HEADER CELL ADHESION 30-JUN-16 5LF2
TITLE CRYSTAL STRUCTURE OF LAMININ BETA2 LE5-LF-LE6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMININ SUBUNIT BETA-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 523-833;
COMPND 5 SYNONYM: LAMININ CHAIN B3,LAMININ-11 SUBUNIT BETA,LAMININ-14 SUBUNIT
COMPND 6 BETA,LAMININ-15 SUBUNIT BETA,LAMININ-3 SUBUNIT BETA,LAMININ-4 SUBUNIT
COMPND 7 BETA,LAMININ-7 SUBUNIT BETA,LAMININ-9 SUBUNIT BETA,S-LAMININ SUBUNIT
COMPND 8 BETA,S-LAM BETA;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: SEQUENCE MISMATCH WITH UNIPROT P15800 AT RESIDUE 545
COMPND 11 (ARGININE IN THE CDNA USED TO MAKE THE EXPRESSION CONSTRUCT)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: LAMB2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCEP-PU
KEYWDS EXTRACELLULAR MATRIX, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PULIDO,E.HOHENESTER
REVDAT 2 08-MAR-17 5LF2 1 JRNL
REVDAT 1 27-JUL-16 5LF2 0
JRNL AUTH D.PULIDO,D.C.BRIGGS,J.HUA,E.HOHENESTER
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF THE LAMININ BETA 2 SHORT ARM
JRNL TITL 2 REVEALS HOW THE LF DOMAIN IS INSERTED INTO A REGULAR ARRAY
JRNL TITL 3 OF LE DOMAINS.
JRNL REF MATRIX BIOL. V.7-58 204 2017
JRNL REFN ISSN 1569-1802
JRNL PMID 27425256
JRNL DOI 10.1016/J.MATBIO.2016.06.006
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 65000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3251
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 62.9155 - 5.2603 0.98 2762 161 0.1661 0.2030
REMARK 3 2 5.2603 - 4.1755 0.99 2763 139 0.1381 0.1521
REMARK 3 3 4.1755 - 3.6477 0.98 2660 128 0.1582 0.1731
REMARK 3 4 3.6477 - 3.3143 0.99 2713 159 0.1812 0.2288
REMARK 3 5 3.3143 - 3.0767 0.99 2677 144 0.1830 0.2256
REMARK 3 6 3.0767 - 2.8953 0.99 2727 135 0.1915 0.2155
REMARK 3 7 2.8953 - 2.7503 0.98 2654 129 0.1727 0.2103
REMARK 3 8 2.7503 - 2.6306 0.99 2733 120 0.1832 0.2292
REMARK 3 9 2.6306 - 2.5293 0.99 2698 143 0.1758 0.2276
REMARK 3 10 2.5293 - 2.4420 0.99 2683 144 0.1785 0.2091
REMARK 3 11 2.4420 - 2.3657 1.00 2670 184 0.1804 0.2239
REMARK 3 12 2.3657 - 2.2980 0.99 2647 136 0.1832 0.2267
REMARK 3 13 2.2980 - 2.2375 1.00 2711 150 0.1871 0.2090
REMARK 3 14 2.2375 - 2.1830 0.99 2690 126 0.1917 0.2240
REMARK 3 15 2.1830 - 2.1333 0.98 2629 138 0.2015 0.2508
REMARK 3 16 2.1333 - 2.0879 0.98 2683 130 0.2044 0.2429
REMARK 3 17 2.0879 - 2.0462 0.99 2648 130 0.2047 0.2060
REMARK 3 18 2.0462 - 2.0075 0.99 2697 145 0.2180 0.2408
REMARK 3 19 2.0075 - 1.9717 0.99 2662 127 0.2301 0.2669
REMARK 3 20 1.9717 - 1.9383 0.99 2663 169 0.2532 0.3010
REMARK 3 21 1.9383 - 1.9070 0.99 2633 142 0.2775 0.3157
REMARK 3 22 1.9070 - 1.8777 0.99 2690 148 0.2914 0.3416
REMARK 3 23 1.8777 - 1.8500 0.99 2656 124 0.3088 0.3265
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.180
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 : 0.014 4692
REMARK 3 ANGLE : 1.280 6356
REMARK 3 CHIRALITY : 0.065 692
REMARK 3 PLANARITY : 0.009 849
REMARK 3 DIHEDRAL : 12.763 1737
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3294 43.5640 31.6553
REMARK 3 T TENSOR
REMARK 3 T11: 0.2218 T22: 0.2082
REMARK 3 T33: 0.2953 T12: -0.0049
REMARK 3 T13: -0.0615 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.6293 L22: 0.1560
REMARK 3 L33: 1.5242 L12: -0.0361
REMARK 3 L13: -0.3948 L23: -0.1501
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: -0.0051 S13: 0.0397
REMARK 3 S21: -0.0062 S22: -0.0196 S23: -0.0232
REMARK 3 S31: 0.0283 S32: -0.0208 S33: 0.0318
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 5LF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-15
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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 62.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 1.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CONDITION H4 OF THE MORPHEUS SCREEN
REMARK 280 (MOLECULAR DIMENSIONS), PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 72.16000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.16000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.67500
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
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1197 LIES ON A SPECIAL POSITION.
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 519
REMARK 465 ALA A 520
REMARK 465 LEU A 521
REMARK 465 ALA A 522
REMARK 465 ALA A 705
REMARK 465 HIS A 706
REMARK 465 PRO A 707
REMARK 465 GLU A 708
REMARK 465 THR A 709
REMARK 465 PRO A 710
REMARK 465 TYR A 711
REMARK 465 SER A 712
REMARK 465 GLY A 713
REMARK 465 GLY B 519
REMARK 465 ALA B 520
REMARK 465 LEU B 521
REMARK 465 ALA B 522
REMARK 465 ARG B 523
REMARK 465 ALA B 705
REMARK 465 HIS B 706
REMARK 465 PRO B 707
REMARK 465 GLU B 708
REMARK 465 THR B 709
REMARK 465 PRO B 710
REMARK 465 TYR B 711
REMARK 465 SER B 712
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 ARG A 523 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 526 CG OD1 OD2
REMARK 470 GLN A 536 CG CD OE1 NE2
REMARK 470 ASP A 538 CG OD1 OD2
REMARK 470 GLU A 539 CG CD OE1 OE2
REMARK 470 ARG A 545 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 578 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 581 CG1 CG2
REMARK 470 ASN A 591 CG OD1 ND2
REMARK 470 ARG A 592 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 593 CG CD OE1 OE2
REMARK 470 GLU A 766 CG CD OE1 OE2
REMARK 470 ARG B 545 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 592 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 593 CG CD OE1 OE2
REMARK 470 ARG B 704 CG CD NE CZ NH1 NH2
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 O HOH A 1244 O HOH B 1210 2656 2.19
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 GLU A 539 -148.20 60.94
REMARK 500 GLU A 593 -164.48 58.99
REMARK 500 ASN A 781 63.40 61.98
REMARK 500 MET B 622 -179.21 -170.56
REMARK 500 ASN B 781 70.86 56.15
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 B1215 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH B1216 DISTANCE = 7.97 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 A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 573 OE1
REMARK 620 2 GLU A 575 OE1 91.0
REMARK 620 3 GLU A 575 OE2 91.7 51.3
REMARK 620 4 THR A 598 O 81.4 130.9 80.4
REMARK 620 5 GLY A 601 O 171.2 84.3 79.5 96.0
REMARK 620 6 ASP A 719 O 80.5 75.7 126.3 148.0 105.4
REMARK 620 7 ASP A 719 OD1 100.5 145.8 157.6 82.9 87.5 74.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 573 OE1
REMARK 620 2 GLU B 575 OE1 92.7
REMARK 620 3 GLU B 575 OE2 92.2 52.1
REMARK 620 4 THR B 598 O 79.6 132.8 81.4
REMARK 620 5 GLY B 601 O 168.9 86.4 78.5 92.9
REMARK 620 6 ASP B 719 O 85.3 74.3 126.2 149.1 105.1
REMARK 620 7 ASP B 719 OD1 102.9 142.7 156.6 83.8 84.2 73.5
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 902
DBREF 5LF2 A 523 833 UNP P15800 LAMB2_RAT 523 833
DBREF 5LF2 B 523 833 UNP P15800 LAMB2_RAT 523 833
SEQADV 5LF2 GLY A 519 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 ALA A 520 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 LEU A 521 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 ALA A 522 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 ARG A 545 UNP P15800 PRO 545 CONFLICT
SEQADV 5LF2 GLY B 519 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 ALA B 520 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 LEU B 521 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 ALA B 522 UNP P15800 EXPRESSION TAG
SEQADV 5LF2 ARG B 545 UNP P15800 PRO 545 CONFLICT
SEQRES 1 A 315 GLY ALA LEU ALA ARG PRO CYS ASP CYS ASP VAL GLY GLY
SEQRES 2 A 315 ALA LEU ASP PRO GLN CYS ASP GLU ALA THR GLY GLN CYS
SEQRES 3 A 315 ARG CYS ARG PRO HIS MET ILE GLY ARG ARG CYS GLU GLN
SEQRES 4 A 315 VAL GLN PRO GLY TYR PHE ARG PRO PHE LEU ASP HIS LEU
SEQRES 5 A 315 THR TRP GLU ALA GLU GLY ALA HIS GLY GLN VAL LEU GLU
SEQRES 6 A 315 VAL VAL GLU ARG LEU VAL THR ASN ARG GLU THR PRO SER
SEQRES 7 A 315 TRP THR GLY VAL GLY PHE VAL ARG LEU ARG GLU GLY GLN
SEQRES 8 A 315 GLU VAL GLU PHE LEU VAL THR SER LEU PRO ARG ALA MET
SEQRES 9 A 315 ASP TYR ASP LEU LEU LEU ARG TRP GLU PRO GLN VAL PRO
SEQRES 10 A 315 GLU GLN TRP ALA GLU LEU GLU LEU VAL VAL GLN ARG PRO
SEQRES 11 A 315 GLY PRO VAL SER ALA HIS SER PRO CYS GLY HIS VAL LEU
SEQRES 12 A 315 PRO ARG ASP ASP ARG ILE GLN GLY MET LEU HIS PRO ASN
SEQRES 13 A 315 THR ARG VAL LEU VAL PHE PRO ARG PRO VAL CYS LEU GLU
SEQRES 14 A 315 PRO GLY LEU SER TYR LYS LEU LYS LEU LYS LEU THR GLY
SEQRES 15 A 315 THR GLY GLY ARG ALA HIS PRO GLU THR PRO TYR SER GLY
SEQRES 16 A 315 SER GLY ILE LEU ILE ASP SER LEU VAL LEU GLN PRO HIS
SEQRES 17 A 315 VAL LEU MET LEU GLU MET PHE SER GLY GLY ASP ALA ALA
SEQRES 18 A 315 ALA LEU GLU ARG ARG THR THR PHE GLU ARG TYR ARG CYS
SEQRES 19 A 315 HIS GLU GLU GLY LEU MET PRO SER LYS THR PRO LEU SER
SEQRES 20 A 315 GLU ALA CYS VAL PRO LEU LEU ILE SER ALA SER SER LEU
SEQRES 21 A 315 VAL TYR ASN GLY ALA LEU PRO CYS GLN CYS ASP PRO GLN
SEQRES 22 A 315 GLY SER LEU SER SER GLU CYS ASN PRO HIS GLY GLY GLN
SEQRES 23 A 315 CYS ARG CYS LYS PRO GLY VAL VAL GLY ARG ARG CYS ASP
SEQRES 24 A 315 ALA CYS ALA THR GLY TYR TYR GLY PHE GLY PRO ALA GLY
SEQRES 25 A 315 CYS GLN ALA
SEQRES 1 B 315 GLY ALA LEU ALA ARG PRO CYS ASP CYS ASP VAL GLY GLY
SEQRES 2 B 315 ALA LEU ASP PRO GLN CYS ASP GLU ALA THR GLY GLN CYS
SEQRES 3 B 315 ARG CYS ARG PRO HIS MET ILE GLY ARG ARG CYS GLU GLN
SEQRES 4 B 315 VAL GLN PRO GLY TYR PHE ARG PRO PHE LEU ASP HIS LEU
SEQRES 5 B 315 THR TRP GLU ALA GLU GLY ALA HIS GLY GLN VAL LEU GLU
SEQRES 6 B 315 VAL VAL GLU ARG LEU VAL THR ASN ARG GLU THR PRO SER
SEQRES 7 B 315 TRP THR GLY VAL GLY PHE VAL ARG LEU ARG GLU GLY GLN
SEQRES 8 B 315 GLU VAL GLU PHE LEU VAL THR SER LEU PRO ARG ALA MET
SEQRES 9 B 315 ASP TYR ASP LEU LEU LEU ARG TRP GLU PRO GLN VAL PRO
SEQRES 10 B 315 GLU GLN TRP ALA GLU LEU GLU LEU VAL VAL GLN ARG PRO
SEQRES 11 B 315 GLY PRO VAL SER ALA HIS SER PRO CYS GLY HIS VAL LEU
SEQRES 12 B 315 PRO ARG ASP ASP ARG ILE GLN GLY MET LEU HIS PRO ASN
SEQRES 13 B 315 THR ARG VAL LEU VAL PHE PRO ARG PRO VAL CYS LEU GLU
SEQRES 14 B 315 PRO GLY LEU SER TYR LYS LEU LYS LEU LYS LEU THR GLY
SEQRES 15 B 315 THR GLY GLY ARG ALA HIS PRO GLU THR PRO TYR SER GLY
SEQRES 16 B 315 SER GLY ILE LEU ILE ASP SER LEU VAL LEU GLN PRO HIS
SEQRES 17 B 315 VAL LEU MET LEU GLU MET PHE SER GLY GLY ASP ALA ALA
SEQRES 18 B 315 ALA LEU GLU ARG ARG THR THR PHE GLU ARG TYR ARG CYS
SEQRES 19 B 315 HIS GLU GLU GLY LEU MET PRO SER LYS THR PRO LEU SER
SEQRES 20 B 315 GLU ALA CYS VAL PRO LEU LEU ILE SER ALA SER SER LEU
SEQRES 21 B 315 VAL TYR ASN GLY ALA LEU PRO CYS GLN CYS ASP PRO GLN
SEQRES 22 B 315 GLY SER LEU SER SER GLU CYS ASN PRO HIS GLY GLY GLN
SEQRES 23 B 315 CYS ARG CYS LYS PRO GLY VAL VAL GLY ARG ARG CYS ASP
SEQRES 24 B 315 ALA CYS ALA THR GLY TYR TYR GLY PHE GLY PRO ALA GLY
SEQRES 25 B 315 CYS GLN ALA
HET CA A1001 1
HET CL A1002 1
HET CA B 901 1
HET CL B 902 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *435(H2 O)
HELIX 1 AA1 GLU A 575 ALA A 577 5 3
HELIX 2 AA2 LEU A 661 ASP A 664 5 4
HELIX 3 AA3 VAL A 727 MET A 729 5 3
HELIX 4 AA4 LEU A 730 GLY A 735 1 6
HELIX 5 AA5 ASP A 737 TYR A 750 1 14
HELIX 6 AA6 ARG A 751 LEU A 757 5 7
HELIX 7 AA7 ALA A 767 ASN A 781 1 15
HELIX 8 AA8 GLU B 575 ALA B 577 5 3
HELIX 9 AA9 LEU B 661 ASP B 664 5 4
HELIX 10 AB1 VAL B 727 MET B 729 5 3
HELIX 11 AB2 LEU B 730 GLY B 735 1 6
HELIX 12 AB3 ASP B 737 TYR B 750 1 14
HELIX 13 AB4 ARG B 751 LEU B 757 5 7
HELIX 14 AB5 ALA B 767 ASN B 781 1 15
SHEET 1 AA1 2 MET A 550 ILE A 551 0
SHEET 2 AA1 2 GLN A 557 VAL A 558 -1 O GLN A 557 N ILE A 551
SHEET 1 AA2 2 TYR A 562 PHE A 563 0
SHEET 2 AA2 2 LEU A 784 PRO A 785 -1 O LEU A 784 N PHE A 563
SHEET 1 AA3 4 THR A 571 GLU A 573 0
SHEET 2 AA3 4 ILE A 716 PRO A 725 -1 O LEU A 721 N TRP A 572
SHEET 3 AA3 4 MET A 622 GLU A 631 -1 N ASP A 625 O GLN A 724
SHEET 4 AA3 4 VAL A 677 VAL A 679 -1 O LEU A 678 N LEU A 628
SHEET 1 AA4 5 GLU A 583 GLU A 586 0
SHEET 2 AA4 5 GLY A 601 LEU A 605 -1 O PHE A 602 N VAL A 585
SHEET 3 AA4 5 ILE A 716 PRO A 725 -1 O ILE A 716 N LEU A 605
SHEET 4 AA4 5 MET A 622 GLU A 631 -1 N ASP A 625 O GLN A 724
SHEET 5 AA4 5 VAL A 684 LEU A 686 -1 O VAL A 684 N TYR A 624
SHEET 1 AA5 4 GLU A 610 VAL A 615 0
SHEET 2 AA5 4 TYR A 692 GLY A 702 -1 O LEU A 696 N VAL A 611
SHEET 3 AA5 4 TRP A 638 GLN A 646 -1 N VAL A 644 O LYS A 695
SHEET 4 AA5 4 ARG A 666 LEU A 671 -1 O ILE A 667 N LEU A 643
SHEET 1 AA6 2 VAL A 811 VAL A 812 0
SHEET 2 AA6 2 ALA A 818 CYS A 819 -1 O ALA A 818 N VAL A 812
SHEET 1 AA7 2 MET B 550 ILE B 551 0
SHEET 2 AA7 2 GLN B 557 VAL B 558 -1 O GLN B 557 N ILE B 551
SHEET 1 AA8 2 TYR B 562 PHE B 563 0
SHEET 2 AA8 2 LEU B 784 PRO B 785 -1 O LEU B 784 N PHE B 563
SHEET 1 AA9 4 THR B 571 GLU B 573 0
SHEET 2 AA9 4 ILE B 716 PRO B 725 -1 O LEU B 721 N TRP B 572
SHEET 3 AA9 4 MET B 622 GLU B 631 -1 N ASP B 625 O GLN B 724
SHEET 4 AA9 4 VAL B 677 VAL B 679 -1 O LEU B 678 N LEU B 628
SHEET 1 AB1 5 VAL B 584 GLU B 586 0
SHEET 2 AB1 5 GLY B 601 LEU B 605 -1 O PHE B 602 N VAL B 585
SHEET 3 AB1 5 ILE B 716 PRO B 725 -1 O ILE B 716 N LEU B 605
SHEET 4 AB1 5 MET B 622 GLU B 631 -1 N ASP B 625 O GLN B 724
SHEET 5 AB1 5 VAL B 684 LEU B 686 -1 O VAL B 684 N TYR B 624
SHEET 1 AB2 4 GLU B 610 VAL B 615 0
SHEET 2 AB2 4 TYR B 692 GLY B 702 -1 O TYR B 692 N VAL B 615
SHEET 3 AB2 4 TRP B 638 GLN B 646 -1 N GLU B 640 O GLY B 700
SHEET 4 AB2 4 ARG B 666 LEU B 671 -1 O ILE B 667 N LEU B 643
SHEET 1 AB3 2 VAL B 811 VAL B 812 0
SHEET 2 AB3 2 ALA B 818 CYS B 819 -1 O ALA B 818 N VAL B 812
SSBOND 1 CYS A 525 CYS A 537 1555 1555 2.03
SSBOND 2 CYS A 527 CYS A 544 1555 1555 2.04
SSBOND 3 CYS A 546 CYS A 555 1555 1555 2.05
SSBOND 4 CYS A 657 CYS A 685 1555 1555 2.11
SSBOND 5 CYS A 752 CYS A 768 1555 1555 2.07
SSBOND 6 CYS A 786 CYS A 798 1555 1555 2.07
SSBOND 7 CYS A 788 CYS A 805 1555 1555 2.06
SSBOND 8 CYS A 807 CYS A 816 1555 1555 2.06
SSBOND 9 CYS A 819 CYS A 831 1555 1555 2.11
SSBOND 10 CYS B 525 CYS B 537 1555 1555 2.05
SSBOND 11 CYS B 527 CYS B 544 1555 1555 2.03
SSBOND 12 CYS B 546 CYS B 555 1555 1555 2.05
SSBOND 13 CYS B 657 CYS B 685 1555 1555 2.11
SSBOND 14 CYS B 752 CYS B 768 1555 1555 2.10
SSBOND 15 CYS B 786 CYS B 798 1555 1555 2.06
SSBOND 16 CYS B 788 CYS B 805 1555 1555 2.06
SSBOND 17 CYS B 807 CYS B 816 1555 1555 2.07
SSBOND 18 CYS B 819 CYS B 831 1555 1555 2.08
LINK OE1 GLU A 573 CA CA A1001 1555 1555 2.37
LINK OE1 GLU A 575 CA CA A1001 1555 1555 2.56
LINK OE2 GLU A 575 CA CA A1001 1555 1555 2.52
LINK O THR A 598 CA CA A1001 1555 1555 2.42
LINK O GLY A 601 CA CA A1001 1555 1555 2.36
LINK O ASP A 719 CA CA A1001 1555 1555 2.56
LINK OD1 ASP A 719 CA CA A1001 1555 1555 2.32
LINK OE1 GLU B 573 CA CA B 901 1555 1555 2.29
LINK OE1 GLU B 575 CA CA B 901 1555 1555 2.49
LINK OE2 GLU B 575 CA CA B 901 1555 1555 2.48
LINK O THR B 598 CA CA B 901 1555 1555 2.43
LINK O GLY B 601 CA CA B 901 1555 1555 2.39
LINK O ASP B 719 CA CA B 901 1555 1555 2.59
LINK OD1 ASP B 719 CA CA B 901 1555 1555 2.35
SITE 1 AC1 5 GLU A 573 GLU A 575 THR A 598 GLY A 601
SITE 2 AC1 5 ASP A 719
SITE 1 AC2 1 ARG A 814
SITE 1 AC3 5 GLU B 573 GLU B 575 THR B 598 GLY B 601
SITE 2 AC3 5 ASP B 719
SITE 1 AC4 2 HIS B 569 ARG B 814
CRYST1 144.320 55.350 111.340 90.00 119.38 90.00 C 1 2 1 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 0.006929 0.000000 0.003901 0.00000
SCALE2 0.000000 0.018067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010307 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
