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HEADER LIPID BINDING PROTEIN 13-JUL-26 37CB
TITLE CRYSTAL STRUCTURE OF THERMOMYCES LANUGINOSA LIPASE WITH ACYL
TITLE 2 INTERMEDIATE: SPACE GROUP I222
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_TAXID: 5541;
SOURCE 4 GENE: LIP;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5052
KEYWDS ACYL INTERMEDIATE, FUNGAL, HYDROLASE, SUBSTRATE, CRYSTALLIZATION,
KEYWDS 2 LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCPHERSON
REVDAT 1 05-AUG-26 37CB 0
SPRSDE 05-AUG-26 37CB 6OR3
JRNL AUTH A.MCPHERSON
JRNL TITL CRYSTAL STRUCTURE OF THERMOMYCES LANUGINOSA LIPASE WITH ACYL
JRNL TITL 2 INTERMEDIATE: SPACE GROUP I222
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.1_5286
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 46144
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2287
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 60.8100 - 3.6500 1.00 2933 130 0.1328 0.1977
REMARK 3 2 3.6500 - 2.9000 1.00 2787 147 0.1240 0.2117
REMARK 3 3 2.9000 - 2.5300 1.00 2771 149 0.1410 0.2416
REMARK 3 4 2.5300 - 2.3000 1.00 2782 130 0.1470 0.2332
REMARK 3 5 2.3000 - 2.1400 1.00 2719 152 0.1542 0.2017
REMARK 3 6 2.1400 - 2.0100 1.00 2740 145 0.1646 0.2837
REMARK 3 7 2.0100 - 1.9100 1.00 2736 139 0.1773 0.2163
REMARK 3 8 1.9100 - 1.8300 1.00 2770 113 0.1960 0.2396
REMARK 3 9 1.8300 - 1.7600 1.00 2707 141 0.2234 0.3105
REMARK 3 10 1.7600 - 1.7000 1.00 2729 144 0.2482 0.3280
REMARK 3 11 1.7000 - 1.6400 1.00 2668 171 0.2493 0.3146
REMARK 3 12 1.6400 - 1.6000 1.00 2711 141 0.2616 0.3028
REMARK 3 13 1.6000 - 1.5500 1.00 2703 135 0.2823 0.3242
REMARK 3 14 1.5500 - 1.5200 1.00 2742 135 0.3285 0.3434
REMARK 3 15 1.5200 - 1.4800 1.00 2704 151 0.3495 0.4119
REMARK 3 16 1.4800 - 1.4500 0.99 2655 164 0.3944 0.4324
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.234
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.672
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.04
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 : 0.010 2307
REMARK 3 ANGLE : 1.253 3095
REMARK 3 CHIRALITY : 0.083 327
REMARK 3 PLANARITY : 0.011 400
REMARK 3 DIHEDRAL : 15.411 888
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 37CB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-26.
REMARK 100 THE DEPOSITION ID IS D_1000309832.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-19
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 4.5 - 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46198
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 61.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 62.80
REMARK 200 R MERGE (I) : 0.33400
REMARK 200 R SYM (I) : 0.33600
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 38.70
REMARK 200 R MERGE FOR SHELL (I) : 3.60000
REMARK 200 R SYM FOR SHELL (I) : 3.70000
REMARK 200 FOR SHELL : 0.600
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: RECTANGULAR BLOCKS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZED BY SITTING DROP VAPOR
REMARK 280 DIFFUSION WITH RESERVOIRS OF 0.6 ML AND DROP VOLUMES OF 6 UL.
REMARK 280 RESERVOIRS WERE 20% PEG 3350 WITH 0.1 M HEPES AT PH 6.0. DROPS
REMARK 280 WERE EQUAL AMOUNTS OF THE RESERVOIR AND A 30 MG/ML STOCK PROTEIN
REMARK 280 SOLUTION. THE SOLUTION WAS THE RAW GROWTH BROTH FOR THE
REMARK 280 ASPERGILLUS EXPRESSION SYSTEM AND THE PROTEIN WAS NOT OTHERWISE
REMARK 280 PURIFIED,, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.63400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.37050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.63400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.37050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.63400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.37050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.63400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 43.37050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 A 615 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 MET A -21
REMARK 465 ARG A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 LEU A -17
REMARK 465 VAL A -16
REMARK 465 LEU A -15
REMARK 465 PHE A -14
REMARK 465 PHE A -13
REMARK 465 VAL A -12
REMARK 465 SER A -11
REMARK 465 ALA A -10
REMARK 465 TRP A -9
REMARK 465 THR A -8
REMARK 465 ALA A -7
REMARK 465 LEU A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 PRO A -3
REMARK 465 ILE A -2
REMARK 465 ARG A -1
REMARK 465 ARG A 0
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 O HOH A 611 O HOH A 612 1.79
REMARK 500 O HOH A 537 O HOH A 549 1.85
REMARK 500 O HOH A 403 O HOH A 544 1.96
REMARK 500 O HOH A 572 O HOH A 603 2.06
REMARK 500 O HOH A 589 O HOH A 609 2.10
REMARK 500 O HOH A 578 O HOH A 587 2.13
REMARK 500 O HOH A 472 O HOH A 577 2.14
REMARK 500 O PRO A 29 O HOH A 401 2.14
REMARK 500 O HOH A 568 O HOH A 574 2.18
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 O ASN A 71 O4 PEG A 312 7557 1.90
REMARK 500 OE2 GLU A 183 O4 PEG A 313 7547 1.92
REMARK 500 O HOH A 591 O HOH A 591 3657 1.94
REMARK 500 O HOH A 421 O HOH A 583 8557 1.97
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 ASP A 27 42.03 -145.18
REMARK 500 ASN A 39 33.93 -99.57
REMARK 500 CYS A 41 63.12 -152.40
REMARK 500 ARG A 84 -46.62 -144.50
REMARK 500 SER A 146 -128.11 64.65
REMARK 500 THR A 199 -122.86 37.02
REMARK 500 PHE A 262 -38.57 71.07
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 A 611 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 612 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 613 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH A 614 DISTANCE = 9.41 ANGSTROMS
REMARK 525 HOH A 615 DISTANCE = 14.15 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 315
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 316 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 62 OD1 77.8
REMARK 620 3 ASP A 62 OD2 124.2 53.6
REMARK 620 4 HOH A 413 O 90.3 72.3 98.1
REMARK 620 5 HOH A 545 O 146.6 132.6 89.0 88.2
REMARK 620 6 HOH A 558 O 89.2 160.3 144.4 93.2 57.7
REMARK 620 7 HOH A 572 O 109.2 129.9 87.2 152.3 64.6 68.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 407 O
REMARK 620 2 HOH A 451 O 82.9
REMARK 620 3 HOH A 582 O 141.8 83.8
REMARK 620 4 HOH A 595 O 89.2 142.0 79.7
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6OR3 RELATED DB: PDB
DBREF 37CB A -21 269 UNP O59952 LIP_THELA 1 291
SEQRES 1 A 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 A 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 A 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 A 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 A 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 A 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 A 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 A 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 A 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 A 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 A 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 A 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 A 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 A 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 A 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 A 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 A 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 A 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 A 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 A 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 A 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 A 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 A 291 ILE GLY THR CYS LEU
HET CA A 301 1
HET PLM A 302 48
HET NAG A 303 27
HET PO4 A 304 5
HET PG4 A 305 31
HET PEG A 306 17
HET PG4 A 307 31
HET PEG A 308 17
HET PEG A 309 17
HET PEG A 310 17
HET PEG A 311 17
HET PEG A 312 17
HET PEG A 313 17
HET PEG A 314 17
HET PG4 A 315 18
HET CA A 316 1
HET CL A 317 1
HET PEG A 318 17
HET PEG A 319 17
HET PEG A 320 15
HET PEG A 321 17
HETNAM CA CALCIUM ION
HETNAM PLM PALMITIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 CA 2(CA 2+)
FORMUL 3 PLM C16 H32 O2
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 PO4 O4 P 3-
FORMUL 6 PG4 3(C8 H18 O5)
FORMUL 7 PEG 12(C4 H10 O3)
FORMUL 18 CL CL 1-
FORMUL 23 HOH *215(H2 O)
HELIX 1 AA1 SER A 3 ALA A 20 1 18
HELIX 2 AA2 TYR A 21 ASN A 26 5 6
HELIX 3 AA3 CYS A 41 ALA A 47 1 7
HELIX 4 AA4 SER A 85 LEU A 93 1 9
HELIX 5 AA5 ASP A 111 HIS A 135 1 25
HELIX 6 AA6 SER A 146 ARG A 160 1 15
HELIX 7 AA7 ASN A 178 GLN A 188 1 11
HELIX 8 AA8 ILE A 202 LEU A 206 5 5
HELIX 9 AA9 PRO A 208 GLY A 212 5 5
HELIX 10 AB1 THR A 231 ASN A 233 5 3
HELIX 11 AB2 ILE A 255 TRP A 260 5 6
SHEET 1 AA1 8 ALA A 49 SER A 58 0
SHEET 2 AA1 8 VAL A 63 ASP A 70 -1 O LEU A 69 N THR A 50
SHEET 3 AA1 8 LEU A 75 PHE A 80 -1 O SER A 79 N PHE A 66
SHEET 4 AA1 8 ARG A 139 HIS A 145 1 O VAL A 141 N ILE A 76
SHEET 5 AA1 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA1 8 LEU A 193 HIS A 198 1 O TYR A 194 N VAL A 168
SHEET 7 AA1 8 GLU A 219 ILE A 222 1 O ILE A 222 N THR A 197
SHEET 8 AA1 8 ILE A 235 ILE A 238 -1 O ILE A 238 N GLU A 219
SHEET 1 AA2 2 LEU A 97 GLU A 99 0
SHEET 2 AA2 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.05
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.03
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.08
LINK ND2 ASN A 33 C1 NAG A 303 1555 1555 1.42
LINK OG SER A 146 C1 PLM A 302 1555 1555 1.38
LINK OD1 ASP A 57 CA CA A 316 1555 1555 2.24
LINK OD1 ASP A 62 CA CA A 316 1555 1555 2.57
LINK OD2 ASP A 62 CA CA A 316 1555 1555 2.44
LINK CA CA A 301 O HOH A 407 1555 1555 2.18
LINK CA CA A 301 O HOH A 451 1555 1555 2.11
LINK CA CA A 301 O HOH A 582 1555 1555 2.13
LINK CA CA A 301 O HOH A 595 1555 1555 2.13
LINK CA CA A 316 O HOH A 413 1555 1555 2.17
LINK CA CA A 316 O HOH A 545 1555 1555 2.98
LINK CA CA A 316 O HOH A 558 1555 1555 2.57
LINK CA CA A 316 O HOH A 572 1555 1555 2.87
CISPEP 1 LEU A 206 PRO A 207 0 -12.89
CISPEP 2 SER A 217 PRO A 218 0 2.05
CRYST1 69.865 85.268 86.741 90.00 90.00 90.00 I 2 2 2 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 0.014313 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011529 0.00000
TER 4123 LEU A 269
MASTER 377 0 21 11 10 0 0 6 2444 1 384 23
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