Header list of 2fwu.pdb file
Complete list - r 9 2 Bytes
HEADER METAL TRANSPORT REGULATOR 03-FEB-06 2FWU
TITLE SECOND CA2+ BINDING DOMAIN OF THE NA,CA-EXCHANGER (NCX1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SODIUM/CALCIUM EXCHANGER 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CBD2, CA2+ BINDING DOMAIN 2;
COMPND 5 SYNONYM: NA(+)/CA(2+)-EXCHANGE PROTEIN 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 STRAIN: FAMILIARIS;
SOURCE 6 GENE: NCX1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS BETA-SANDWICH, GREEK KEY, BETA-BULGE, CA2+ BINDING, METAL TRANSPORT
KEYWDS 2 REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.HILGE,G.W.VUISTER,J.AELEN
REVDAT 3 09-MAR-22 2FWU 1 REMARK LINK
REVDAT 2 24-FEB-09 2FWU 1 VERSN
REVDAT 1 18-APR-06 2FWU 0
JRNL AUTH M.HILGE,J.AELEN,G.W.VUISTER
JRNL TITL CA(2+) REGULATION IN THE NA(+)/CA(2+) EXCHANGER INVOLVES TWO
JRNL TITL 2 MARKEDLY DIFFERENT CA(2+) SENSORS
JRNL REF MOL.CELL V. 22 15 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16600866
JRNL DOI 10.1016/J.MOLCEL.2006.03.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, X-PLOR NIH VERSION 2.9.7
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), CLORE, G.M. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2394 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 185 DIHEDRAL ANGLE RESTRAINTS
REMARK 3 (TALOS), 8 DISTANCE CONSTRAINTS TO THE 2 CA2+ IONS
REMARK 4
REMARK 4 2FWU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036407.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 306
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20MM HEPES (SODIUM SALT)
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5-1.0MM 13C, 15N LABELED CBD2
REMARK 210 SAMPLE IN 20MM HEPES (PH 7.0),
REMARK 210 20MM BETA-MERCAPTOETHANOL BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C SEPARATED ALIPHATIC
REMARK 210 NOESY; 3D_13C SEPARATED AROMATIC
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, CYANA 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 6 GLU A 648 CD GLU A 648 OE1 -0.067
REMARK 500 7 GLU A 648 CD GLU A 648 OE1 -0.078
REMARK 500 13 GLU A 579 CD GLU A 579 OE2 -0.085
REMARK 500 14 GLU A 580 CD GLU A 580 OE1 -0.073
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 1 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 2 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 3 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 6 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 6 GLU A 648 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 7 GLU A 648 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 8 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 9 GLU A 579 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 9 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 10 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 11 GLU A 516 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 11 GLU A 582 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 14 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 16 SER A 529 N - CA - CB ANGL. DEV. = -9.5 DEGREES
REMARK 500 18 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 19 GLU A 648 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 20 GLU A 516 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 20 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 20 GLU A 582 OE1 - CD - OE2 ANGL. DEV. = -7.5 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 1 ALA A 502 -70.40 170.79
REMARK 500 1 VAL A 568 -171.73 44.49
REMARK 500 1 THR A 609 82.10 67.01
REMARK 500 1 ASP A 613 -141.04 -103.71
REMARK 500 1 PRO A 617 -159.64 -71.39
REMARK 500 1 GLU A 638 -71.40 -84.54
REMARK 500 1 LYS A 641 129.44 -178.33
REMARK 500 1 TYR A 650 -68.35 -141.42
REMARK 500 1 GLU A 651 152.93 173.85
REMARK 500 2 ALA A 502 -39.38 -155.93
REMARK 500 2 SER A 517 70.16 -102.60
REMARK 500 2 ARG A 532 74.96 -114.94
REMARK 500 2 VAL A 568 155.50 49.97
REMARK 500 2 GLU A 579 -38.19 -166.71
REMARK 500 2 LYS A 603 -73.30 -112.88
REMARK 500 2 THR A 609 122.91 -172.81
REMARK 500 2 TYR A 612 67.42 62.32
REMARK 500 2 PRO A 617 -168.43 -62.94
REMARK 500 2 TYR A 650 -55.94 -151.42
REMARK 500 2 GLU A 651 -162.99 -164.60
REMARK 500 3 ALA A 502 15.89 -150.04
REMARK 500 3 SER A 517 75.07 -107.95
REMARK 500 3 GLU A 551 -65.75 -101.41
REMARK 500 3 VAL A 568 165.82 49.54
REMARK 500 3 PRO A 617 -168.68 -79.35
REMARK 500 3 LYS A 621 -65.09 67.26
REMARK 500 3 GLU A 622 -40.15 171.70
REMARK 500 3 LYS A 641 137.25 -175.23
REMARK 500 3 SER A 649 40.11 -85.52
REMARK 500 3 VAL A 656 93.18 46.81
REMARK 500 4 THR A 545 14.07 -143.17
REMARK 500 4 VAL A 568 153.75 58.66
REMARK 500 4 LYS A 583 -157.73 -89.26
REMARK 500 4 MET A 599 78.68 60.64
REMARK 500 4 ILE A 608 79.32 72.56
REMARK 500 4 THR A 609 -175.15 178.77
REMARK 500 4 PRO A 617 174.73 -56.24
REMARK 500 4 THR A 619 131.93 72.33
REMARK 500 4 GLU A 622 -7.24 74.93
REMARK 500 4 SER A 649 85.93 28.56
REMARK 500 4 TYR A 650 -72.09 -96.18
REMARK 500 5 GLU A 551 -70.39 -84.29
REMARK 500 5 VAL A 568 176.28 50.14
REMARK 500 5 GLU A 580 -156.27 -122.64
REMARK 500 5 LYS A 583 -158.75 -85.64
REMARK 500 5 GLU A 601 92.59 59.38
REMARK 500 5 LEU A 618 99.55 -67.27
REMARK 500 5 GLU A 622 -3.82 68.60
REMARK 500 5 GLU A 638 -66.78 -127.53
REMARK 500 5 LYS A 641 132.10 -177.49
REMARK 500
REMARK 500 THIS ENTRY HAS 210 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 8 ARG A 547 0.08 SIDE CHAIN
REMARK 500 11 ARG A 547 0.08 SIDE CHAIN
REMARK 500 11 ARG A 595 0.10 SIDE CHAIN
REMARK 500 12 ARG A 626 0.09 SIDE CHAIN
REMARK 500 13 ARG A 527 0.07 SIDE CHAIN
REMARK 500 18 ARG A 595 0.09 SIDE CHAIN
REMARK 500 18 ARG A 626 0.08 SIDE CHAIN
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 800 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 516 OE1
REMARK 620 2 GLU A 516 OE2 65.9
REMARK 620 3 ASP A 578 OD1 82.2 110.1
REMARK 620 4 ASP A 578 OD2 85.4 115.0 5.0
REMARK 620 5 GLU A 582 OE1 163.7 98.6 99.4 97.4
REMARK 620 6 GLU A 648 OE1 96.6 112.1 133.0 129.0 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 850 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 552 OD2
REMARK 620 2 ASP A 578 OD2 90.0
REMARK 620 3 ASP A 578 OD1 91.8 3.4
REMARK 620 4 GLU A 579 OE1 107.3 121.1 117.7
REMARK 620 5 GLU A 579 OE2 86.9 154.7 152.1 37.8
REMARK 620 6 GLU A 580 OE1 161.5 90.2 89.3 88.4 100.6
REMARK 620 7 GLU A 580 OE2 100.8 131.8 134.0 100.4 73.3 65.8
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 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 850
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FWS RELATED DB: PDB
REMARK 900 FIRST CA2+ BINDING DOMAIN OF THE NA,CA-EXCHANGER (NCX1)
DBREF 2FWU A 501 657 UNP P23685 NAC1_CANFA 533 724
SEQRES 1 A 157 HIS ALA GLY ILE PHE THR PHE GLU GLU PRO VAL THR HIS
SEQRES 2 A 157 VAL SER GLU SER ILE GLY ILE MET GLU VAL LYS VAL LEU
SEQRES 3 A 157 ARG THR SER GLY ALA ARG GLY ASN VAL ILE VAL PRO TYR
SEQRES 4 A 157 LYS THR ILE GLU GLY THR ALA ARG GLY GLY GLY GLU ASP
SEQRES 5 A 157 PHE GLU ASP THR CYS GLY GLU LEU GLU PHE GLN ASN ASP
SEQRES 6 A 157 GLU ILE VAL LYS THR ILE SER VAL LYS VAL ILE ASP ASP
SEQRES 7 A 157 GLU GLU TYR GLU LYS ASN LYS THR PHE PHE LEU GLU ILE
SEQRES 8 A 157 GLY GLU PRO ARG LEU VAL GLU MET SER GLU LYS LYS GLY
SEQRES 9 A 157 GLY PHE THR ILE THR GLU GLU TYR ASP ASP LYS GLN PRO
SEQRES 10 A 157 LEU THR SER LYS GLU GLU GLU GLU ARG ARG ILE ALA GLU
SEQRES 11 A 157 MET GLY ARG PRO ILE LEU GLY GLU HIS THR LYS LEU GLU
SEQRES 12 A 157 VAL ILE ILE GLU GLU SER TYR GLU PHE LYS SER THR VAL
SEQRES 13 A 157 ASP
HET CA A 800 1
HET CA A 850 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 GLU A 624 GLY A 632 1 9
SHEET 1 A 4 THR A 506 PHE A 507 0
SHEET 2 A 4 ILE A 520 LEU A 526 -1 O LEU A 526 N THR A 506
SHEET 3 A 4 THR A 570 VAL A 575 -1 O VAL A 573 N MET A 521
SHEET 4 A 4 PHE A 553 GLU A 554 -1 N GLU A 554 O LYS A 574
SHEET 1 B 5 VAL A 511 SER A 515 0
SHEET 2 B 5 LEU A 642 GLU A 647 1 O GLU A 647 N VAL A 514
SHEET 3 B 5 LYS A 585 ILE A 591 -1 N LYS A 585 O ILE A 646
SHEET 4 B 5 VAL A 535 ILE A 542 -1 N ILE A 542 O PHE A 588
SHEET 5 B 5 CYS A 557 PHE A 562 -1 O LEU A 560 N VAL A 537
SHEET 1 C 5 VAL A 511 SER A 515 0
SHEET 2 C 5 LEU A 642 GLU A 647 1 O GLU A 647 N VAL A 514
SHEET 3 C 5 LYS A 585 ILE A 591 -1 N LYS A 585 O ILE A 646
SHEET 4 C 5 VAL A 535 ILE A 542 -1 N ILE A 542 O PHE A 588
SHEET 5 C 5 ARG A 595 LEU A 596 -1 O ARG A 595 N ILE A 536
LINK OE1 GLU A 516 CA CA A 800 1555 1555 2.03
LINK OE2 GLU A 516 CA CA A 800 1555 1555 1.78
LINK OD2 ASP A 552 CA CA A 850 1555 1555 1.75
LINK OD1 ASP A 578 CA CA A 800 1555 1555 4.00
LINK OD2 ASP A 578 CA CA A 800 1555 1555 1.77
LINK OD2 ASP A 578 CA CA A 850 1555 1555 4.03
LINK OD1 ASP A 578 CA CA A 850 1555 1555 1.80
LINK OE1 GLU A 579 CA CA A 850 1555 1555 1.81
LINK OE2 GLU A 579 CA CA A 850 1555 1555 3.35
LINK OE1 GLU A 580 CA CA A 850 1555 1555 1.91
LINK OE2 GLU A 580 CA CA A 850 1555 1555 1.85
LINK OE1 GLU A 582 CA CA A 800 1555 1555 1.78
LINK OE1 GLU A 648 CA CA A 800 1555 1555 1.74
SITE 1 AC1 4 GLU A 516 ASP A 578 GLU A 582 GLU A 648
SITE 1 AC2 4 ASP A 552 ASP A 578 GLU A 579 GLU A 580
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes