HEADER METAL BINDING PROTEIN 28-MAR-11 3RB5
TITLE CRYSTAL STRUCTURE OF CALCIUM BINDING DOMAIN CBD12 OF CALX1.1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NA/CA EXCHANGE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 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
KEYWDS CBD12, CALCIUM BINDING AND REGULATION, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WU,L.ZHENG
REVDAT 3 21-FEB-24 3RB5 1 REMARK LINK
REVDAT 2 08-NOV-17 3RB5 1 REMARK
REVDAT 1 02-NOV-11 3RB5 0
JRNL AUTH M.WU,S.TONG,J.GONZALEZ,V.JAYARAMAN,J.L.SPUDICH,L.ZHENG
JRNL TITL STRUCTURAL BASIS OF THE CA(2+) INHIBITORY MECHANISM OF
JRNL TITL 2 DROSOPHILA NA(+)/CA(2+) EXCHANGER CALX AND ITS MODIFICATION
JRNL TITL 3 BY ALTERNATIVE SPLICING.
JRNL REF STRUCTURE V. 19 1509 2011
JRNL REFN ISSN 0969-2126
JRNL PMID 22000518
JRNL DOI 10.1016/J.STR.2011.07.008
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 34576
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1820
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064713.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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 : ROSENBAUM-ROCK SI(111) SAGITALLY
REMARK 200 FOCUSED MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36396
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
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 (%): 63.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.4 M AMMONIUM
REMARK 280 SULFATE, 16% POLYETHYLENE GLYCOL 3350, PH 5.5, EVAPORATION,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.74950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 170.62425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.87475
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -56.87475
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 433
REMARK 465 ASP A 434
REMARK 465 ASP A 435
REMARK 465 GLU A 436
REMARK 465 GLU A 437
REMARK 465 ALA A 438
REMARK 465 ASP A 439
REMARK 465 ASP A 440
REMARK 465 PRO A 441
REMARK 465 THR A 597
REMARK 465 ALA A 598
REMARK 465 THR A 599
REMARK 465 GLU A 600
REMARK 465 SER A 601
REMARK 465 ILE A 626
REMARK 465 LEU A 627
REMARK 465 GLU A 628
REMARK 465 GLU A 629
REMARK 465 SER A 630
REMARK 465 SER A 631
REMARK 465 TYR A 632
REMARK 465 GLU A 633
REMARK 465 LYS A 634
REMARK 465 GLU A 694
REMARK 465 SER A 695
REMARK 465 GLN A 696
REMARK 465 GLU A 697
REMARK 465 PHE A 698
REMARK 465 LYS A 699
REMARK 465 ALA A 700
REMARK 465 THR A 701
REMARK 465 VAL A 702
REMARK 465 ASP A 703
REMARK 465 LYS A 704
REMARK 465 LEU A 705
REMARK 465 VAL A 706
REMARK 465 ALA A 707
REMARK 465 LYS A 708
REMARK 465 ALA A 709
REMARK 465 ASN A 710
REMARK 465 VAL A 711
REMARK 465 SER A 712
REMARK 465 ALA A 713
REMARK 465 VAL A 714
REMARK 465 LEU A 715
REMARK 465 GLY A 716
REMARK 465 THR A 717
REMARK 465 SER A 718
REMARK 465 SER A 719
REMARK 465 TRP A 720
REMARK 465 LYS A 721
REMARK 465 GLU A 722
REMARK 465 GLN A 723
REMARK 465 PHE A 724
REMARK 465 LYS A 725
REMARK 465 ASP A 726
REMARK 465 ALA A 727
REMARK 465 LEU A 728
REMARK 465 THR A 729
REMARK 465 VAL A 730
REMARK 465 GLY B 433
REMARK 465 ASP B 434
REMARK 465 ASP B 435
REMARK 465 GLU B 436
REMARK 465 GLU B 437
REMARK 465 ALA B 438
REMARK 465 ASP B 439
REMARK 465 ASP B 440
REMARK 465 PRO B 441
REMARK 465 SER B 630
REMARK 465 SER B 631
REMARK 465 TYR B 632
REMARK 465 GLU B 633
REMARK 465 LYS B 634
REMARK 465 ASP B 635
REMARK 465 ARG B 693
REMARK 465 GLU B 694
REMARK 465 SER B 695
REMARK 465 GLN B 696
REMARK 465 GLU B 697
REMARK 465 PHE B 698
REMARK 465 LYS B 699
REMARK 465 ALA B 700
REMARK 465 THR B 701
REMARK 465 VAL B 702
REMARK 465 ASP B 703
REMARK 465 LYS B 704
REMARK 465 LEU B 705
REMARK 465 VAL B 706
REMARK 465 ALA B 707
REMARK 465 LYS B 708
REMARK 465 ALA B 709
REMARK 465 ASN B 710
REMARK 465 VAL B 711
REMARK 465 SER B 712
REMARK 465 ALA B 713
REMARK 465 VAL B 714
REMARK 465 LEU B 715
REMARK 465 GLY B 716
REMARK 465 THR B 717
REMARK 465 SER B 718
REMARK 465 SER B 719
REMARK 465 TRP B 720
REMARK 465 LYS B 721
REMARK 465 GLU B 722
REMARK 465 GLN B 723
REMARK 465 PHE B 724
REMARK 465 LYS B 725
REMARK 465 ASP B 726
REMARK 465 ALA B 727
REMARK 465 LEU B 728
REMARK 465 THR B 729
REMARK 465 VAL B 730
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 ILE A 442 N
REMARK 470 ILE B 442 N
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 GLU A 447 115.45 -177.65
REMARK 500 GLU A 459 178.72 177.54
REMARK 500 SER A 471 -38.69 -12.91
REMARK 500 ARG A 494 107.09 -165.02
REMARK 500 PHE A 509 128.08 178.80
REMARK 500 PHE A 530 -161.03 -121.27
REMARK 500 ASN A 531 45.95 37.21
REMARK 500 ALA A 539 -152.31 -110.97
REMARK 500 ASP A 551 41.30 -145.32
REMARK 500 GLU A 568 -67.79 -7.93
REMARK 500 ARG A 572 167.19 170.72
REMARK 500 PHE A 573 99.68 147.63
REMARK 500 SER A 581 82.35 -65.47
REMARK 500 VAL A 589 108.88 -164.25
REMARK 500 ASP A 603 -35.51 -138.29
REMARK 500 GLU A 652 -34.71 -29.02
REMARK 500 PRO A 664 144.22 -39.77
REMARK 500 LEU A 668 124.28 -37.18
REMARK 500 GLU A 684 -76.35 -41.95
REMARK 500 ASP B 469 78.97 -105.49
REMARK 500 ILE B 470 12.95 -67.05
REMARK 500 ALA B 487 145.53 -40.00
REMARK 500 PRO B 501 -175.21 -59.63
REMARK 500 SER B 533 145.18 -37.14
REMARK 500 HIS B 553 -75.31 -71.39
REMARK 500 ALA B 554 -49.60 -179.15
REMARK 500 THR B 567 -108.07 -72.71
REMARK 500 GLU B 568 -106.07 -97.72
REMARK 500 SER B 581 -20.62 71.57
REMARK 500 ASP B 596 -80.09 -125.79
REMARK 500 GLU B 600 89.56 -50.39
REMARK 500 SER B 601 -67.90 132.13
REMARK 500 ASP B 603 -60.86 125.77
REMARK 500 ASN B 615 41.55 -59.59
REMARK 500 ASN B 616 0.02 178.85
REMARK 500 LEU B 627 171.15 -50.09
REMARK 500 PRO B 649 -92.43 -60.93
REMARK 500 GLU B 652 -89.86 -25.10
REMARK 500 LEU B 653 -39.64 -37.91
REMARK 500 ASP B 667 39.65 -93.20
REMARK 500 ARG B 673 -65.92 -24.80
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 ARG A 572 PHE A 573 -89.47
REMARK 500 TYR A 580 SER A 581 -149.42
REMARK 500 SER A 581 GLY A 582 54.00
REMARK 500 GLY A 582 ALA A 583 -147.30
REMARK 500 SER B 569 VAL B 570 -136.23
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 ASP A 490 OD1
REMARK 620 2 ASP A 490 OD2 46.8
REMARK 620 3 GLU A 520 OE2 88.4 60.0
REMARK 620 4 GLU A 523 OE1 50.3 62.1 51.4
REMARK 620 5 GLU A 523 OE2 76.7 109.2 84.3 48.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 455 OE2
REMARK 620 2 ASP A 515 OD2 107.3
REMARK 620 3 ASP A 516 O 109.3 69.6
REMARK 620 4 ASP A 551 OD1 89.7 108.9 160.7
REMARK 620 5 ASP A 552 OD1 122.1 119.2 62.7 104.6
REMARK 620 6 ASP A 552 OD2 79.6 128.8 60.7 122.0 45.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 455 OE2
REMARK 620 2 GLU A 455 OE1 45.2
REMARK 620 3 ASP A 516 OD2 134.1 101.3
REMARK 620 4 VAL A 518 O 146.2 158.8 77.4
REMARK 620 5 GLU A 520 OE1 86.6 55.8 97.8 103.2
REMARK 620 6 ASP A 550 OD1 65.6 81.2 152.8 90.6 60.9
REMARK 620 7 ASP A 550 OD2 79.3 115.9 142.7 67.1 100.7 42.2
REMARK 620 8 ASP A 552 OD2 90.6 130.6 96.8 70.2 162.2 102.0 61.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 18 O
REMARK 620 2 GLU A 455 OE1 118.1
REMARK 620 3 ASP A 490 OD2 136.3 100.2
REMARK 620 4 GLU A 520 OE1 98.6 60.8 81.5
REMARK 620 5 GLU A 520 OE2 91.1 104.7 57.5 46.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 490 OD2
REMARK 620 2 ASP B 490 OD1 46.8
REMARK 620 3 GLU B 520 OE2 64.4 110.9
REMARK 620 4 GLU B 523 OE2 82.5 90.3 74.0
REMARK 620 N 1 2 3
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 GLU B 455 OE2
REMARK 620 2 ASP B 515 OD2 62.4
REMARK 620 3 ASP B 516 O 71.4 68.8
REMARK 620 4 ASP B 551 OD1 69.8 112.0 134.0
REMARK 620 5 ASP B 552 OD1 93.4 154.9 98.3 60.8
REMARK 620 6 ASP B 552 OD2 60.6 109.3 56.1 83.5 48.0
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 OE1
REMARK 620 2 GLU B 455 OE2 49.6
REMARK 620 3 ASP B 516 OD2 85.5 71.6
REMARK 620 4 VAL B 518 O 139.9 149.7 80.2
REMARK 620 5 GLU B 520 OE1 71.7 108.4 66.0 68.2
REMARK 620 6 ASP B 550 OD1 78.3 79.7 151.1 127.0 128.7
REMARK 620 7 ASP B 552 OD2 113.7 64.1 76.1 98.9 141.3 88.7
REMARK 620 N 1 2 3 4 5 6
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 ASP B 490 OD2 136.2
REMARK 620 3 GLU B 520 OE2 71.2 68.8
REMARK 620 N 1 2
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 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 4984
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 731
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 732
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 731
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RB7 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE DNA SEQUENCING RESULT CONFIRMED THE RESIDUE
REMARK 999 AT THIS POSITION IS A GLU.
DBREF 3RB5 A 433 730 UNP Q24413 Q24413_DROME 433 730
DBREF 3RB5 B 433 730 UNP Q24413 Q24413_DROME 433 730
SEQADV 3RB5 GLU A 652 UNP Q24413 GLY 652 SEE REMARK 999
SEQADV 3RB5 GLU B 652 UNP Q24413 GLY 652 SEE REMARK 999
SEQRES 1 A 298 GLY ASP ASP GLU GLU ALA ASP ASP PRO ILE ARG MET TYR
SEQRES 2 A 298 PHE GLU PRO GLY HIS TYR THR VAL MET GLU ASN CYS GLY
SEQRES 3 A 298 GLU PHE GLU VAL ARG VAL VAL ARG ARG GLY ASP ILE SER
SEQRES 4 A 298 THR TYR ALA SER VAL GLU TYR GLU THR GLN ASP GLY THR
SEQRES 5 A 298 ALA SER ALA GLY THR ASP PHE VAL GLY ARG LYS GLY LEU
SEQRES 6 A 298 LEU SER PHE PRO PRO GLY VAL ASP GLU GLN ARG PHE ARG
SEQRES 7 A 298 ILE GLU VAL ILE ASP ASP ASP VAL PHE GLU GLU ASP GLU
SEQRES 8 A 298 CYS PHE TYR ILE ARG LEU PHE ASN PRO SER GLU GLY VAL
SEQRES 9 A 298 LYS LEU ALA VAL PRO MET ILE ALA THR VAL MET ILE LEU
SEQRES 10 A 298 ASP ASP ASP HIS ALA GLY ILE PHE ALA PHE THR ASP SER
SEQRES 11 A 298 VAL PHE GLU ILE THR GLU SER VAL GLY ARG PHE GLU LEU
SEQRES 12 A 298 LYS VAL MET ARG TYR SER GLY ALA ARG GLY THR VAL ILE
SEQRES 13 A 298 VAL PRO TYR TRP THR GLU ASN ASP THR ALA THR GLU SER
SEQRES 14 A 298 LYS ASP TYR GLU GLY ALA ARG GLY GLU LEU VAL PHE GLU
SEQRES 15 A 298 ASN ASN GLU SER GLU LYS PHE ILE ASP LEU PHE ILE LEU
SEQRES 16 A 298 GLU GLU SER SER TYR GLU LYS ASP VAL SER PHE LYS VAL
SEQRES 17 A 298 HIS ILE GLY GLU PRO ARG LEU ALA PRO ASP ASP GLU LEU
SEQRES 18 A 298 ALA ALA LYS ILE LYS GLU VAL GLU LYS LYS PRO VAL GLN
SEQRES 19 A 298 ASP LEU THR GLU LEU ASP ARG ILE LEU LEU LEU SER LYS
SEQRES 20 A 298 PRO ARG ASN GLY GLU LEU THR THR ALA TYR VAL ARG ILE
SEQRES 21 A 298 ARG GLU SER GLN GLU PHE LYS ALA THR VAL ASP LYS LEU
SEQRES 22 A 298 VAL ALA LYS ALA ASN VAL SER ALA VAL LEU GLY THR SER
SEQRES 23 A 298 SER TRP LYS GLU GLN PHE LYS ASP ALA LEU THR VAL
SEQRES 1 B 298 GLY ASP ASP GLU GLU ALA ASP ASP PRO ILE ARG MET TYR
SEQRES 2 B 298 PHE GLU PRO GLY HIS TYR THR VAL MET GLU ASN CYS GLY
SEQRES 3 B 298 GLU PHE GLU VAL ARG VAL VAL ARG ARG GLY ASP ILE SER
SEQRES 4 B 298 THR TYR ALA SER VAL GLU TYR GLU THR GLN ASP GLY THR
SEQRES 5 B 298 ALA SER ALA GLY THR ASP PHE VAL GLY ARG LYS GLY LEU
SEQRES 6 B 298 LEU SER PHE PRO PRO GLY VAL ASP GLU GLN ARG PHE ARG
SEQRES 7 B 298 ILE GLU VAL ILE ASP ASP ASP VAL PHE GLU GLU ASP GLU
SEQRES 8 B 298 CYS PHE TYR ILE ARG LEU PHE ASN PRO SER GLU GLY VAL
SEQRES 9 B 298 LYS LEU ALA VAL PRO MET ILE ALA THR VAL MET ILE LEU
SEQRES 10 B 298 ASP ASP ASP HIS ALA GLY ILE PHE ALA PHE THR ASP SER
SEQRES 11 B 298 VAL PHE GLU ILE THR GLU SER VAL GLY ARG PHE GLU LEU
SEQRES 12 B 298 LYS VAL MET ARG TYR SER GLY ALA ARG GLY THR VAL ILE
SEQRES 13 B 298 VAL PRO TYR TRP THR GLU ASN ASP THR ALA THR GLU SER
SEQRES 14 B 298 LYS ASP TYR GLU GLY ALA ARG GLY GLU LEU VAL PHE GLU
SEQRES 15 B 298 ASN ASN GLU SER GLU LYS PHE ILE ASP LEU PHE ILE LEU
SEQRES 16 B 298 GLU GLU SER SER TYR GLU LYS ASP VAL SER PHE LYS VAL
SEQRES 17 B 298 HIS ILE GLY GLU PRO ARG LEU ALA PRO ASP ASP GLU LEU
SEQRES 18 B 298 ALA ALA LYS ILE LYS GLU VAL GLU LYS LYS PRO VAL GLN
SEQRES 19 B 298 ASP LEU THR GLU LEU ASP ARG ILE LEU LEU LEU SER LYS
SEQRES 20 B 298 PRO ARG ASN GLY GLU LEU THR THR ALA TYR VAL ARG ILE
SEQRES 21 B 298 ARG GLU SER GLN GLU PHE LYS ALA THR VAL ASP LYS LEU
SEQRES 22 B 298 VAL ALA LYS ALA ASN VAL SER ALA VAL LEU GLY THR SER
SEQRES 23 B 298 SER TRP LYS GLU GLN PHE LYS ASP ALA LEU THR VAL
HET CA A 1 1
HET CA A 2 1
HET CA A 3 1
HET CA A 4 1
HET MPD A4984 8
HET SO4 A 731 5
HET SO4 A 732 5
HET SO4 A 7 5
HET CA B 1 1
HET CA B 2 1
HET CA B 3 1
HET CA B 4 1
HET SO4 B 731 5
HET SO4 B 6 5
HET SO4 B 5 5
HET SO4 B 8 5
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SO4 SULFATE ION
FORMUL 3 CA 8(CA 2+)
FORMUL 7 MPD C6 H14 O2
FORMUL 8 SO4 7(O4 S 2-)
FORMUL 19 HOH *42(H2 O)
HELIX 1 1 ASP A 651 GLU A 661 1 11
HELIX 2 2 THR A 669 LEU A 677 1 9
HELIX 3 3 ASP B 651 GLU B 661 1 11
HELIX 4 4 LYS B 662 LYS B 663 5 2
HELIX 5 5 PRO B 664 LEU B 668 5 5
HELIX 6 6 THR B 669 SER B 678 1 10
SHEET 1 A 4 GLU A 506 GLN A 507 0
SHEET 2 A 4 VAL A 464 ARG A 466 -1 N VAL A 464 O GLN A 507
SHEET 3 A 4 ARG A 443 PHE A 446 -1 N TYR A 445 O VAL A 465
SHEET 4 A 4 LYS A 537 LEU A 538 1 O LYS A 537 N MET A 444
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 ILE A 527 O ALA A 544
SHEET 4 B 5 ALA A 474 ASP A 482 -1 N GLN A 481 O TYR A 526
SHEET 5 B 5 LYS A 495 PHE A 500 -1 O PHE A 500 N ALA A 474
SHEET 1 C 2 PHE A 460 GLU A 461 0
SHEET 2 C 2 ARG A 510 ILE A 511 -1 O ILE A 511 N PHE A 460
SHEET 1 D 4 GLU A 619 LEU A 624 0
SHEET 2 D 4 PHE A 573 TYR A 580 -1 N LEU A 575 O ILE A 622
SHEET 3 D 4 ILE A 556 ALA A 558 -1 N ILE A 556 O TYR A 580
SHEET 4 D 4 ARG A 681 ASN A 682 1 O ARG A 681 N PHE A 557
SHEET 1 E 5 VAL A 563 ILE A 566 0
SHEET 2 E 5 THR A 687 ILE A 692 1 O ARG A 691 N ILE A 566
SHEET 3 E 5 VAL A 636 ILE A 642 -1 N VAL A 636 O ILE A 692
SHEET 4 E 5 VAL A 587 ASP A 596 -1 N GLU A 594 O LYS A 639
SHEET 5 E 5 ARG A 608 PHE A 613 -1 O LEU A 611 N VAL A 589
SHEET 1 F 5 VAL A 563 ILE A 566 0
SHEET 2 F 5 THR A 687 ILE A 692 1 O ARG A 691 N ILE A 566
SHEET 3 F 5 VAL A 636 ILE A 642 -1 N VAL A 636 O ILE A 692
SHEET 4 F 5 VAL A 587 ASP A 596 -1 N GLU A 594 O LYS A 639
SHEET 5 F 5 ARG A 646 LEU A 647 -1 O ARG A 646 N ILE A 588
SHEET 1 G 3 ARG B 443 PHE B 446 0
SHEET 2 G 3 GLU B 459 ARG B 467 -1 O VAL B 465 N TYR B 445
SHEET 3 G 3 GLU B 506 GLU B 512 -1 O PHE B 509 N VAL B 462
SHEET 1 H 5 HIS B 450 MET B 454 0
SHEET 2 H 5 ILE B 543 LEU B 549 1 O MET B 547 N TYR B 451
SHEET 3 H 5 GLU B 523 PHE B 530 -1 N PHE B 525 O VAL B 546
SHEET 4 H 5 ALA B 474 GLN B 481 -1 N GLN B 481 O TYR B 526
SHEET 5 H 5 LYS B 495 PHE B 500 -1 O LEU B 498 N VAL B 476
SHEET 1 I 4 GLU B 619 PHE B 625 0
SHEET 2 I 4 ARG B 572 TYR B 580 -1 N PHE B 573 O LEU B 624
SHEET 3 I 4 ILE B 556 PHE B 559 -1 N ILE B 556 O TYR B 580
SHEET 4 I 4 ARG B 681 ASN B 682 1 O ARG B 681 N PHE B 557
SHEET 1 J 5 VAL B 563 GLU B 565 0
SHEET 2 J 5 THR B 687 ARG B 691 1 O ARG B 691 N PHE B 564
SHEET 3 J 5 PHE B 638 ILE B 642 -1 N VAL B 640 O ALA B 688
SHEET 4 J 5 VAL B 587 GLU B 594 -1 N GLU B 594 O LYS B 639
SHEET 5 J 5 ARG B 608 PHE B 613 -1 O LEU B 611 N VAL B 589
SHEET 1 K 5 VAL B 563 GLU B 565 0
SHEET 2 K 5 THR B 687 ARG B 691 1 O ARG B 691 N PHE B 564
SHEET 3 K 5 PHE B 638 ILE B 642 -1 N VAL B 640 O ALA B 688
SHEET 4 K 5 VAL B 587 GLU B 594 -1 N GLU B 594 O LYS B 639
SHEET 5 K 5 ARG B 646 LEU B 647 -1 O ARG B 646 N ILE B 588
LINK CA CA A 1 OD1 ASP A 490 1555 1555 2.69
LINK CA CA A 1 OD2 ASP A 490 1555 1555 2.87
LINK CA CA A 1 OE2 GLU A 520 1555 1555 2.63
LINK CA CA A 1 OE1 GLU A 523 1555 1555 2.62
LINK CA CA A 1 OE2 GLU A 523 1555 1555 2.73
LINK CA CA A 2 OE2 GLU A 455 1555 1555 2.90
LINK CA CA A 2 OD2 ASP A 515 1555 1555 2.71
LINK CA CA A 2 O ASP A 516 1555 1555 2.71
LINK CA CA A 2 OD1 ASP A 551 1555 1555 2.59
LINK CA CA A 2 OD1 ASP A 552 1555 1555 2.84
LINK CA CA A 2 OD2 ASP A 552 1555 1555 2.86
LINK CA CA A 3 OE2 GLU A 455 1555 1555 2.74
LINK CA CA A 3 OE1 GLU A 455 1555 1555 2.97
LINK CA CA A 3 OD2 ASP A 516 1555 1555 2.72
LINK CA CA A 3 O VAL A 518 1555 1555 2.64
LINK CA CA A 3 OE1 GLU A 520 1555 1555 2.61
LINK CA CA A 3 OD1 ASP A 550 1555 1555 2.86
LINK CA CA A 3 OD2 ASP A 550 1555 1555 3.19
LINK CA CA A 3 OD2 ASP A 552 1555 1555 2.43
LINK CA CA A 4 O HOH A 18 1555 1555 2.89
LINK CA CA A 4 OE1 GLU A 455 1555 1555 2.71
LINK CA CA A 4 OD2 ASP A 490 1555 1555 2.78
LINK CA CA A 4 OE1 GLU A 520 1555 1555 2.47
LINK CA CA A 4 OE2 GLU A 520 1555 1555 2.95
LINK CA CA B 1 OD2 ASP B 490 1555 1555 2.60
LINK CA CA B 1 OD1 ASP B 490 1555 1555 2.90
LINK CA CA B 1 OE2 GLU B 520 1555 1555 3.14
LINK CA CA B 1 OE2 GLU B 523 1555 1555 2.66
LINK CA CA B 2 OE2 GLU B 455 1555 1555 2.94
LINK CA CA B 2 OD2 ASP B 515 1555 1555 2.40
LINK CA CA B 2 O ASP B 516 1555 1555 2.53
LINK CA CA B 2 OD1 ASP B 551 1555 1555 2.96
LINK CA CA B 2 OD1 ASP B 552 1555 1555 2.56
LINK CA CA B 2 OD2 ASP B 552 1555 1555 2.80
LINK CA CA B 3 OE1 GLU B 455 1555 1555 2.63
LINK CA CA B 3 OE2 GLU B 455 1555 1555 2.63
LINK CA CA B 3 OD2 ASP B 516 1555 1555 2.57
LINK CA CA B 3 O VAL B 518 1555 1555 2.57
LINK CA CA B 3 OE1 GLU B 520 1555 1555 2.93
LINK CA CA B 3 OD1 ASP B 550 1555 1555 2.53
LINK CA CA B 3 OD2 ASP B 552 1555 1555 2.82
LINK CA CA B 4 OE1 GLU B 455 1555 1555 2.88
LINK CA CA B 4 OD2 ASP B 490 1555 1555 2.61
LINK CA CA B 4 OE2 GLU B 520 1555 1555 2.85
CISPEP 1 GLU A 447 PRO A 448 0 -0.70
CISPEP 2 VAL A 540 PRO A 541 0 7.63
CISPEP 3 ALA A 554 GLY A 555 0 -10.12
CISPEP 4 LEU A 624 PHE A 625 0 4.25
CISPEP 5 GLU B 447 PRO B 448 0 7.87
CISPEP 6 VAL B 540 PRO B 541 0 7.70
CISPEP 7 ALA B 554 GLY B 555 0 -8.74
CISPEP 8 VAL B 570 GLY B 571 0 4.51
CISPEP 9 VAL B 636 SER B 637 0 -6.68
SITE 1 AC1 3 ASP A 490 GLU A 520 GLU A 523
SITE 1 AC2 5 GLU A 455 ASP A 515 ASP A 516 ASP A 551
SITE 2 AC2 5 ASP A 552
SITE 1 AC3 6 GLU A 455 ASP A 516 VAL A 518 GLU A 520
SITE 2 AC3 6 ASP A 550 ASP A 552
SITE 1 AC4 6 HOH A 18 GLU A 455 ASP A 490 GLU A 520
SITE 2 AC4 6 GLU A 523 ILE A 548
SITE 1 AC5 3 TYR A 689 GLN B 481 ILE B 543
SITE 1 AC6 3 LYS A 620 PHE A 621 ARG B 572
SITE 1 AC7 2 GLY A 449 HIS A 450
SITE 1 AC8 4 PRO A 448 GLU A 461 ARG A 463 ARG A 508
SITE 1 AC9 3 ASP B 490 GLU B 520 GLU B 523
SITE 1 BC1 6 GLU B 455 ASP B 515 ASP B 516 ASP B 551
SITE 2 BC1 6 ASP B 552 ARG B 584
SITE 1 BC2 6 GLU B 455 ASP B 516 VAL B 518 GLU B 520
SITE 2 BC2 6 ASP B 550 ASP B 552
SITE 1 BC3 5 GLU B 455 ASP B 490 ILE B 514 ASP B 516
SITE 2 BC3 5 GLU B 520
SITE 1 BC4 3 PRO B 448 GLY B 449 HIS B 450
SITE 1 BC5 2 ARG B 467 GLY B 468
SITE 1 BC6 3 ARG A 572 LYS B 620 PHE B 621
CRYST1 63.091 63.091 227.499 90.00 90.00 90.00 P 43 8
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 0.015850 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004396 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
