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HEADER HYDROLASE 10-SEP-09 3A6Z
TITLE CRYSTAL STRUCTURE OF PSEUDOMONAS SP. MIS38 LIPASE (PML) IN THE OPEN
TITLE 2 CONFORMATION FOLLOWING DIALYSIS AGAINST CA-FREE BUFFER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, C;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;
SOURCE 3 ORGANISM_TAXID: 91465;
SOURCE 4 STRAIN: MIS38;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC18
KEYWDS FAMILY I.3 LIPASE, BETA-ROLL, OPEN CONFORMATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ANGKAWIDJAJA,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA
REVDAT 1 26-MAY-10 3A6Z 0
JRNL AUTH C.ANGKAWIDJAJA,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA
JRNL TITL X-RAY CRYSTALLOGRAPHIC AND MD SIMULATION STUDIES ON THE
JRNL TITL 2 MECHANISM OF INTERFACIAL ACTIVATION OF A FAMILY I.3 LIPASE
JRNL TITL 3 WITH TWO LIDS
JRNL REF J.MOL.BIOL. 2010
JRNL REFN ESSN 1089-8638
JRNL PMID 20438738
JRNL DOI 10.1016/J.JMB.2010.04.051
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 83266
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4397
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6036
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 300
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9078
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 631
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.263
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9266 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12593 ; 1.724 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1226 ; 7.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 419 ;38.304 ;25.346
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1351 ;15.402 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;22.138 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1388 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7235 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4363 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6209 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 745 ; 0.172 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 60 ; 0.099 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 39 ; 0.276 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.510 ; 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): 6160 ; 0.977 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9505 ; 1.573 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3583 ; 2.542 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3088 ; 3.610 ; 4.500
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 3A6Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB028889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87709
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : 0.10900
REMARK 200 FOR THE DATA SET : 13.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.43700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2ZVD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, PH8.5, 0.2M AMMONIUM
REMARK 280 ACETATE, 30% 2-PROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 330.11667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.05833
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 247.58750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 82.52917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 412.64583
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 330.11667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 165.05833
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 82.52917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 247.58750
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 412.64583
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 MET A 1
REMARK 465 LEU A 464
REMARK 465 PHE A 465
REMARK 465 LYS A 466
REMARK 465 MET C 1
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 LYS A 7 -126.87 54.97
REMARK 500 PHE A 45 17.50 -144.61
REMARK 500 SER A 144 162.43 111.46
REMARK 500 SER A 197 -166.24 -110.73
REMARK 500 SER A 207 -124.61 64.76
REMARK 500 ASN A 352 12.88 -147.01
REMARK 500 ARG A 392 -147.87 56.53
REMARK 500 ASP A 449 29.11 49.54
REMARK 500 TRP A 462 53.40 -68.40
REMARK 500 LEU A 512 -159.65 58.80
REMARK 500 LYS C 7 -127.78 53.79
REMARK 500 SER C 144 166.97 120.96
REMARK 500 ASN C 149 33.25 -147.28
REMARK 500 PHE C 180 18.65 -141.95
REMARK 500 SER C 207 -125.29 65.44
REMARK 500 TRP C 224 29.24 49.38
REMARK 500 ARG C 392 -159.74 59.24
REMARK 500 GLN C 419 15.63 56.16
REMARK 500 LEU C 512 -158.28 60.85
REMARK 500 ASP C 577 133.96 -32.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 262 GLY A 263 -64.69
REMARK 500 GLY A 263 SER A 264 146.49
REMARK 500 GLY A 459 PHE A 460 145.42
REMARK 500 ASP C 262 GLY C 263 -72.82
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 ASP A 62 23.1 L L OUTSIDE RANGE
REMARK 500 SER A 264 19.7 L L OUTSIDE RANGE
REMARK 500 ASN A 607 24.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 807 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C 809 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH C 812 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 843 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 853 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A 872 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH A 900 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A 905 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH A 906 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH A 908 DISTANCE = 5.48 ANGSTROMS
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 628 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 118 O
REMARK 620 2 GLN A 120 OE1 76.8
REMARK 620 3 SER A 144 O 164.6 88.4
REMARK 620 4 ASP A 153 OD2 96.0 99.0 81.7
REMARK 620 5 ASP A 157 OD1 122.7 160.2 72.4 83.4
REMARK 620 6 ASP A 157 OD2 72.8 144.6 122.6 101.8 51.8
REMARK 620 7 HOH A 715 O 98.1 83.8 84.6 165.9 89.4 82.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 253 OE2
REMARK 620 2 ASP A 275 OD1 104.9
REMARK 620 3 ASP A 275 OD2 91.5 51.9
REMARK 620 4 ASP A 283 O 87.2 90.0 140.1
REMARK 620 5 ASN A 284 OD1 96.9 152.3 145.4 74.0
REMARK 620 6 HOH A 658 O 175.4 78.2 87.8 96.3 81.2
REMARK 620 7 HOH A 681 O 87.5 125.5 75.4 144.2 71.5 87.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 374 O
REMARK 620 2 SER A 376 O 87.2
REMARK 620 3 ASP A 378 OD2 80.3 83.4
REMARK 620 4 GLY A 391 O 77.7 163.8 88.5
REMARK 620 5 ALA A 393 O 82.5 82.2 158.0 101.1
REMARK 620 6 ASP A 396 OD1 157.7 82.1 79.1 110.2 115.0
REMARK 620 7 ASP A 396 OD2 146.9 123.5 112.4 72.5 89.4 51.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 383 O
REMARK 620 2 GLY A 385 O 94.5
REMARK 620 3 ASP A 387 OD2 84.3 79.0
REMARK 620 4 ASP A 400 OD1 87.9 161.3 82.8
REMARK 620 5 ASP A 400 OD2 86.9 147.0 133.9 51.6
REMARK 620 6 GLY A 402 O 96.2 78.4 157.4 119.8 68.6
REMARK 620 7 ASN A 405 OD1 168.5 97.0 96.8 80.8 84.1 87.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 622 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 392 O
REMARK 620 2 GLY A 394 O 115.8
REMARK 620 3 ASP A 396 OD2 87.6 86.1
REMARK 620 4 GLY A 409 O 84.8 159.0 99.6
REMARK 620 5 ALA A 411 O 95.3 74.4 159.6 100.8
REMARK 620 6 ASN A 414 OD1 168.7 75.4 95.0 84.0 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 623 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 494 O
REMARK 620 2 GLY A 496 O 86.0
REMARK 620 3 ASP A 498 OD2 81.6 84.5
REMARK 620 4 GLY A 511 O 80.6 165.1 87.1
REMARK 620 5 ASP A 513 O 85.2 80.2 160.4 105.0
REMARK 620 6 ASP A 516 OD1 147.6 123.1 112.5 71.5 86.2
REMARK 620 7 ASP A 516 OD2 163.4 84.6 83.9 106.8 106.5 47.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 624 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 512 O
REMARK 620 2 GLY A 514 O 112.0
REMARK 620 3 ASP A 516 OD1 81.2 81.9
REMARK 620 4 GLY A 529 O 80.2 165.9 93.4
REMARK 620 5 ALA A 531 O 86.6 83.5 155.9 105.1
REMARK 620 6 ASP A 534 OD1 161.7 79.0 86.1 87.5 109.7
REMARK 620 7 ASP A 534 OD2 137.7 107.3 120.1 63.7 82.6 42.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 625 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 521 O
REMARK 620 2 GLY A 523 O 84.7
REMARK 620 3 ASP A 525 OD2 85.2 82.0
REMARK 620 4 SER A 538 O 77.6 161.2 90.1
REMARK 620 5 GLY A 540 O 87.1 88.8 168.5 96.5
REMARK 620 6 ASP A 543 OD1 164.0 79.4 90.9 118.0 94.2
REMARK 620 7 ASP A 543 OD2 144.9 127.6 110.0 71.2 81.1 50.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 626 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 530 O
REMARK 620 2 GLY A 532 O 99.3
REMARK 620 3 ASP A 534 OD2 86.1 85.9
REMARK 620 4 PHE A 551 O 88.5 78.2 162.1
REMARK 620 5 ASP A 554 OD1 167.2 89.1 84.8 102.8
REMARK 620 6 HOH A 761 O 81.4 177.4 91.7 104.4 89.8
REMARK 620 7 ASP A 554 OD2 131.2 125.6 112.5 83.8 46.0 54.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 628 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 118 O
REMARK 620 2 GLN C 120 OE1 76.9
REMARK 620 3 SER C 144 O 161.8 85.6
REMARK 620 4 ASP C 153 OD2 94.6 94.7 81.8
REMARK 620 5 ASP C 157 OD1 70.8 145.9 127.3 98.6
REMARK 620 6 ASP C 157 OD2 122.8 159.6 75.2 89.2 52.2
REMARK 620 7 HOH C 699 O 94.9 86.5 89.0 170.5 85.4 86.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 253 OE2
REMARK 620 2 ASP C 275 OD1 100.9
REMARK 620 3 ASP C 275 OD2 94.4 51.3
REMARK 620 4 ASP C 283 O 86.8 87.0 137.9
REMARK 620 5 ASN C 284 OD1 97.8 154.3 144.2 76.5
REMARK 620 6 HOH C 669 O 93.5 127.9 78.0 144.0 67.8
REMARK 620 7 HOH C 698 O 174.1 83.7 85.6 97.2 79.0 80.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 374 O
REMARK 620 2 SER C 376 O 91.9
REMARK 620 3 ASP C 378 OD2 80.7 87.0
REMARK 620 4 GLY C 391 O 76.9 168.7 90.7
REMARK 620 5 ALA C 393 O 86.7 82.3 163.2 97.2
REMARK 620 6 ASP C 396 OD1 158.6 74.5 82.1 116.1 107.3
REMARK 620 7 ASP C 396 OD2 148.4 116.1 113.4 74.8 83.0 52.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 383 O
REMARK 620 2 GLY C 385 O 91.1
REMARK 620 3 ASP C 387 OD2 83.7 77.1
REMARK 620 4 ASP C 400 OD1 86.8 157.8 80.6
REMARK 620 5 ASP C 400 OD2 84.5 148.1 133.3 53.7
REMARK 620 6 GLY C 402 O 87.7 73.1 148.8 128.8 75.1
REMARK 620 7 ASN C 405 OD1 174.6 92.8 93.5 88.2 94.2 97.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 623 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 494 O
REMARK 620 2 GLY C 496 O 83.8
REMARK 620 3 ASP C 498 OD2 78.9 74.4
REMARK 620 4 GLY C 511 O 84.5 163.0 91.4
REMARK 620 5 ASP C 513 O 86.7 87.3 157.6 104.2
REMARK 620 6 ASP C 516 OD1 149.8 125.8 112.5 67.9 88.5
REMARK 620 7 ASP C 516 OD2 157.2 82.6 80.0 104.4 110.7 49.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 624 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 512 O
REMARK 620 2 GLY C 514 O 103.1
REMARK 620 3 ASP C 516 OD1 78.7 87.1
REMARK 620 4 GLY C 529 O 85.8 171.1 94.3
REMARK 620 5 ALA C 531 O 80.9 73.3 147.6 109.1
REMARK 620 6 ASP C 534 OD1 160.3 84.4 83.7 87.0 118.8
REMARK 620 7 ASP C 534 OD2 143.5 108.3 120.3 63.4 90.8 43.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 625 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 521 O
REMARK 620 2 GLY C 523 O 84.2
REMARK 620 3 ASP C 525 OD2 89.5 84.3
REMARK 620 4 SER C 538 O 73.4 156.9 89.4
REMARK 620 5 GLY C 540 O 89.0 87.2 171.5 98.2
REMARK 620 6 ASP C 543 OD1 164.9 80.7 89.8 121.6 89.4
REMARK 620 7 ASP C 543 OD2 143.3 131.0 102.1 72.0 84.0 51.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 626 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 530 O
REMARK 620 2 GLY C 532 O 98.9
REMARK 620 3 ASP C 534 OD2 86.6 86.0
REMARK 620 4 PHE C 551 O 90.9 75.0 160.2
REMARK 620 5 ASP C 554 OD1 170.1 86.4 85.3 98.6
REMARK 620 6 ASP C 554 OD2 134.1 121.3 115.3 80.1 46.2
REMARK 620 7 HOH C 675 O 81.3 179.6 94.4 104.6 93.5 58.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 628
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z8X RELATED DB: PDB
REMARK 900 PML CLOSED CONFORMATION
REMARK 900 RELATED ID: 2ZVD RELATED DB: PDB
REMARK 900 PML OPEN CONFORMATION
REMARK 900 RELATED ID: 2ZJ6 RELATED DB: PDB
REMARK 900 D337A MUTANT, CLOSED CONFORMATION
REMARK 900 RELATED ID: 2ZJ7 RELATED DB: PDB
REMARK 900 D157A MUTANT, CLOSED CONFORMATION
REMARK 900 RELATED ID: 2Z8Z RELATED DB: PDB
REMARK 900 PML CLOSED CONFORMATION, PT-DERIVATIZED
REMARK 900 RELATED ID: 3A70 RELATED DB: PDB
DBREF 3A6Z A 1 617 UNP Q9RBY1 Q9RBY1_9PSED 1 617
DBREF 3A6Z C 1 617 UNP Q9RBY1 Q9RBY1_9PSED 1 617
SEQRES 1 A 617 MET GLY VAL TYR ASP TYR LYS ASN PHE GLY THR ALA ASP
SEQRES 2 A 617 SER LYS ALA LEU PHE SER ASP ALA MET ALA ILE THR LEU
SEQRES 3 A 617 TYR SER TYR HIS ASN LEU ASP ASN GLY PHE ALA ALA GLY
SEQRES 4 A 617 TYR GLN HIS ASN GLY PHE GLY LEU GLY LEU PRO ALA THR
SEQRES 5 A 617 LEU VAL THR ALA LEU LEU GLY GLY THR ASP SER GLN GLY
SEQRES 6 A 617 VAL ILE PRO GLY ILE PRO TRP ASN PRO ASP SER GLU LYS
SEQRES 7 A 617 LEU ALA LEU ASP ALA VAL LYS LYS ALA GLY TRP THR PRO
SEQRES 8 A 617 ILE THR ALA SER GLN LEU GLY TYR ASP GLY LYS THR ASP
SEQRES 9 A 617 ALA ARG GLY THR PHE PHE GLY GLU LYS ALA GLY TYR THR
SEQRES 10 A 617 THR ALA GLN VAL GLU ILE LEU GLY LYS TYR ASP ALA GLN
SEQRES 11 A 617 GLY HIS LEU THR GLU ILE GLY ILE ALA PHE ARG GLY THR
SEQRES 12 A 617 SER GLY PRO ARG GLU ASN LEU ILE LEU ASP SER ILE GLY
SEQRES 13 A 617 ASP VAL ILE ASN ASP LEU LEU ALA ALA PHE GLY PRO LYS
SEQRES 14 A 617 ASP TYR ALA LYS ASN TYR VAL GLY GLU ALA PHE GLY ASN
SEQRES 15 A 617 LEU LEU ASN ASP VAL VAL ALA PHE ALA LYS ALA ASN GLY
SEQRES 16 A 617 LEU SER GLY LYS ASP VAL LEU VAL SER GLY HIS SER LEU
SEQRES 17 A 617 GLY GLY LEU ALA VAL ASN SER MET ALA ASP LEU SER GLY
SEQRES 18 A 617 GLY LYS TRP GLY GLY PHE PHE ALA ASP SER ASN TYR ILE
SEQRES 19 A 617 ALA TYR ALA SER PRO THR GLN SER SER THR ASP LYS VAL
SEQRES 20 A 617 LEU ASN VAL GLY TYR GLU ASN ASP PRO VAL PHE ARG ALA
SEQRES 21 A 617 LEU ASP GLY SER THR PHE THR GLY ALA SER VAL GLY VAL
SEQRES 22 A 617 HIS ASP ALA PRO LYS GLU SER ALA THR ASP ASN ILE VAL
SEQRES 23 A 617 SER PHE ASN ASP HIS TYR ALA SER THR ALA TRP ASN LEU
SEQRES 24 A 617 LEU PRO PHE SER ILE LEU ASN ILE PRO THR TRP ILE SER
SEQRES 25 A 617 HIS LEU PRO THR ALA TYR GLY ASP GLY MET ASN ARG ILE
SEQRES 26 A 617 ILE GLU SER LYS PHE TYR ASP LEU THR SER LYS ASP SER
SEQRES 27 A 617 THR ILE ILE VAL ALA ASN LEU SER ASP PRO ALA ARG ALA
SEQRES 28 A 617 ASN THR TRP VAL GLN ASP LEU ASN ARG ASN ALA GLU THR
SEQRES 29 A 617 HIS LYS GLY SER THR PHE ILE ILE GLY SER ASP SER ASN
SEQRES 30 A 617 ASP LEU ILE GLN GLY GLY SER GLY ASN ASP TYR LEU GLU
SEQRES 31 A 617 GLY ARG ALA GLY ASN ASP THR PHE ARG ASP GLY GLY GLY
SEQRES 32 A 617 TYR ASN VAL ILE LEU GLY GLY ALA GLY ASN ASN THR LEU
SEQRES 33 A 617 ASP LEU GLN LYS SER VAL ASN THR PHE ASP PHE ALA ASN
SEQRES 34 A 617 ASP GLY ALA GLY ASN LEU TYR VAL ARG ASP ALA ASN GLY
SEQRES 35 A 617 GLY ILE SER ILE THR ARG ASP ILE GLY SER ILE VAL THR
SEQRES 36 A 617 LYS GLU PRO GLY PHE LEU TRP GLY LEU PHE LYS ASP ASP
SEQRES 37 A 617 VAL THR HIS SER VAL THR ALA SER GLY LEU LYS VAL GLY
SEQRES 38 A 617 SER ASN VAL THR GLN TYR ASP ALA SER VAL LYS GLY THR
SEQRES 39 A 617 ASN GLY ALA ASP THR LEU LYS ALA HIS ALA GLY GLY ASP
SEQRES 40 A 617 TRP LEU PHE GLY LEU ASP GLY ASN ASP HIS LEU ILE GLY
SEQRES 41 A 617 GLY VAL GLY ASN ASP VAL PHE VAL GLY GLY ALA GLY ASN
SEQRES 42 A 617 ASP LEU MET GLU SER GLY GLY GLY ALA ASP THR PHE LEU
SEQRES 43 A 617 PHE ASN GLY ALA PHE GLY GLN ASP ARG VAL VAL GLY PHE
SEQRES 44 A 617 THR SER ASN ASP LYS LEU VAL PHE LEU GLY VAL GLN GLY
SEQRES 45 A 617 VAL LEU PRO ASN ASP ASP PHE ARG ALA HIS ALA SER MET
SEQRES 46 A 617 VAL GLY GLN ASP THR VAL LEU LYS PHE GLY GLY ASP SER
SEQRES 47 A 617 VAL THR LEU VAL GLY VAL ALA LEU ASN SER LEU SER ALA
SEQRES 48 A 617 ASP GLY ILE VAL ILE ALA
SEQRES 1 C 617 MET GLY VAL TYR ASP TYR LYS ASN PHE GLY THR ALA ASP
SEQRES 2 C 617 SER LYS ALA LEU PHE SER ASP ALA MET ALA ILE THR LEU
SEQRES 3 C 617 TYR SER TYR HIS ASN LEU ASP ASN GLY PHE ALA ALA GLY
SEQRES 4 C 617 TYR GLN HIS ASN GLY PHE GLY LEU GLY LEU PRO ALA THR
SEQRES 5 C 617 LEU VAL THR ALA LEU LEU GLY GLY THR ASP SER GLN GLY
SEQRES 6 C 617 VAL ILE PRO GLY ILE PRO TRP ASN PRO ASP SER GLU LYS
SEQRES 7 C 617 LEU ALA LEU ASP ALA VAL LYS LYS ALA GLY TRP THR PRO
SEQRES 8 C 617 ILE THR ALA SER GLN LEU GLY TYR ASP GLY LYS THR ASP
SEQRES 9 C 617 ALA ARG GLY THR PHE PHE GLY GLU LYS ALA GLY TYR THR
SEQRES 10 C 617 THR ALA GLN VAL GLU ILE LEU GLY LYS TYR ASP ALA GLN
SEQRES 11 C 617 GLY HIS LEU THR GLU ILE GLY ILE ALA PHE ARG GLY THR
SEQRES 12 C 617 SER GLY PRO ARG GLU ASN LEU ILE LEU ASP SER ILE GLY
SEQRES 13 C 617 ASP VAL ILE ASN ASP LEU LEU ALA ALA PHE GLY PRO LYS
SEQRES 14 C 617 ASP TYR ALA LYS ASN TYR VAL GLY GLU ALA PHE GLY ASN
SEQRES 15 C 617 LEU LEU ASN ASP VAL VAL ALA PHE ALA LYS ALA ASN GLY
SEQRES 16 C 617 LEU SER GLY LYS ASP VAL LEU VAL SER GLY HIS SER LEU
SEQRES 17 C 617 GLY GLY LEU ALA VAL ASN SER MET ALA ASP LEU SER GLY
SEQRES 18 C 617 GLY LYS TRP GLY GLY PHE PHE ALA ASP SER ASN TYR ILE
SEQRES 19 C 617 ALA TYR ALA SER PRO THR GLN SER SER THR ASP LYS VAL
SEQRES 20 C 617 LEU ASN VAL GLY TYR GLU ASN ASP PRO VAL PHE ARG ALA
SEQRES 21 C 617 LEU ASP GLY SER THR PHE THR GLY ALA SER VAL GLY VAL
SEQRES 22 C 617 HIS ASP ALA PRO LYS GLU SER ALA THR ASP ASN ILE VAL
SEQRES 23 C 617 SER PHE ASN ASP HIS TYR ALA SER THR ALA TRP ASN LEU
SEQRES 24 C 617 LEU PRO PHE SER ILE LEU ASN ILE PRO THR TRP ILE SER
SEQRES 25 C 617 HIS LEU PRO THR ALA TYR GLY ASP GLY MET ASN ARG ILE
SEQRES 26 C 617 ILE GLU SER LYS PHE TYR ASP LEU THR SER LYS ASP SER
SEQRES 27 C 617 THR ILE ILE VAL ALA ASN LEU SER ASP PRO ALA ARG ALA
SEQRES 28 C 617 ASN THR TRP VAL GLN ASP LEU ASN ARG ASN ALA GLU THR
SEQRES 29 C 617 HIS LYS GLY SER THR PHE ILE ILE GLY SER ASP SER ASN
SEQRES 30 C 617 ASP LEU ILE GLN GLY GLY SER GLY ASN ASP TYR LEU GLU
SEQRES 31 C 617 GLY ARG ALA GLY ASN ASP THR PHE ARG ASP GLY GLY GLY
SEQRES 32 C 617 TYR ASN VAL ILE LEU GLY GLY ALA GLY ASN ASN THR LEU
SEQRES 33 C 617 ASP LEU GLN LYS SER VAL ASN THR PHE ASP PHE ALA ASN
SEQRES 34 C 617 ASP GLY ALA GLY ASN LEU TYR VAL ARG ASP ALA ASN GLY
SEQRES 35 C 617 GLY ILE SER ILE THR ARG ASP ILE GLY SER ILE VAL THR
SEQRES 36 C 617 LYS GLU PRO GLY PHE LEU TRP GLY LEU PHE LYS ASP ASP
SEQRES 37 C 617 VAL THR HIS SER VAL THR ALA SER GLY LEU LYS VAL GLY
SEQRES 38 C 617 SER ASN VAL THR GLN TYR ASP ALA SER VAL LYS GLY THR
SEQRES 39 C 617 ASN GLY ALA ASP THR LEU LYS ALA HIS ALA GLY GLY ASP
SEQRES 40 C 617 TRP LEU PHE GLY LEU ASP GLY ASN ASP HIS LEU ILE GLY
SEQRES 41 C 617 GLY VAL GLY ASN ASP VAL PHE VAL GLY GLY ALA GLY ASN
SEQRES 42 C 617 ASP LEU MET GLU SER GLY GLY GLY ALA ASP THR PHE LEU
SEQRES 43 C 617 PHE ASN GLY ALA PHE GLY GLN ASP ARG VAL VAL GLY PHE
SEQRES 44 C 617 THR SER ASN ASP LYS LEU VAL PHE LEU GLY VAL GLN GLY
SEQRES 45 C 617 VAL LEU PRO ASN ASP ASP PHE ARG ALA HIS ALA SER MET
SEQRES 46 C 617 VAL GLY GLN ASP THR VAL LEU LYS PHE GLY GLY ASP SER
SEQRES 47 C 617 VAL THR LEU VAL GLY VAL ALA LEU ASN SER LEU SER ALA
SEQRES 48 C 617 ASP GLY ILE VAL ILE ALA
HET CA A 618 1
HET CA A 620 1
HET CA A 621 1
HET CA A 622 1
HET CA A 623 1
HET CA A 624 1
HET CA A 625 1
HET CA A 626 1
HET CA A 628 1
HET CA C 618 1
HET CA C 620 1
HET CA C 621 1
HET CA C 623 1
HET CA C 624 1
HET CA C 625 1
HET CA C 626 1
HET CA C 628 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 17(CA 2+)
FORMUL 20 HOH *631(H2 O)
HELIX 1 1 GLY A 10 TYR A 29 1 20
HELIX 2 2 ASP A 33 GLY A 44 1 12
HELIX 3 3 GLY A 48 GLY A 59 1 12
HELIX 4 4 ASP A 75 ALA A 87 1 13
HELIX 5 5 THR A 93 GLY A 98 1 6
HELIX 6 6 PRO A 146 GLU A 148 5 3
HELIX 7 7 ASN A 149 GLY A 167 1 19
HELIX 8 8 ASP A 170 ASN A 194 1 25
HELIX 9 9 SER A 197 LYS A 199 5 3
HELIX 10 10 SER A 207 SER A 220 1 14
HELIX 11 11 LYS A 223 SER A 231 5 9
HELIX 12 12 THR A 267 GLY A 272 5 6
HELIX 13 13 ASN A 289 SER A 294 1 6
HELIX 14 14 ALA A 296 LEU A 300 5 5
HELIX 15 15 ASN A 306 HIS A 313 5 8
HELIX 16 16 LEU A 314 SER A 328 1 15
HELIX 17 17 PHE A 330 THR A 334 5 5
HELIX 18 18 SER A 346 ALA A 351 1 6
HELIX 19 19 SER A 421 PHE A 425 5 5
HELIX 20 20 ASP A 578 ALA A 581 5 4
HELIX 21 21 ALA A 605 LEU A 609 5 5
HELIX 22 22 SER A 610 ASP A 612 5 3
HELIX 23 23 PHE C 9 TYR C 29 1 21
HELIX 24 24 ASP C 33 GLY C 44 1 12
HELIX 25 25 GLY C 48 GLY C 59 1 12
HELIX 26 26 ASP C 75 ALA C 87 1 13
HELIX 27 27 THR C 93 GLY C 98 1 6
HELIX 28 28 PRO C 146 GLU C 148 5 3
HELIX 29 29 ASN C 149 GLY C 167 1 19
HELIX 30 30 ASN C 174 ASN C 194 1 21
HELIX 31 31 SER C 197 LYS C 199 5 3
HELIX 32 32 SER C 207 SER C 220 1 14
HELIX 33 33 LYS C 223 PHE C 227 5 5
HELIX 34 34 THR C 267 GLY C 272 5 6
HELIX 35 35 ASN C 289 SER C 294 1 6
HELIX 36 36 ALA C 296 LEU C 300 5 5
HELIX 37 37 ASN C 306 HIS C 313 5 8
HELIX 38 38 LEU C 314 SER C 328 1 15
HELIX 39 39 PHE C 330 THR C 334 5 5
HELIX 40 40 SER C 346 ALA C 351 1 6
HELIX 41 41 SER C 421 PHE C 425 5 5
HELIX 42 42 ASP C 578 ALA C 581 5 4
HELIX 43 43 ALA C 605 LEU C 609 5 5
HELIX 44 44 SER C 610 ASP C 612 5 3
SHEET 1 A 3 THR A 90 PRO A 91 0
SHEET 2 A 3 GLN A 120 TYR A 127 -1 O GLY A 125 N THR A 90
SHEET 3 A 3 PHE A 109 PHE A 110 -1 N PHE A 109 O VAL A 121
SHEET 1 B 6 THR A 90 PRO A 91 0
SHEET 2 B 6 GLN A 120 TYR A 127 -1 O GLY A 125 N THR A 90
SHEET 3 B 6 LEU A 133 PHE A 140 -1 O THR A 134 N LYS A 126
SHEET 4 B 6 VAL A 201 GLY A 205 1 O SER A 204 N ILE A 138
SHEET 5 B 6 ASN A 232 TYR A 236 1 O ASN A 232 N VAL A 203
SHEET 6 B 6 VAL A 247 VAL A 250 1 O LEU A 248 N ALA A 235
SHEET 1 C 8 ILE A 285 PHE A 288 0
SHEET 2 C 8 THR A 339 ALA A 343 1 O ILE A 340 N VAL A 286
SHEET 3 C 8 THR A 369 ILE A 372 1 O PHE A 370 N ILE A 341
SHEET 4 C 8 ASP A 387 GLU A 390 1 O TYR A 388 N ILE A 371
SHEET 5 C 8 ASN A 405 LEU A 408 1 O VAL A 406 N LEU A 389
SHEET 6 C 8 ILE A 444 ARG A 448 1 O ILE A 446 N ASN A 405
SHEET 7 C 8 ASN A 434 ARG A 438 -1 N LEU A 435 O THR A 447
SHEET 8 C 8 ASP A 426 ASN A 429 -1 N ASP A 426 O ARG A 438
SHEET 1 D 8 TRP A 354 VAL A 355 0
SHEET 2 D 8 LEU A 379 GLY A 382 1 O GLN A 381 N VAL A 355
SHEET 3 D 8 THR A 397 ASP A 400 1 O ARG A 399 N ILE A 380
SHEET 4 D 8 THR A 415 ASP A 417 1 O ASP A 417 N PHE A 398
SHEET 5 D 8 SER A 452 LYS A 456 1 O VAL A 454 N LEU A 416
SHEET 6 D 8 ASP A 468 THR A 474 -1 O HIS A 471 N ILE A 453
SHEET 7 D 8 GLY A 477 VAL A 480 -1 O LYS A 479 N SER A 472
SHEET 8 D 8 ASN A 483 THR A 485 -1 O THR A 485 N LEU A 478
SHEET 1 E 6 SER A 490 LYS A 492 0
SHEET 2 E 6 TRP A 508 PHE A 510 1 O PHE A 510 N VAL A 491
SHEET 3 E 6 VAL A 526 VAL A 528 1 O VAL A 526 N LEU A 509
SHEET 4 E 6 THR A 544 PHE A 547 1 O THR A 544 N PHE A 527
SHEET 5 E 6 LYS A 564 PHE A 567 1 O VAL A 566 N PHE A 545
SHEET 6 E 6 ILE A 614 ILE A 616 1 O VAL A 615 N PHE A 567
SHEET 1 F 7 THR A 499 LYS A 501 0
SHEET 2 F 7 HIS A 517 ILE A 519 1 O ILE A 519 N LEU A 500
SHEET 3 F 7 LEU A 535 GLU A 537 1 O LEU A 535 N LEU A 518
SHEET 4 F 7 GLN A 553 VAL A 557 1 O VAL A 557 N MET A 536
SHEET 5 F 7 ASP A 597 LEU A 601 1 O THR A 600 N VAL A 556
SHEET 6 F 7 ASP A 589 PHE A 594 -1 N THR A 590 O LEU A 601
SHEET 7 F 7 ALA A 583 VAL A 586 -1 N VAL A 586 O ASP A 589
SHEET 1 G 3 TRP C 89 PRO C 91 0
SHEET 2 G 3 GLN C 120 TYR C 127 -1 O GLY C 125 N THR C 90
SHEET 3 G 3 PHE C 109 PHE C 110 -1 N PHE C 109 O VAL C 121
SHEET 1 H 6 TRP C 89 PRO C 91 0
SHEET 2 H 6 GLN C 120 TYR C 127 -1 O GLY C 125 N THR C 90
SHEET 3 H 6 LEU C 133 PHE C 140 -1 O GLY C 137 N LEU C 124
SHEET 4 H 6 VAL C 201 HIS C 206 1 O SER C 204 N ILE C 138
SHEET 5 H 6 ASN C 232 TYR C 236 1 O ASN C 232 N VAL C 203
SHEET 6 H 6 VAL C 247 VAL C 250 1 O VAL C 250 N ALA C 235
SHEET 1 I 8 ILE C 285 PHE C 288 0
SHEET 2 I 8 THR C 339 ALA C 343 1 O ILE C 340 N VAL C 286
SHEET 3 I 8 THR C 369 ILE C 372 1 O PHE C 370 N ILE C 341
SHEET 4 I 8 ASP C 387 GLU C 390 1 O TYR C 388 N ILE C 371
SHEET 5 I 8 ASN C 405 LEU C 408 1 O LEU C 408 N LEU C 389
SHEET 6 I 8 ILE C 444 ARG C 448 1 O ILE C 446 N ILE C 407
SHEET 7 I 8 LEU C 435 ARG C 438 -1 N VAL C 437 O SER C 445
SHEET 8 I 8 ASP C 426 ASN C 429 -1 N ASP C 426 O ARG C 438
SHEET 1 J 7 LEU C 379 GLY C 382 0
SHEET 2 J 7 THR C 397 ASP C 400 1 O ARG C 399 N GLY C 382
SHEET 3 J 7 ASN C 414 ASP C 417 1 O ASP C 417 N PHE C 398
SHEET 4 J 7 ILE C 450 PRO C 458 1 O VAL C 454 N LEU C 416
SHEET 5 J 7 LYS C 466 THR C 474 -1 O HIS C 471 N ILE C 453
SHEET 6 J 7 GLY C 477 VAL C 480 -1 O LYS C 479 N SER C 472
SHEET 7 J 7 ASN C 483 GLN C 486 -1 O ASN C 483 N VAL C 480
SHEET 1 K 6 SER C 490 LYS C 492 0
SHEET 2 K 6 TRP C 508 PHE C 510 1 O PHE C 510 N VAL C 491
SHEET 3 K 6 VAL C 526 VAL C 528 1 O VAL C 526 N LEU C 509
SHEET 4 K 6 THR C 544 PHE C 547 1 O THR C 544 N PHE C 527
SHEET 5 K 6 LYS C 564 PHE C 567 1 O VAL C 566 N PHE C 547
SHEET 6 K 6 ILE C 614 ILE C 616 1 O VAL C 615 N LEU C 565
SHEET 1 L 7 THR C 499 LYS C 501 0
SHEET 2 L 7 HIS C 517 ILE C 519 1 O ILE C 519 N LEU C 500
SHEET 3 L 7 LEU C 535 GLU C 537 1 O LEU C 535 N LEU C 518
SHEET 4 L 7 GLN C 553 VAL C 557 1 O ARG C 555 N MET C 536
SHEET 5 L 7 ASP C 597 LEU C 601 1 O SER C 598 N ASP C 554
SHEET 6 L 7 ASP C 589 PHE C 594 -1 N LEU C 592 O VAL C 599
SHEET 7 L 7 ALA C 583 VAL C 586 -1 N SER C 584 O VAL C 591
LINK O THR A 118 CA CA A 628 1555 1555 2.29
LINK OE1 GLN A 120 CA CA A 628 1555 1555 2.32
LINK O SER A 144 CA CA A 628 1555 1555 2.58
LINK OD2 ASP A 153 CA CA A 628 1555 1555 2.43
LINK OD1 ASP A 157 CA CA A 628 1555 1555 2.45
LINK OD2 ASP A 157 CA CA A 628 1555 1555 2.59
LINK OE2 GLU A 253 CA CA A 618 1555 1555 2.38
LINK OD1 ASP A 275 CA CA A 618 1555 1555 2.40
LINK OD2 ASP A 275 CA CA A 618 1555 1555 2.57
LINK O ASP A 283 CA CA A 618 1555 1555 2.39
LINK OD1 ASN A 284 CA CA A 618 1555 1555 2.42
LINK O SER A 374 CA CA A 620 1555 1555 2.29
LINK O SER A 376 CA CA A 620 1555 1555 2.45
LINK OD2 ASP A 378 CA CA A 620 1555 1555 2.37
LINK O GLY A 383 CA CA A 621 1555 1555 2.31
LINK O GLY A 385 CA CA A 621 1555 1555 2.55
LINK OD2 ASP A 387 CA CA A 621 1555 1555 2.25
LINK O GLY A 391 CA CA A 620 1555 1555 2.36
LINK O ARG A 392 CA CA A 622 1555 1555 2.47
LINK O ALA A 393 CA CA A 620 1555 1555 2.31
LINK O GLY A 394 CA CA A 622 1555 1555 2.60
LINK OD1 ASP A 396 CA CA A 620 1555 1555 2.40
LINK OD2 ASP A 396 CA CA A 620 1555 1555 2.60
LINK OD2 ASP A 396 CA CA A 622 1555 1555 2.47
LINK OD1 ASP A 400 CA CA A 621 1555 1555 2.52
LINK OD2 ASP A 400 CA CA A 621 1555 1555 2.51
LINK O GLY A 402 CA CA A 621 1555 1555 2.45
LINK OD1 ASN A 405 CA CA A 621 1555 1555 2.33
LINK O GLY A 409 CA CA A 622 1555 1555 2.34
LINK O ALA A 411 CA CA A 622 1555 1555 2.40
LINK OD1 ASN A 414 CA CA A 622 1555 1555 2.53
LINK O THR A 494 CA CA A 623 1555 1555 2.25
LINK O GLY A 496 CA CA A 623 1555 1555 2.36
LINK OD2 ASP A 498 CA CA A 623 1555 1555 2.35
LINK O GLY A 511 CA CA A 623 1555 1555 2.36
LINK O LEU A 512 CA CA A 624 1555 1555 2.45
LINK O ASP A 513 CA CA A 623 1555 1555 2.39
LINK O GLY A 514 CA CA A 624 1555 1555 2.37
LINK OD1 ASP A 516 CA CA A 624 1555 1555 2.27
LINK OD1 ASP A 516 CA CA A 623 1555 1555 2.97
LINK OD2 ASP A 516 CA CA A 623 1555 1555 2.38
LINK O GLY A 521 CA CA A 625 1555 1555 2.59
LINK O GLY A 523 CA CA A 625 1555 1555 2.60
LINK OD2 ASP A 525 CA CA A 625 1555 1555 2.42
LINK O GLY A 529 CA CA A 624 1555 1555 2.50
LINK O GLY A 530 CA CA A 626 1555 1555 2.46
LINK O ALA A 531 CA CA A 624 1555 1555 2.46
LINK O GLY A 532 CA CA A 626 1555 1555 2.50
LINK OD1 ASP A 534 CA CA A 624 1555 1555 2.31
LINK OD2 ASP A 534 CA CA A 626 1555 1555 2.23
LINK O SER A 538 CA CA A 625 1555 1555 2.51
LINK O GLY A 540 CA CA A 625 1555 1555 2.32
LINK OD1 ASP A 543 CA CA A 625 1555 1555 2.41
LINK OD2 ASP A 543 CA CA A 625 1555 1555 2.64
LINK O PHE A 551 CA CA A 626 1555 1555 2.23
LINK OD1 ASP A 554 CA CA A 626 1555 1555 2.48
LINK O THR C 118 CA CA C 628 1555 1555 2.31
LINK OE1 GLN C 120 CA CA C 628 1555 1555 2.37
LINK O SER C 144 CA CA C 628 1555 1555 2.49
LINK OD2 ASP C 153 CA CA C 628 1555 1555 2.34
LINK OD1 ASP C 157 CA CA C 628 1555 1555 2.61
LINK OD2 ASP C 157 CA CA C 628 1555 1555 2.40
LINK OE2 GLU C 253 CA CA C 618 1555 1555 2.34
LINK OD1 ASP C 275 CA CA C 618 1555 1555 2.55
LINK OD2 ASP C 275 CA CA C 618 1555 1555 2.54
LINK O ASP C 283 CA CA C 618 1555 1555 2.41
LINK OD1 ASN C 284 CA CA C 618 1555 1555 2.35
LINK O SER C 374 CA CA C 620 1555 1555 2.34
LINK O SER C 376 CA CA C 620 1555 1555 2.41
LINK OD2 ASP C 378 CA CA C 620 1555 1555 2.40
LINK O GLY C 383 CA CA C 621 1555 1555 2.48
LINK O GLY C 385 CA CA C 621 1555 1555 2.48
LINK OD2 ASP C 387 CA CA C 621 1555 1555 2.48
LINK O GLY C 391 CA CA C 620 1555 1555 2.32
LINK O ALA C 393 CA CA C 620 1555 1555 2.41
LINK OD1 ASP C 396 CA CA C 620 1555 1555 2.44
LINK OD2 ASP C 396 CA CA C 620 1555 1555 2.56
LINK OD1 ASP C 400 CA CA C 621 1555 1555 2.52
LINK OD2 ASP C 400 CA CA C 621 1555 1555 2.37
LINK O GLY C 402 CA CA C 621 1555 1555 2.32
LINK OD1 ASN C 405 CA CA C 621 1555 1555 2.35
LINK O THR C 494 CA CA C 623 1555 1555 2.27
LINK O GLY C 496 CA CA C 623 1555 1555 2.59
LINK OD2 ASP C 498 CA CA C 623 1555 1555 2.43
LINK O GLY C 511 CA CA C 623 1555 1555 2.34
LINK O LEU C 512 CA CA C 624 1555 1555 2.25
LINK O ASP C 513 CA CA C 623 1555 1555 2.33
LINK O GLY C 514 CA CA C 624 1555 1555 2.50
LINK OD1 ASP C 516 CA CA C 624 1555 1555 2.50
LINK OD1 ASP C 516 CA CA C 623 1555 1555 2.79
LINK OD2 ASP C 516 CA CA C 623 1555 1555 2.43
LINK O GLY C 521 CA CA C 625 1555 1555 2.64
LINK O GLY C 523 CA CA C 625 1555 1555 2.54
LINK OD2 ASP C 525 CA CA C 625 1555 1555 2.39
LINK O GLY C 529 CA CA C 624 1555 1555 2.40
LINK O GLY C 530 CA CA C 626 1555 1555 2.46
LINK O ALA C 531 CA CA C 624 1555 1555 2.45
LINK O GLY C 532 CA CA C 626 1555 1555 2.53
LINK OD1 ASP C 534 CA CA C 624 1555 1555 2.30
LINK OD2 ASP C 534 CA CA C 626 1555 1555 2.26
LINK O SER C 538 CA CA C 625 1555 1555 2.54
LINK O GLY C 540 CA CA C 625 1555 1555 2.41
LINK OD1 ASP C 543 CA CA C 625 1555 1555 2.46
LINK OD2 ASP C 543 CA CA C 625 1555 1555 2.63
LINK O PHE C 551 CA CA C 626 1555 1555 2.35
LINK OD1 ASP C 554 CA CA C 626 1555 1555 2.38
LINK OD2 ASP C 554 CA CA C 626 1555 1555 2.97
LINK CA CA A 618 O HOH A 658 1555 1555 2.47
LINK CA CA A 618 O HOH A 681 1555 1555 2.37
LINK CA CA A 626 O HOH A 761 1555 1555 2.50
LINK CA CA A 628 O HOH A 715 1555 1555 2.22
LINK CA CA C 618 O HOH C 669 1555 1555 2.46
LINK CA CA C 618 O HOH C 698 1555 1555 2.58
LINK CA CA C 626 O HOH C 675 1555 1555 2.21
LINK CA CA C 628 O HOH C 699 1555 1555 2.32
LINK OD2 ASP A 554 CA CA A 626 1555 1555 3.06
LINK OD2 ASP C 534 CA CA C 624 1555 1555 3.12
LINK OD2 ASP A 534 CA CA A 624 1555 1555 3.20
SITE 1 AC1 6 GLU A 253 ASP A 275 ASP A 283 ASN A 284
SITE 2 AC1 6 HOH A 658 HOH A 681
SITE 1 AC2 6 SER A 374 SER A 376 ASP A 378 GLY A 391
SITE 2 AC2 6 ALA A 393 ASP A 396
SITE 1 AC3 6 GLY A 383 GLY A 385 ASP A 387 ASP A 400
SITE 2 AC3 6 GLY A 402 ASN A 405
SITE 1 AC4 6 ARG A 392 GLY A 394 ASP A 396 GLY A 409
SITE 2 AC4 6 ALA A 411 ASN A 414
SITE 1 AC5 6 THR A 494 GLY A 496 ASP A 498 GLY A 511
SITE 2 AC5 6 ASP A 513 ASP A 516
SITE 1 AC6 6 LEU A 512 GLY A 514 ASP A 516 GLY A 529
SITE 2 AC6 6 ALA A 531 ASP A 534
SITE 1 AC7 6 GLY A 521 GLY A 523 ASP A 525 SER A 538
SITE 2 AC7 6 GLY A 540 ASP A 543
SITE 1 AC8 6 GLY A 530 GLY A 532 ASP A 534 PHE A 551
SITE 2 AC8 6 ASP A 554 HOH A 761
SITE 1 AC9 6 THR A 118 GLN A 120 SER A 144 ASP A 153
SITE 2 AC9 6 ASP A 157 HOH A 715
SITE 1 BC1 6 GLU C 253 ASP C 275 ASP C 283 ASN C 284
SITE 2 BC1 6 HOH C 669 HOH C 698
SITE 1 BC2 6 SER C 374 SER C 376 ASP C 378 GLY C 391
SITE 2 BC2 6 ALA C 393 ASP C 396
SITE 1 BC3 6 GLY C 383 GLY C 385 ASP C 387 ASP C 400
SITE 2 BC3 6 GLY C 402 ASN C 405
SITE 1 BC4 6 THR C 494 GLY C 496 ASP C 498 GLY C 511
SITE 2 BC4 6 ASP C 513 ASP C 516
SITE 1 BC5 6 LEU C 512 GLY C 514 ASP C 516 GLY C 529
SITE 2 BC5 6 ALA C 531 ASP C 534
SITE 1 BC6 6 GLY C 521 GLY C 523 ASP C 525 SER C 538
SITE 2 BC6 6 GLY C 540 ASP C 543
SITE 1 BC7 6 GLY C 530 GLY C 532 ASP C 534 PHE C 551
SITE 2 BC7 6 ASP C 554 HOH C 675
SITE 1 BC8 6 THR C 118 GLN C 120 SER C 144 ASP C 153
SITE 2 BC8 6 ASP C 157 HOH C 699
CRYST1 104.382 104.382 495.175 90.00 90.00 120.00 P 65 2 2 24
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 0.009580 0.005531 0.000000 0.00000
SCALE2 0.000000 0.011062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002019 0.00000
TER 4526 ALA A 617
TER 9080 ALA C 617
MASTER 662 0 17 44 75 0 34 6 9726 2 147 96
END |