR E 103 GLY E 104
SITE 3 BC7 10 THR E 106 ASP E 107
SITE 1 BC8 12 LEU E 143 ARG F 83 LEU F 102 THR F 103
SITE 2 BC8 12 GLY F 104 ASP F 107 VAL H 124 LEU H 125
SITE 3 BC8 12 ALA H 137 GLN H 138 SER H 139 CA H 161
SITE 1 BC9 8 LEU E 129 ALA E 137 GLN E 138 SER E 139
SITE 2 BC9 8 LEU G 102 THR G 103 GLY G 104 LEU H 143
SITE 1 CC1 9 ALA B 137 GLN B 138 SER B 139 ARG H 83
SITE 2 CC1 9 LEU H 102 THR H 103 GLY H 104 THR H 106
SITE 3 CC1 9 ASP H 107
SITE 1 CC2 3 ASN A 118 GLU D 62 GLY D 67
SITE 1 CC3 2 ASN E 65 GOL E 809
SITE 1 CC4 3 ASN C 118 GLU F 62 GLY F 67
SITE 1 CC5 4 GLN A 15 VAL A 16 GLU A 19 ARG A 31
SITE 1 CC6 4 ASN D 65 THR D 115 ASP D 116 HOH D1169
SITE 1 CC7 7 LEU E 68 ASP E 116 MSE E 117 GOL E 907
SITE 2 CC7 7 LEU H 68 ASP H 116 MSE H 117
CRYST1 65.389 149.771 77.845 90.00 105.68 90.00 P 1 21 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 0.015293 0.000000 0.004292 0.00000
SCALE2 0.000000 0.006677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013342 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
