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HEADER HYDROLASE/IMMUNE SYSTEM 28-JAN-15 4XWG
TITLE CRYSTAL STRUCTURE OF LCAT (C31Y) IN COMPLEX WITH FAB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB1 LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB1 HEAVY CHAIN;
COMPND 7 CHAIN: H;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PHOSPHATIDYLCHOLINE-STEROL ACYLTRANSFERASE;
COMPND 11 CHAIN: A;
COMPND 12 FRAGMENT: UNP RESIDUES 25-440;
COMPND 13 SYNONYM: LECITHIN-CHOLESTEROL ACYLTRANSFERASE,PHOSPHOLIPID-
COMPND 14 CHOLESTEROL ACYLTRANSFERASE;
COMPND 15 EC: 2.3.1.43;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: LCAT;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS A-B HYDROLASE COMPLEX, ESTERASE, ACYL TRANSFERASE, HYDROLASE-IMMUNE
KEYWDS 2 SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.PIPER,N.P.C.WALKER,W.G.ROMANOW,S.T.THIBAULT
REVDAT 1 29-JUL-15 4XWG 0
JRNL AUTH D.E.PIPER,W.G.ROMANOW,R.N.GUNAWARDANE,P.FORDSTROM,
JRNL AUTH 2 S.MASTERMAN,O.PAN,S.T.THIBAULT,R.ZHANG,D.MEININGER,
JRNL AUTH 3 M.SCHWARZ,Z.WANG,C.KING,M.ZHOU,N.P.C.WALKER
JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF HUMAN LCAT
JRNL REF J.LIPID RES. 2015
JRNL REFN ISSN 0022-2275
JRNL DOI 10.1194/JLR.M059873
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 28792
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 1414
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 34.0079 - 5.7017 1.00 2739 143 0.1738 0.2186
REMARK 3 2 5.7017 - 4.5290 1.00 2763 131 0.1545 0.1870
REMARK 3 3 4.5290 - 3.9575 1.00 2721 143 0.1467 0.2451
REMARK 3 4 3.9575 - 3.5961 1.00 2722 137 0.1659 0.2461
REMARK 3 5 3.5961 - 3.3386 1.00 2756 156 0.1802 0.2785
REMARK 3 6 3.3386 - 3.1419 1.00 2743 134 0.1975 0.3376
REMARK 3 7 3.1419 - 2.9846 1.00 2742 128 0.2108 0.3097
REMARK 3 8 2.9846 - 2.8548 1.00 2718 167 0.2174 0.2993
REMARK 3 9 2.8548 - 2.7449 1.00 2734 125 0.2269 0.3036
REMARK 3 10 2.7449 - 2.6502 1.00 2740 150 0.2380 0.3187
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.25
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 6506
REMARK 3 ANGLE : 1.540 8816
REMARK 3 CHIRALITY : 0.065 965
REMARK 3 PLANARITY : 0.008 1128
REMARK 3 DIHEDRAL : 15.724 2295
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 4XWG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28802
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 84.295
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.64400
REMARK 200 R SYM FOR SHELL (I) : 0.64400
REMARK 200 FOR SHELL : 1.200
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 (%): 53.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 0.2 M ZINC
REMARK 280 ACETATE, 0.01 M COBALT CHLORIDE, 4-8% PEG 1500, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 84.29500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.66774
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.19000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 84.29500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 48.66774
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.19000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 84.29500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 48.66774
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.19000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 97.33548
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 62.38000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 97.33548
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 62.38000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 97.33548
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 62.38000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -396.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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 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 GLU L 211
REMARK 465 CYS L 212
REMARK 465 SER L 213
REMARK 465 GLN H 1
REMARK 465 SER H 141
REMARK 465 LYS H 142
REMARK 465 SER H 143
REMARK 465 THR H 144
REMARK 465 SER H 145
REMARK 465 GLY H 146
REMARK 465 CYS H 229
REMARK 465 ALA H 230
REMARK 465 ALA H 231
REMARK 465 ALA H 232
REMARK 465 GLU H 233
REMARK 465 ASN H 234
REMARK 465 LEU H 235
REMARK 465 TYR H 236
REMARK 465 PHE H 237
REMARK 465 GLN H 238
REMARK 465 PHE A 1
REMARK 465 TRP A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 ASN A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 PHE A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 HIS A 11
REMARK 465 THR A 12
REMARK 465 THR A 13
REMARK 465 PRO A 14
REMARK 465 LYS A 15
REMARK 465 ALA A 16
REMARK 465 GLU A 17
REMARK 465 LEU A 18
REMARK 465 SER A 19
REMARK 465 ASN A 20
REMARK 465 ILE A 231
REMARK 465 PRO A 232
REMARK 465 ILE A 233
REMARK 465 MET A 234
REMARK 465 SER A 235
REMARK 465 SER A 236
REMARK 465 ILE A 237
REMARK 465 ALA A 397
REMARK 465 TYR A 398
REMARK 465 ARG A 399
REMARK 465 GLN A 400
REMARK 465 GLY A 401
REMARK 465 PRO A 402
REMARK 465 PRO A 403
REMARK 465 ALA A 404
REMARK 465 SER A 405
REMARK 465 PRO A 406
REMARK 465 THR A 407
REMARK 465 ALA A 408
REMARK 465 SER A 409
REMARK 465 PRO A 410
REMARK 465 GLU A 411
REMARK 465 PRO A 412
REMARK 465 PRO A 413
REMARK 465 PRO A 414
REMARK 465 PRO A 415
REMARK 465 GLU A 416
REMARK 465 GLU A 417
REMARK 465 ASN A 418
REMARK 465 LEU A 419
REMARK 465 TYR A 420
REMARK 465 PHE A 421
REMARK 465 GLN A 422
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 CD2 HIS A 263 ZN ZN A 504 1.52
REMARK 500 CG HIS A 263 ZN ZN A 504 1.53
REMARK 500 ND2 ASN A 272 O5 NAG A 502 2.10
REMARK 500 O GLY L 101 O HOH L 407 2.11
REMARK 500 OE1 GLN A 126 NH1 ARG A 135 2.11
REMARK 500 O LEU A 304 NH1 ARG A 362 2.17
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 OD2 ASP A 262 OE2 GLU A 288 8554 2.02
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 ASP L 152 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 GLU A 261 OE1 - CD - OE2 ANGL. DEV. = -7.4 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 GLN L 16 -172.82 -66.43
REMARK 500 ASP L 50 -51.18 79.52
REMARK 500 SER L 66 124.71 170.43
REMARK 500 ASP L 81 6.41 -65.49
REMARK 500 LEU L 107 60.19 -63.00
REMARK 500 ASN L 129 46.36 33.59
REMARK 500 ASP L 152 -96.60 25.07
REMARK 500 PRO L 165 162.38 -48.88
REMARK 500 GLU L 199 58.60 29.45
REMARK 500 CYS H 22 87.66 -167.50
REMARK 500 SER H 56 -96.21 -71.17
REMARK 500 ASN H 77 40.14 34.96
REMARK 500 ARG H 104 -92.75 -108.11
REMARK 500 SER H 105 -117.25 -94.93
REMARK 500 THR H 204 -48.41 -154.56
REMARK 500 PRO H 215 -8.36 -58.28
REMARK 500 SER H 216 11.54 -141.94
REMARK 500 ASN H 217 73.79 50.04
REMARK 500 ASP A 41 55.82 -166.97
REMARK 500 LEU A 70 -24.16 85.83
REMARK 500 ARG A 80 155.93 -46.50
REMARK 500 TYR A 120 -84.23 -105.11
REMARK 500 ASN A 130 1.13 -63.69
REMARK 500 GLU A 137 -80.83 -133.94
REMARK 500 ALA A 142 75.16 -115.20
REMARK 500 SER A 181 -112.58 56.02
REMARK 500 ALA A 224 -94.91 -87.07
REMARK 500 LEU A 239 -12.30 -165.48
REMARK 500 ARG A 244 95.70 -160.22
REMARK 500 HIS A 286 54.17 39.48
REMARK 500 PHE A 287 73.95 -111.56
REMARK 500 GLU A 289 -46.69 -17.07
REMARK 500 ALA A 302 114.69 -35.37
REMARK 500 LEU A 304 76.28 45.81
REMARK 500 PRO A 332 30.62 -98.27
REMARK 500 ASP A 346 1.10 117.77
REMARK 500 THR A 347 -50.59 -134.60
REMARK 500 ARG A 362 -0.99 -154.00
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 ZN L 304 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 139 OD1
REMARK 620 2 ASP L 139 OD2 63.7
REMARK 620 3 HIS H 177 NE2 115.6 129.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 161 OE1
REMARK 620 2 GLU L 161 OE2 65.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 204 OE1
REMARK 620 2 GLU L 204 OE2 65.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 511 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 44 OD1
REMARK 620 2 ASP A 44 OD2 65.7
REMARK 620 3 GLU A 261 OE1 160.5 133.4
REMARK 620 4 GLU A 261 OE2 157.6 136.4 3.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 514 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 73 OD1
REMARK 620 2 ASP A 73 OD2 66.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 508 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 168 NE2
REMARK 620 2 ASP L 152 OD1 28.9
REMARK 620 3 ASP L 152 OD2 28.2 1.1
REMARK 620 4 HIS L 189 ND1 28.0 1.4 1.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 262 OD1
REMARK 620 2 ASP A 262 OD2 62.5
REMARK 620 3 GLU A 288 OE1 25.8 36.7
REMARK 620 4 GLU A 288 OE2 23.4 39.3 2.7
REMARK 620 5 GLU A 289 OE1 27.0 36.6 5.1 5.1
REMARK 620 6 GLU A 289 OE2 25.4 38.4 5.6 4.6 1.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 263 ND1
REMARK 620 2 HIS A 263 NE2 61.3
REMARK 620 3 HIS A 286 NE2 42.0 75.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 512 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 354 OE1
REMARK 620 2 GLU A 354 OE2 64.7
REMARK 620 3 HIS A 329 O 55.3 80.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 377 NE2
REMARK 620 2 HOH A 618 O 83.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound
REMARK 800 to ASN A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 503 bound
REMARK 800 to ASN A 384
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XX1 RELATED DB: PDB
DBREF 4XWG L 1 213 PDB 4XWG 4XWG 1 213
DBREF 4XWG H 1 238 PDB 4XWG 4XWG 1 238
DBREF 4XWG A 1 416 UNP P04180 LCAT_HUMAN 25 440
SEQADV 4XWG TYR A 31 UNP P04180 CYS 55 ENGINEERED MUTATION
SEQADV 4XWG GLU A 417 UNP P04180 EXPRESSION TAG
SEQADV 4XWG ASN A 418 UNP P04180 EXPRESSION TAG
SEQADV 4XWG LEU A 419 UNP P04180 EXPRESSION TAG
SEQADV 4XWG TYR A 420 UNP P04180 EXPRESSION TAG
SEQADV 4XWG PHE A 421 UNP P04180 EXPRESSION TAG
SEQADV 4XWG GLN A 422 UNP P04180 EXPRESSION TAG
SEQRES 1 L 213 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER
SEQRES 2 L 213 PRO GLY GLN THR ALA SER ILE THR CYS SER GLY ASP LYS
SEQRES 3 L 213 LEU GLY ASN LYS PHE THR SER TRP TYR GLN ARG LYS PRO
SEQRES 4 L 213 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP THR LYS
SEQRES 5 L 213 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER THR
SEQRES 6 L 213 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN
SEQRES 7 L 213 ALA MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP
SEQRES 8 L 213 SER SER THR ALA TRP VAL PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 213 GLU VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR
SEQRES 10 L 213 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS
SEQRES 11 L 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY
SEQRES 12 L 213 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL
SEQRES 13 L 213 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER
SEQRES 14 L 213 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR
SEQRES 15 L 213 PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN
SEQRES 16 L 213 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA
SEQRES 17 L 213 PRO THR GLU CYS SER
SEQRES 1 H 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 H 238 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 238 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 H 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP
SEQRES 5 H 238 TYR ASP GLY SER ASN LYS PHE TYR GLU ASP SER VAL LYS
SEQRES 6 H 238 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 H 238 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 238 ALA VAL TYR TYR CYS ALA ARG GLU GLY ALA ALA VAL ARG
SEQRES 9 H 238 SER PHE TYR TYR SER TYR TYR GLY MET ASP VAL TRP GLY
SEQRES 10 H 238 GLN GLY THR THR VAL THR VAL SER SER ALA SER THR LYS
SEQRES 11 H 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 12 H 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 13 H 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 14 H 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 15 H 238 LEU GLN SER SER GLY LEU TYR SER HIS SER SER VAL VAL
SEQRES 16 H 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 17 H 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 18 H 238 LYS LYS VAL GLU PRO LYS SER CYS ALA ALA ALA GLU ASN
SEQRES 19 H 238 LEU TYR PHE GLN
SEQRES 1 A 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 A 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 A 422 LEU VAL PRO GLY TYR LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 A 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 A 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 A 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 A 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 A 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 A 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 A 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 A 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 A 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 A 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 A 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 A 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 A 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 A 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 A 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 A 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 A 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 A 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 A 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 A 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 A 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 A 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 A 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 A 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 A 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 A 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 A 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 A 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 A 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 A 422 GLU ASN LEU TYR PHE GLN
HET ZN L 301 1
HET ZN L 302 1
HET ZN L 303 1
HET ZN L 304 1
HET NAG A 501 14
HET NAG A 502 14
HET NAG A 503 14
HET ZN A 504 1
HET ZN A 505 1
HET ZN A 506 1
HET ZN A 507 1
HET ZN A 508 1
HET ZN A 509 1
HET ZN A 510 1
HET ZN A 511 1
HET ZN A 512 1
HET ZN A 513 1
HET ZN A 514 1
HET ZN A 515 1
HETNAM ZN ZINC ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 4 ZN 16(ZN 2+)
FORMUL 8 NAG 3(C8 H15 N O6)
FORMUL 23 HOH *104(H2 O)
HELIX 1 AA1 SER L 122 GLN L 127 1 6
HELIX 2 AA2 THR L 182 SER L 188 1 7
HELIX 3 AA3 THR H 28 TYR H 32 5 5
HELIX 4 AA4 ASP H 62 LYS H 65 5 4
HELIX 5 AA5 ASN H 74 LYS H 76 5 3
HELIX 6 AA6 ARG H 87 THR H 91 5 5
HELIX 7 AA7 SER H 169 ALA H 171 5 3
HELIX 8 AA8 SER H 200 LEU H 202 5 3
HELIX 9 AA9 LYS H 214 ASN H 217 5 4
HELIX 10 AB1 ASP A 63 PHE A 67 5 5
HELIX 11 AB2 LEU A 70 ARG A 80 1 11
HELIX 12 AB3 THR A 106 TYR A 111 1 6
HELIX 13 AB4 LEU A 121 ASN A 130 1 10
HELIX 14 AB5 GLU A 149 GLN A 152 5 4
HELIX 15 AB6 GLN A 153 GLY A 172 1 20
HELIX 16 AB7 SER A 181 ARG A 193 1 13
HELIX 17 AB8 PRO A 195 PHE A 202 1 8
HELIX 18 AB9 ILE A 217 SER A 225 1 9
HELIX 19 AC1 SER A 249 PHE A 253 5 5
HELIX 20 AC2 ASP A 277 LEU A 285 1 9
HELIX 21 AC3 PHE A 287 ARG A 298 1 12
HELIX 22 AC4 ALA A 349 GLU A 354 1 6
HELIX 23 AC5 LEU A 355 GLN A 363 5 9
HELIX 24 AC6 ASN A 379 PHE A 382 5 4
HELIX 25 AC7 SER A 383 GLY A 396 1 14
SHEET 1 AA1 5 SER L 9 VAL L 12 0
SHEET 2 AA1 5 THR L 102 VAL L 106 1 O GLU L 105 N VAL L 10
SHEET 3 AA1 5 ALA L 83 ASP L 91 -1 N ALA L 83 O LEU L 104
SHEET 4 AA1 5 PHE L 31 ARG L 37 -1 N SER L 33 O GLN L 88
SHEET 5 AA1 5 VAL L 44 ILE L 47 -1 O ILE L 47 N TRP L 34
SHEET 1 AA2 4 SER L 9 VAL L 12 0
SHEET 2 AA2 4 THR L 102 VAL L 106 1 O GLU L 105 N VAL L 10
SHEET 3 AA2 4 ALA L 83 ASP L 91 -1 N ALA L 83 O LEU L 104
SHEET 4 AA2 4 THR L 94 PHE L 98 -1 O VAL L 97 N ALA L 89
SHEET 1 AA3 3 ALA L 18 SER L 23 0
SHEET 2 AA3 3 THR L 69 ILE L 74 -1 O ALA L 70 N CYS L 22
SHEET 3 AA3 3 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73
SHEET 1 AA4 4 SER L 115 PHE L 119 0
SHEET 2 AA4 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AA4 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 140
SHEET 4 AA4 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178
SHEET 1 AA5 4 SER L 115 PHE L 119 0
SHEET 2 AA5 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AA5 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 140
SHEET 4 AA5 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174
SHEET 1 AA6 4 SER L 154 VAL L 156 0
SHEET 2 AA6 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154
SHEET 3 AA6 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148
SHEET 4 AA6 4 SER L 201 VAL L 207 -1 O VAL L 207 N TYR L 192
SHEET 1 AA7 4 GLN H 3 SER H 7 0
SHEET 2 AA7 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3
SHEET 3 AA7 4 THR H 78 MET H 83 -1 O LEU H 81 N LEU H 20
SHEET 4 AA7 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80
SHEET 1 AA8 6 GLY H 10 VAL H 12 0
SHEET 2 AA8 6 THR H 120 VAL H 124 1 O THR H 123 N GLY H 10
SHEET 3 AA8 6 ALA H 92 GLU H 99 -1 N TYR H 94 O THR H 120
SHEET 4 AA8 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95
SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AA8 6 LYS H 58 TYR H 60 -1 O PHE H 59 N VAL H 50
SHEET 1 AA9 4 GLY H 10 VAL H 12 0
SHEET 2 AA9 4 THR H 120 VAL H 124 1 O THR H 123 N GLY H 10
SHEET 3 AA9 4 ALA H 92 GLU H 99 -1 N TYR H 94 O THR H 120
SHEET 4 AA9 4 MET H 113 TRP H 116 -1 O VAL H 115 N ARG H 98
SHEET 1 AB1 4 SER H 133 LEU H 137 0
SHEET 2 AB1 4 THR H 148 TYR H 158 -1 O GLY H 152 N LEU H 137
SHEET 3 AB1 4 TYR H 189 PRO H 198 -1 O TYR H 189 N TYR H 158
SHEET 4 AB1 4 VAL H 176 THR H 178 -1 N HIS H 177 O VAL H 194
SHEET 1 AB2 4 SER H 133 LEU H 137 0
SHEET 2 AB2 4 THR H 148 TYR H 158 -1 O GLY H 152 N LEU H 137
SHEET 3 AB2 4 TYR H 189 PRO H 198 -1 O TYR H 189 N TYR H 158
SHEET 4 AB2 4 VAL H 182 LEU H 183 -1 N VAL H 182 O SER H 190
SHEET 1 AB3 3 THR H 164 TRP H 167 0
SHEET 2 AB3 3 ILE H 208 ASN H 212 -1 O ASN H 210 N SER H 166
SHEET 3 AB3 3 LYS H 219 LYS H 223 -1 O LYS H 222 N CYS H 209
SHEET 1 AB4 6 VAL A 139 ALA A 141 0
SHEET 2 AB4 6 VAL A 25 VAL A 28 1 N LEU A 27 O ARG A 140
SHEET 3 AB4 6 VAL A 175 HIS A 180 1 O PHE A 176 N ILE A 26
SHEET 4 AB4 6 ILE A 203 LEU A 209 1 O ILE A 207 N LEU A 177
SHEET 5 AB4 6 VAL A 311 VAL A 317 1 O TYR A 312 N PHE A 206
SHEET 6 AB4 6 VAL A 367 HIS A 373 1 O LEU A 370 N CYS A 313
SHEET 1 AB5 3 PHE A 58 TRP A 61 0
SHEET 2 AB5 3 LEU A 36 LEU A 40 -1 N ALA A 38 O PHE A 58
SHEET 3 AB5 3 VAL A 96 ARG A 99 -1 O GLN A 97 N LYS A 39
SHEET 1 AB6 2 VAL A 81 TYR A 83 0
SHEET 2 AB6 2 VAL A 90 ASN A 92 -1 O SER A 91 N VAL A 82
SHEET 1 AB7 4 ASN A 272 TYR A 273 0
SHEET 2 AB7 4 ILE A 266 SER A 267 -1 N ILE A 266 O TYR A 273
SHEET 3 AB7 4 LEU A 319 ILE A 326 1 O TYR A 325 N SER A 267
SHEET 4 AB7 4 GLY A 338 GLY A 344 -1 O GLU A 342 N THR A 321
SSBOND 1 CYS L 22 CYS L 87 1555 1555 2.02
SSBOND 2 CYS L 135 CYS L 194 1555 1555 2.09
SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.07
SSBOND 4 CYS H 153 CYS H 209 1555 1555 2.08
SSBOND 5 CYS A 50 CYS A 74 1555 1555 2.07
SSBOND 6 CYS A 313 CYS A 356 1555 1555 2.09
LINK OD1 ASP L 139 ZN ZN L 304 1555 1555 2.05
LINK OD2 ASP L 139 ZN ZN L 304 1555 1555 2.02
LINK OE1 GLU L 161 ZN ZN L 301 1555 1555 2.02
LINK OE2 GLU L 161 ZN ZN L 301 1555 1555 2.01
LINK ND1 HIS L 198 ZN ZN L 302 1555 1555 2.10
LINK OE1 GLU L 204 ZN ZN L 303 1555 1555 2.02
LINK OE2 GLU L 204 ZN ZN L 303 1555 1555 2.01
LINK NE2 HIS H 177 ZN ZN L 304 1555 1555 2.04
LINK OD1 ASP A 44 ZN ZN A 511 1555 1555 2.00
LINK OD2 ASP A 44 ZN ZN A 511 1555 1555 2.01
LINK OD1 ASP A 73 ZN ZN A 514 1555 1555 2.01
LINK OD2 ASP A 73 ZN ZN A 514 1555 1555 2.00
LINK ND2 ASN A 84 C1 NAG A 501 1555 1555 1.45
LINK NE2 HIS A 122 ZN ZN A 507 1555 1555 2.05
LINK NE2 HIS A 168 ZN ZN A 508 1555 1555 2.04
LINK OD1 ASP A 262 ZN ZN A 506 1555 1555 2.04
LINK OD2 ASP A 262 ZN ZN A 506 1555 1555 2.05
LINK ND1 HIS A 263 ZN ZN A 504 1555 1555 2.11
LINK NE2 HIS A 263 ZN ZN A 504 1555 1555 2.11
LINK ND2 ASN A 272 C1 NAG A 502 1555 1555 1.43
LINK NE2 HIS A 329 ZN ZN A 515 1555 1555 2.07
LINK OE1 GLU A 354 ZN ZN A 512 1555 1555 2.04
LINK OE2 GLU A 354 ZN ZN A 512 1555 1555 2.02
LINK ND1 HIS A 368 ZN ZN A 513 1555 1555 2.06
LINK NE2 HIS A 373 ZN ZN A 510 1555 1555 2.08
LINK NE2 HIS A 377 ZN ZN A 505 1555 1555 2.06
LINK ND2 ASN A 384 C1 NAG A 503 1555 1555 1.47
LINK NE2 HIS A 389 ZN ZN A 509 1555 1555 2.04
LINK ZN ZN A 505 O HOH A 618 1555 1555 2.11
LINK OD1 ASP L 152 ZN ZN A 508 1555 7445 2.01
LINK OD2 ASP L 152 ZN ZN A 508 1555 7445 1.97
LINK ND1 HIS L 189 ZN ZN A 508 1555 7445 2.03
LINK OE1 GLU A 261 ZN ZN A 511 1555 8554 2.03
LINK OE2 GLU A 261 ZN ZN A 511 1555 8554 2.04
LINK NE2 HIS A 286 ZN ZN A 504 1555 6455 1.98
LINK OE1 GLU A 288 ZN ZN A 506 1555 6455 2.03
LINK OE2 GLU A 288 ZN ZN A 506 1555 6455 2.01
LINK OE1 GLU A 289 ZN ZN A 506 1555 6455 2.05
LINK OE2 GLU A 289 ZN ZN A 506 1555 6455 2.00
LINK O HIS A 329 ZN ZN A 512 1555 6455 2.06
CISPEP 1 TYR L 141 PRO L 142 0 1.18
CISPEP 2 PHE H 159 PRO H 160 0 -3.60
CISPEP 3 GLU H 161 PRO H 162 0 -1.25
CISPEP 4 TRP A 61 LEU A 62 0 6.98
CISPEP 5 PHE A 331 PRO A 332 0 -1.73
SITE 1 AC1 1 GLU L 161
SITE 1 AC2 2 ALA L 112 HIS L 198
SITE 1 AC3 1 GLU L 204
SITE 1 AC4 2 HIS H 177 ASP L 139
SITE 1 AC5 2 HIS A 263 HIS A 286
SITE 1 AC6 2 HIS A 377 HOH A 618
SITE 1 AC7 3 ASP A 262 GLU A 288 GLU A 289
SITE 1 AC8 1 HIS A 122
SITE 1 AC9 3 HIS A 168 ASP L 152 HIS L 189
SITE 1 AD1 1 HIS A 389
SITE 1 AD2 2 HIS A 329 HIS A 373
SITE 1 AD3 2 ASP A 44 GLU A 261
SITE 1 AD4 2 HIS A 329 GLU A 354
SITE 1 AD5 1 HIS A 368
SITE 1 AD6 1 ASP A 73
SITE 1 AD7 1 HIS A 329
SITE 1 AD8 3 ASN A 84 SER A 86 SER A 87
SITE 1 AD9 1 ASN A 272
SITE 1 AE1 2 ASN A 384 GLU A 388
CRYST1 168.590 168.590 93.570 90.00 90.00 120.00 H 3 9
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 0.005932 0.003425 0.000000 0.00000
SCALE2 0.000000 0.006849 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010687 0.00000
TER 1578 THR L 210
TER 3259 SER H 228
TER 6236 GLY A 396
MASTER 579 0 19 25 64 0 19 6 6395 3 99 69
END |