HEADER MEMBRANE PROTEIN 23-AUG-08 3E9T
TITLE CRYSTAL STRUCTURE OF APO-FORM CALX CBD1 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NA/CA EXCHANGE PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CALX CBD1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: CALX, NCX, CG5685;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CBD1, CALX, MEMBRANE, TRANSMEMBRANE, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WU,L.ZHENG
REVDAT 3 05-JUL-23 3E9T 1 JRNL REMARK LINK
REVDAT 2 13-JUL-11 3E9T 1 VERSN
REVDAT 1 01-SEP-09 3E9T 0
JRNL AUTH M.WU,H.D.LE,M.WANG,V.YURKOV,A.OMELCHENKO,M.HNATOWICH,J.NIX,
JRNL AUTH 2 L.V.HRYSHKO,L.ZHENG
JRNL TITL CRYSTAL STRUCTURES OF PROGRESSIVE CA2+ BINDING STATES OF THE
JRNL TITL 2 CA2+ SENSOR CA2+ BINDING DOMAIN 1 (CBD1) FROM THE CALX
JRNL TITL 3 NA+/CA2+ EXCHANGER REVEAL INCREMENTAL CONFORMATIONAL
JRNL TITL 4 TRANSITIONS.
JRNL REF J.BIOL.CHEM. V. 285 2554 2010
JRNL REFN ESSN 1083-351X
JRNL PMID 19815561
JRNL DOI 10.1074/JBC.M109.059162
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 73482
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3868
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5261
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 277
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3460
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 461
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
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): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.084
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.318
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3559 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4819 ; 1.634 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 439 ;12.601 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;34.716 ;23.529
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 586 ;15.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;19.643 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 523 ; 0.159 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2779 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1665 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2439 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 373 ; 0.143 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 77 ; 0.315 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 54 ; 0.263 ; 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): 2223 ; 0.833 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3512 ; 1.317 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1500 ; 2.114 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1301 ; 3.219 ; 4.500
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 442 A 550
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5213 7.3836 14.8201
REMARK 3 T TENSOR
REMARK 3 T11: -0.0651 T22: -0.0652
REMARK 3 T33: -0.0417 T12: 0.0076
REMARK 3 T13: 0.0220 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.2615 L22: 2.1964
REMARK 3 L33: 1.2728 L12: 0.5274
REMARK 3 L13: 0.0773 L23: 0.5360
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: -0.0369 S13: -0.0364
REMARK 3 S21: -0.1159 S22: -0.0020 S23: -0.1857
REMARK 3 S31: 0.0218 S32: 0.0129 S33: 0.0446
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 442 B 550
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6444 8.4900 15.7868
REMARK 3 T TENSOR
REMARK 3 T11: -0.0709 T22: -0.0482
REMARK 3 T33: -0.0517 T12: -0.0120
REMARK 3 T13: 0.0045 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.2878 L22: 2.0891
REMARK 3 L33: 1.9681 L12: -0.7660
REMARK 3 L13: -0.4865 L23: 0.7580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0424 S12: 0.0055 S13: -0.0553
REMARK 3 S21: -0.0137 S22: -0.0147 S23: 0.0600
REMARK 3 S31: 0.0266 S32: -0.0576 S33: 0.0570
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 442 C 515
REMARK 3 RESIDUE RANGE : C 522 C 549
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3463 -3.2446 28.6188
REMARK 3 T TENSOR
REMARK 3 T11: -0.0543 T22: -0.0538
REMARK 3 T33: -0.0725 T12: 0.0276
REMARK 3 T13: 0.0352 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 1.5810 L22: 1.8911
REMARK 3 L33: 2.0094 L12: 0.5689
REMARK 3 L13: -0.1903 L23: -0.1090
REMARK 3 S TENSOR
REMARK 3 S11: 0.0385 S12: -0.2222 S13: -0.0291
REMARK 3 S21: 0.1924 S22: -0.0563 S23: -0.0058
REMARK 3 S31: 0.0248 S32: -0.0071 S33: 0.0178
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 442 D 510
REMARK 3 RESIDUE RANGE : D 522 D 549
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0906 21.7976 -0.3675
REMARK 3 T TENSOR
REMARK 3 T11: -0.0901 T22: -0.0731
REMARK 3 T33: -0.0792 T12: 0.0173
REMARK 3 T13: -0.0140 T23: 0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 2.5640 L22: 3.8499
REMARK 3 L33: 2.3812 L12: -0.8434
REMARK 3 L13: 1.1655 L23: -0.7544
REMARK 3 S TENSOR
REMARK 3 S11: 0.0427 S12: -0.1764 S13: -0.2386
REMARK 3 S21: -0.0061 S22: 0.1481 S23: 0.2386
REMARK 3 S31: 0.0484 S32: -0.1712 S33: -0.1908
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3E9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049055.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73482
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 47.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS, 200 MM NH4AC, 10 MM
REMARK 280 MGCL2, 15% POLYETHYLENE GLYCOL 10,000, PH 6.5, EVAPORATION,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.54300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.45900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.21450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.45900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.54300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.21450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 552
REMARK 465 HIS A 553
REMARK 465 HIS B 553
REMARK 465 ASP C 516
REMARK 465 ASP C 517
REMARK 465 VAL C 518
REMARK 465 PHE C 519
REMARK 465 GLU C 520
REMARK 465 ASP C 550
REMARK 465 ASP C 551
REMARK 465 ASP C 552
REMARK 465 HIS C 553
REMARK 465 GLU D 440
REMARK 465 PHE D 441
REMARK 465 ASP D 516
REMARK 465 ASP D 517
REMARK 465 VAL D 518
REMARK 465 PHE D 519
REMARK 465 GLU D 520
REMARK 465 ASP D 550
REMARK 465 ASP D 551
REMARK 465 ASP D 552
REMARK 465 HIS D 553
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 GLU C 521 N
REMARK 470 GLU D 521 N
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 OE1 GLN C 481 O HOH C 569 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP B 522 NH2 ARG C 443 1655 1.92
REMARK 500 NE2 GLN B 481 NE2 GLN D 481 4555 2.01
REMARK 500 OE1 GLN D 481 O HOH B 656 4455 2.06
REMARK 500 OD1 ASP A 522 NH2 ARG D 443 4455 2.12
REMARK 500 O HOH A 690 O HOH B 668 1455 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER B 471 N - CA - C ANGL. DEV. = -19.5 DEGREES
REMARK 500 ARG C 443 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 443 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 THR C 452 N - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 SER C 471 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 ARG D 443 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG D 443 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE B 470 -13.25 -44.74
REMARK 500 SER C 471 -29.44 -159.82
REMARK 500 SER D 471 -47.71 172.93
REMARK 500 ALA D 487 20.03 -61.19
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 ILE A 470 SER A 471 -116.04
REMARK 500 ILE B 470 SER B 471 -122.91
REMARK 500 TYR C 451 THR C 452 128.14
REMARK 500 ILE C 470 SER C 471 -78.33
REMARK 500 ILE D 470 SER D 471 -46.14
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 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 455 OE1
REMARK 620 2 GLU A 455 OE2 50.9
REMARK 620 3 ASP A 516 OD2 78.0 102.5
REMARK 620 4 VAL A 518 O 140.5 168.6 83.9
REMARK 620 5 GLU A 520 OE1 63.4 113.9 67.4 77.2
REMARK 620 6 ASP A 550 OD1 81.7 87.1 143.7 93.4 76.7
REMARK 620 7 HOH A 653 O 130.4 80.3 109.0 88.7 165.7 107.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 6 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 455 OE2
REMARK 620 2 ASP A 515 OD2 84.2
REMARK 620 3 ASP A 516 O 93.9 85.6
REMARK 620 4 ASP A 551 OD1 80.4 102.2 169.8
REMARK 620 5 HOH A 653 O 75.9 149.3 73.0 97.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 490 OD1
REMARK 620 2 ASP B 490 OD2 48.0
REMARK 620 3 GLU B 520 OE2 117.9 70.8
REMARK 620 4 GLU B 523 OE1 80.9 87.5 88.0
REMARK 620 5 HOH B 613 O 67.0 114.8 164.4 78.0
REMARK 620 6 HOH B 647 O 151.6 147.0 86.6 116.2 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 455 OE2
REMARK 620 2 ASP B 515 OD2 84.7
REMARK 620 3 ASP B 516 O 97.9 94.2
REMARK 620 4 ASP B 551 OD1 75.5 99.7 163.9
REMARK 620 5 ASP B 552 OD1 113.1 161.7 79.7 89.3
REMARK 620 6 ASP B 552 OD2 65.7 144.4 72.1 91.9 49.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 455 OE1
REMARK 620 2 GLU B 455 OE2 49.3
REMARK 620 3 ASP B 516 OD2 80.9 99.9
REMARK 620 4 VAL B 518 O 148.0 162.8 86.5
REMARK 620 5 GLU B 520 OE1 61.8 109.5 80.4 87.2
REMARK 620 6 ASP B 550 OD1 87.6 85.4 159.0 94.3 78.7
REMARK 620 7 ASP B 552 OD2 129.6 81.3 101.8 81.7 168.5 99.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 5 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 455 OE1
REMARK 620 2 ASP B 490 OD2 149.2
REMARK 620 3 GLU B 520 OE1 65.5 113.0
REMARK 620 4 GLU B 520 OE2 115.9 69.7 50.4
REMARK 620 5 HOH B 575 O 80.9 92.8 145.9 162.2
REMARK 620 6 HOH B 584 O 138.9 70.5 119.3 81.6 89.5
REMARK 620 7 HOH B 608 O 70.7 140.0 74.7 91.8 100.1 72.0
REMARK 620 8 HOH B 657 O 75.1 74.8 76.5 88.6 90.1 145.2 142.0
REMARK 620 N 1 2 3 4 5 6 7
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E9U RELATED DB: PDB
REMARK 900 RELATED ID: 3EAD RELATED DB: PDB
DBREF 3E9T A 442 553 UNP Q24413 Q24413_DROME 442 553
DBREF 3E9T B 442 553 UNP Q24413 Q24413_DROME 442 553
DBREF 3E9T C 442 553 UNP Q24413 Q24413_DROME 442 553
DBREF 3E9T D 442 553 UNP Q24413 Q24413_DROME 442 553
SEQADV 3E9T GLU A 440 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T PHE A 441 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T GLU B 440 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T PHE B 441 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T GLU C 440 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T PHE C 441 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T GLU D 440 UNP Q24413 EXPRESSION TAG
SEQADV 3E9T PHE D 441 UNP Q24413 EXPRESSION TAG
SEQRES 1 A 114 GLU PHE ILE ARG MET TYR PHE GLU PRO GLY HIS TYR THR
SEQRES 2 A 114 VAL MET GLU ASN CYS GLY GLU PHE GLU VAL ARG VAL VAL
SEQRES 3 A 114 ARG ARG GLY ASP ILE SER THR TYR ALA SER VAL GLU TYR
SEQRES 4 A 114 GLU THR GLN ASP GLY THR ALA SER ALA GLY THR ASP PHE
SEQRES 5 A 114 VAL GLY ARG LYS GLY LEU LEU SER PHE PRO PRO GLY VAL
SEQRES 6 A 114 ASP GLU GLN ARG PHE ARG ILE GLU VAL ILE ASP ASP ASP
SEQRES 7 A 114 VAL PHE GLU GLU ASP GLU CYS PHE TYR ILE ARG LEU PHE
SEQRES 8 A 114 ASN PRO SER GLU GLY VAL LYS LEU ALA VAL PRO MET ILE
SEQRES 9 A 114 ALA THR VAL MET ILE LEU ASP ASP ASP HIS
SEQRES 1 B 114 GLU PHE ILE ARG MET TYR PHE GLU PRO GLY HIS TYR THR
SEQRES 2 B 114 VAL MET GLU ASN CYS GLY GLU PHE GLU VAL ARG VAL VAL
SEQRES 3 B 114 ARG ARG GLY ASP ILE SER THR TYR ALA SER VAL GLU TYR
SEQRES 4 B 114 GLU THR GLN ASP GLY THR ALA SER ALA GLY THR ASP PHE
SEQRES 5 B 114 VAL GLY ARG LYS GLY LEU LEU SER PHE PRO PRO GLY VAL
SEQRES 6 B 114 ASP GLU GLN ARG PHE ARG ILE GLU VAL ILE ASP ASP ASP
SEQRES 7 B 114 VAL PHE GLU GLU ASP GLU CYS PHE TYR ILE ARG LEU PHE
SEQRES 8 B 114 ASN PRO SER GLU GLY VAL LYS LEU ALA VAL PRO MET ILE
SEQRES 9 B 114 ALA THR VAL MET ILE LEU ASP ASP ASP HIS
SEQRES 1 C 114 GLU PHE ILE ARG MET TYR PHE GLU PRO GLY HIS TYR THR
SEQRES 2 C 114 VAL MET GLU ASN CYS GLY GLU PHE GLU VAL ARG VAL VAL
SEQRES 3 C 114 ARG ARG GLY ASP ILE SER THR TYR ALA SER VAL GLU TYR
SEQRES 4 C 114 GLU THR GLN ASP GLY THR ALA SER ALA GLY THR ASP PHE
SEQRES 5 C 114 VAL GLY ARG LYS GLY LEU LEU SER PHE PRO PRO GLY VAL
SEQRES 6 C 114 ASP GLU GLN ARG PHE ARG ILE GLU VAL ILE ASP ASP ASP
SEQRES 7 C 114 VAL PHE GLU GLU ASP GLU CYS PHE TYR ILE ARG LEU PHE
SEQRES 8 C 114 ASN PRO SER GLU GLY VAL LYS LEU ALA VAL PRO MET ILE
SEQRES 9 C 114 ALA THR VAL MET ILE LEU ASP ASP ASP HIS
SEQRES 1 D 114 GLU PHE ILE ARG MET TYR PHE GLU PRO GLY HIS TYR THR
SEQRES 2 D 114 VAL MET GLU ASN CYS GLY GLU PHE GLU VAL ARG VAL VAL
SEQRES 3 D 114 ARG ARG GLY ASP ILE SER THR TYR ALA SER VAL GLU TYR
SEQRES 4 D 114 GLU THR GLN ASP GLY THR ALA SER ALA GLY THR ASP PHE
SEQRES 5 D 114 VAL GLY ARG LYS GLY LEU LEU SER PHE PRO PRO GLY VAL
SEQRES 6 D 114 ASP GLU GLN ARG PHE ARG ILE GLU VAL ILE ASP ASP ASP
SEQRES 7 D 114 VAL PHE GLU GLU ASP GLU CYS PHE TYR ILE ARG LEU PHE
SEQRES 8 D 114 ASN PRO SER GLU GLY VAL LYS LEU ALA VAL PRO MET ILE
SEQRES 9 D 114 ALA THR VAL MET ILE LEU ASP ASP ASP HIS
HET CA A 1 1
HET CA A 6 1
HET CA B 2 1
HET CA B 3 1
HET CA B 4 1
HET CA B 5 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 6(CA 2+)
FORMUL 11 HOH *461(H2 O)
SHEET 1 A 4 GLU A 506 GLU A 512 0
SHEET 2 A 4 GLU A 459 GLY A 468 -1 N VAL A 462 O PHE A 509
SHEET 3 A 4 ILE A 442 PHE A 446 -1 N TYR A 445 O VAL A 465
SHEET 4 A 4 VAL A 536 LEU A 538 1 O LYS A 537 N ILE A 442
SHEET 1 B 5 HIS A 450 MET A 454 0
SHEET 2 B 5 ILE A 543 LEU A 549 1 O LEU A 549 N VAL A 453
SHEET 3 B 5 GLU A 523 PHE A 530 -1 N GLU A 523 O ILE A 548
SHEET 4 B 5 ALA A 474 GLN A 481 -1 N GLU A 477 O PHE A 530
SHEET 5 B 5 LYS A 495 PHE A 500 -1 O LEU A 498 N VAL A 476
SHEET 1 C 4 GLU B 506 GLU B 512 0
SHEET 2 C 4 GLU B 459 GLY B 468 -1 N VAL B 462 O PHE B 509
SHEET 3 C 4 ILE B 442 PHE B 446 -1 N ARG B 443 O ARG B 467
SHEET 4 C 4 VAL B 536 LEU B 538 1 O LYS B 537 N ILE B 442
SHEET 1 D 5 HIS B 450 MET B 454 0
SHEET 2 D 5 ILE B 543 LEU B 549 1 O LEU B 549 N VAL B 453
SHEET 3 D 5 GLU B 523 PHE B 530 -1 N GLU B 523 O ILE B 548
SHEET 4 D 5 ALA B 474 GLN B 481 -1 N GLU B 477 O PHE B 530
SHEET 5 D 5 LYS B 495 PHE B 500 -1 O LEU B 498 N VAL B 476
SHEET 1 E 4 GLU C 506 GLU C 512 0
SHEET 2 E 4 GLU C 459 GLY C 468 -1 N VAL C 462 O PHE C 509
SHEET 3 E 4 ILE C 442 PHE C 446 -1 N ARG C 443 O ARG C 467
SHEET 4 E 4 VAL C 536 LEU C 538 1 O LYS C 537 N ILE C 442
SHEET 1 F 5 HIS C 450 MET C 454 0
SHEET 2 F 5 ILE C 543 LEU C 549 1 O MET C 547 N TYR C 451
SHEET 3 F 5 GLU C 523 PHE C 530 -1 N ILE C 527 O ALA C 544
SHEET 4 F 5 ALA C 474 GLN C 481 -1 N GLU C 477 O PHE C 530
SHEET 5 F 5 LYS C 495 PHE C 500 -1 O LEU C 498 N VAL C 476
SHEET 1 G 4 GLU D 506 GLU D 512 0
SHEET 2 G 4 GLU D 459 ARG D 467 -1 N VAL D 462 O PHE D 509
SHEET 3 G 4 ARG D 443 PHE D 446 -1 N ARG D 443 O ARG D 467
SHEET 4 G 4 LYS D 537 LEU D 538 1 O LYS D 537 N MET D 444
SHEET 1 H 5 HIS D 450 MET D 454 0
SHEET 2 H 5 ILE D 543 LEU D 549 1 O LEU D 549 N VAL D 453
SHEET 3 H 5 GLU D 523 PHE D 530 -1 N GLU D 523 O ILE D 548
SHEET 4 H 5 ALA D 474 GLN D 481 -1 N GLN D 481 O TYR D 526
SHEET 5 H 5 LYS D 495 PHE D 500 -1 O LEU D 498 N VAL D 476
LINK CA CA A 1 OE1 GLU A 455 1555 1555 2.68
LINK CA CA A 1 OE2 GLU A 455 1555 1555 2.41
LINK CA CA A 1 OD2 ASP A 516 1555 1555 2.36
LINK CA CA A 1 O VAL A 518 1555 1555 2.20
LINK CA CA A 1 OE1 GLU A 520 1555 1555 2.99
LINK CA CA A 1 OD1 ASP A 550 1555 1555 2.45
LINK CA CA A 1 O HOH A 653 1555 1555 2.45
LINK CA CA A 6 OE2 GLU A 455 1555 1555 2.39
LINK CA CA A 6 OD2 ASP A 515 1555 1555 2.32
LINK CA CA A 6 O ASP A 516 1555 1555 2.40
LINK CA CA A 6 OD1 ASP A 551 1555 1555 2.22
LINK CA CA A 6 O HOH A 653 1555 1555 2.69
LINK CA CA B 2 OD1 ASP B 490 1555 1555 2.87
LINK CA CA B 2 OD2 ASP B 490 1555 1555 2.50
LINK CA CA B 2 OE2 GLU B 520 1555 1555 2.50
LINK CA CA B 2 OE1 GLU B 523 1555 1555 2.54
LINK CA CA B 2 O HOH B 613 1555 1555 2.05
LINK CA CA B 2 O HOH B 647 1555 1555 2.35
LINK CA CA B 3 OE2 GLU B 455 1555 1555 2.61
LINK CA CA B 3 OD2 ASP B 515 1555 1555 2.17
LINK CA CA B 3 O ASP B 516 1555 1555 2.22
LINK CA CA B 3 OD1 ASP B 551 1555 1555 2.39
LINK CA CA B 3 OD1 ASP B 552 1555 1555 2.36
LINK CA CA B 3 OD2 ASP B 552 1555 1555 2.79
LINK CA CA B 4 OE1 GLU B 455 1555 1555 2.81
LINK CA CA B 4 OE2 GLU B 455 1555 1555 2.39
LINK CA CA B 4 OD2 ASP B 516 1555 1555 2.32
LINK CA CA B 4 O VAL B 518 1555 1555 2.18
LINK CA CA B 4 OE1 GLU B 520 1555 1555 2.54
LINK CA CA B 4 OD1 ASP B 550 1555 1555 2.34
LINK CA CA B 4 OD2 ASP B 552 1555 1555 2.11
LINK CA CA B 5 OE1 GLU B 455 1555 1555 2.37
LINK CA CA B 5 OD2 ASP B 490 1555 1555 2.60
LINK CA CA B 5 OE1 GLU B 520 1555 1555 2.70
LINK CA CA B 5 OE2 GLU B 520 1555 1555 2.46
LINK CA CA B 5 O HOH B 575 1555 1555 2.68
LINK CA CA B 5 O HOH B 584 1555 1555 2.66
LINK CA CA B 5 O HOH B 608 1555 1555 2.83
LINK CA CA B 5 O HOH B 657 1555 1555 2.33
CISPEP 1 GLU A 447 PRO A 448 0 2.46
CISPEP 2 VAL A 540 PRO A 541 0 -0.66
CISPEP 3 GLU B 447 PRO B 448 0 3.09
CISPEP 4 VAL B 540 PRO B 541 0 -2.68
CISPEP 5 GLU C 447 PRO C 448 0 -0.83
CISPEP 6 GLU C 521 ASP C 522 0 -2.53
CISPEP 7 VAL C 540 PRO C 541 0 -6.80
CISPEP 8 GLU D 447 PRO D 448 0 0.70
CISPEP 9 VAL D 540 PRO D 541 0 -6.03
SITE 1 AC1 6 GLU A 455 ASP A 516 VAL A 518 GLU A 520
SITE 2 AC1 6 ASP A 550 HOH A 653
SITE 1 AC2 5 ASP B 490 GLU B 520 GLU B 523 HOH B 613
SITE 2 AC2 5 HOH B 647
SITE 1 AC3 5 GLU B 455 ASP B 515 ASP B 516 ASP B 551
SITE 2 AC3 5 ASP B 552
SITE 1 AC4 6 GLU B 455 ASP B 516 VAL B 518 GLU B 520
SITE 2 AC4 6 ASP B 550 ASP B 552
SITE 1 AC5 7 GLU B 455 ASP B 490 GLU B 520 HOH B 575
SITE 2 AC5 7 HOH B 584 HOH B 608 HOH B 657
SITE 1 AC6 5 GLU A 455 ASP A 515 ASP A 516 ASP A 551
SITE 2 AC6 5 HOH A 653
CRYST1 59.086 76.429 128.918 90.00 90.00 90.00 P 21 21 21 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 0.016924 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007757 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
