HEADER IMMUNE SYSTEM,HYDROLASE INHIBITOR 18-DEC-06 2OAY
TITLE CRYSTAL STRUCTURE OF LATENT HUMAN C1-INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMA PROTEASE C1 INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SERPIN DOMAIN;
COMPND 5 SYNONYM: C1-INHIBITOR; C1 INH; C1INH; C1 ESTERASE INHIBITOR; C1-
COMPND 6 INHIBITING FACTOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SERPING1, C1IN, C1NH;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9K
KEYWDS LATENT SERPIN; RCL INSERTION, IMMUNE SYSTEM, HYDROLASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR V.HARMAT,L.BEINROHR,P.GAL,J.DOBO
REVDAT 7 30-AUG-23 2OAY 1 HETSYN
REVDAT 6 29-JUL-20 2OAY 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE
REVDAT 5 18-OCT-17 2OAY 1 REMARK
REVDAT 4 13-JUL-11 2OAY 1 VERSN
REVDAT 3 24-FEB-09 2OAY 1 VERSN
REVDAT 2 07-AUG-07 2OAY 1 JRNL
REVDAT 1 01-MAY-07 2OAY 0
JRNL AUTH L.BEINROHR,V.HARMAT,J.DOBO,Z.LORINCZ,P.GAL,P.ZAVODSZKY
JRNL TITL C1 INHIBITOR SERPIN DOMAIN STRUCTURE REVEALS THE LIKELY
JRNL TITL 2 MECHANISM OF HEPARIN POTENTIATION AND CONFORMATIONAL DISEASE
JRNL REF J.BIOL.CHEM. V. 282 21100 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17488724
JRNL DOI 10.1074/JBC.M700841200
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 20803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1125
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1546
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2845
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 32.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.29000
REMARK 3 B22 (A**2) : 0.29000
REMARK 3 B33 (A**2) : -0.43000
REMARK 3 B12 (A**2) : 0.14000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.239
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.197
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.154
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.574
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2952 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2693 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4015 ; 1.764 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6265 ; 0.804 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 370 ; 7.479 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 481 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3204 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 558 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 599 ; 0.216 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3056 ; 0.256 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1927 ; 0.100 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 148 ; 0.187 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.273 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 45 ; 0.390 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.186 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1852 ; 2.070 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3006 ; 3.238 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1100 ; 2.123 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1006 ; 3.367 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 101 A 476
REMARK 3 RESIDUE RANGE : A 500 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7946 71.6738 -0.6784
REMARK 3 T TENSOR
REMARK 3 T11: 0.1060 T22: 0.0380
REMARK 3 T33: 0.1121 T12: 0.0229
REMARK 3 T13: -0.0025 T23: 0.0519
REMARK 3 L TENSOR
REMARK 3 L11: 1.5314 L22: 2.5613
REMARK 3 L33: 2.8210 L12: 0.1233
REMARK 3 L13: 0.1272 L23: 1.5387
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0272 S13: 0.0470
REMARK 3 S21: -0.0132 S22: -0.0308 S23: -0.0146
REMARK 3 S31: -0.1414 S32: -0.2032 S33: 0.0528
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000040907.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8162
REMARK 200 MONOCHROMATOR : SI [111]
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21930
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 84.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.54
REMARK 200 R MERGE FOR SHELL (I) : 0.65200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: ENSEMBLE OF TRUNCATED SERPIN STRUCTURES. PDB
REMARK 200 CODES: 4CAA, 1QMB, 1E05, 1DVM, 1C8O, 1JTI, 1JJO, 1MTP, 1HLE, 1JRR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.85 M NAH2PO4, 0.85 M KH2PO4, 0.1 M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 63.12267
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 31.56133
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 47.34200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 15.78067
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.90333
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 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 TYR A 89
REMARK 465 VAL A 90
REMARK 465 HIS A 91
REMARK 465 HIS A 92
REMARK 465 HIS A 93
REMARK 465 HIS A 94
REMARK 465 HIS A 95
REMARK 465 HIS A 96
REMARK 465 THR A 97
REMARK 465 GLY A 98
REMARK 465 SER A 99
REMARK 465 PHE A 100
REMARK 465 GLY A 103
REMARK 465 PRO A 104
REMARK 465 MET A 138
REMARK 465 LYS A 139
REMARK 465 LYS A 140
REMARK 465 VAL A 141
REMARK 465 LYS A 294
REMARK 465 ASN A 295
REMARK 465 ARG A 477
REMARK 465 ALA A 478
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 THR A 106 CB OG1 CG2
REMARK 470 LEU A 107 CG CD1 CD2
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 LYS A 168 CE NZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 SER A 261 OG
REMARK 470 LYS A 276 NZ
REMARK 470 LYS A 278 CD CE NZ
REMARK 470 LYS A 285 CE NZ
REMARK 470 ARG A 287 CD NE CZ NH1 NH2
REMARK 470 SER A 296 CB OG
REMARK 470 LYS A 306 CE NZ
REMARK 470 LYS A 307 CD CE NZ
REMARK 470 GLN A 316 CD OE1 NE2
REMARK 470 LYS A 319 CE NZ
REMARK 470 LYS A 342 CG CD CE NZ
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 ASP A 413 CG OD1 OD2
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 THR A 193 O HOH A 18 2.12
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 VAL A 184 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 ASP A 212 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 234 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU A 456 CA - CB - CG ANGL. DEV. = 16.9 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 THR A 106 79.90 65.40
REMARK 500 PHE A 396 -82.89 -87.06
REMARK 500 LEU A 405 43.66 -108.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 180 PHE A 181 -147.98
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2OAY A 97 478 UNP P05155 IC1_HUMAN 119 500
SEQADV 2OAY TYR A 89 UNP P05155 EXPRESSION TAG
SEQADV 2OAY VAL A 90 UNP P05155 EXPRESSION TAG
SEQADV 2OAY HIS A 91 UNP P05155 EXPRESSION TAG
SEQADV 2OAY HIS A 92 UNP P05155 EXPRESSION TAG
SEQADV 2OAY HIS A 93 UNP P05155 EXPRESSION TAG
SEQADV 2OAY HIS A 94 UNP P05155 EXPRESSION TAG
SEQADV 2OAY HIS A 95 UNP P05155 EXPRESSION TAG
SEQADV 2OAY HIS A 96 UNP P05155 EXPRESSION TAG
SEQADV 2OAY MET A 458 UNP P05155 VAL 480 VARIANT
SEQRES 1 A 390 TYR VAL HIS HIS HIS HIS HIS HIS THR GLY SER PHE CYS
SEQRES 2 A 390 PRO GLY PRO VAL THR LEU CYS SER ASP LEU GLU SER HIS
SEQRES 3 A 390 SER THR GLU ALA VAL LEU GLY ASP ALA LEU VAL ASP PHE
SEQRES 4 A 390 SER LEU LYS LEU TYR HIS ALA PHE SER ALA MET LYS LYS
SEQRES 5 A 390 VAL GLU THR ASN MET ALA PHE SER PRO PHE SER ILE ALA
SEQRES 6 A 390 SER LEU LEU THR GLN VAL LEU LEU GLY ALA GLY GLU ASN
SEQRES 7 A 390 THR LYS THR ASN LEU GLU SER ILE LEU SER TYR PRO LYS
SEQRES 8 A 390 ASP PHE THR CYS VAL HIS GLN ALA LEU LYS GLY PHE THR
SEQRES 9 A 390 THR LYS GLY VAL THR SER VAL SER GLN ILE PHE HIS SER
SEQRES 10 A 390 PRO ASP LEU ALA ILE ARG ASP THR PHE VAL ASN ALA SER
SEQRES 11 A 390 ARG THR LEU TYR SER SER SER PRO ARG VAL LEU SER ASN
SEQRES 12 A 390 ASN SER ASP ALA ASN LEU GLU LEU ILE ASN THR TRP VAL
SEQRES 13 A 390 ALA LYS ASN THR ASN ASN LYS ILE SER ARG LEU LEU ASP
SEQRES 14 A 390 SER LEU PRO SER ASP THR ARG LEU VAL LEU LEU ASN ALA
SEQRES 15 A 390 ILE TYR LEU SER ALA LYS TRP LYS THR THR PHE ASP PRO
SEQRES 16 A 390 LYS LYS THR ARG MET GLU PRO PHE HIS PHE LYS ASN SER
SEQRES 17 A 390 VAL ILE LYS VAL PRO MET MET ASN SER LYS LYS TYR PRO
SEQRES 18 A 390 VAL ALA HIS PHE ILE ASP GLN THR LEU LYS ALA LYS VAL
SEQRES 19 A 390 GLY GLN LEU GLN LEU SER HIS ASN LEU SER LEU VAL ILE
SEQRES 20 A 390 LEU VAL PRO GLN ASN LEU LYS HIS ARG LEU GLU ASP MET
SEQRES 21 A 390 GLU GLN ALA LEU SER PRO SER VAL PHE LYS ALA ILE MET
SEQRES 22 A 390 GLU LYS LEU GLU MET SER LYS PHE GLN PRO THR LEU LEU
SEQRES 23 A 390 THR LEU PRO ARG ILE LYS VAL THR THR SER GLN ASP MET
SEQRES 24 A 390 LEU SER ILE MET GLU LYS LEU GLU PHE PHE ASP PHE SER
SEQRES 25 A 390 TYR ASP LEU ASN LEU CYS GLY LEU THR GLU ASP PRO ASP
SEQRES 26 A 390 LEU GLN VAL SER ALA MET GLN HIS GLN THR VAL LEU GLU
SEQRES 27 A 390 LEU THR GLU THR GLY VAL GLU ALA ALA ALA ALA SER ALA
SEQRES 28 A 390 ILE SER VAL ALA ARG THR LEU LEU VAL PHE GLU VAL GLN
SEQRES 29 A 390 GLN PRO PHE LEU PHE MET LEU TRP ASP GLN GLN HIS LYS
SEQRES 30 A 390 PHE PRO VAL PHE MET GLY ARG VAL TYR ASP PRO ARG ALA
MODRES 2OAY ASN A 216 ASN GLYCOSYLATION SITE
HET NAG A 500 14
HET GOL A5001 6
HET GOL A5002 6
HET GOL A5003 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
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
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 HOH *70(H2 O)
HELIX 1 1 GLU A 112 SER A 136 1 25
HELIX 2 2 SER A 148 GLY A 162 1 15
HELIX 3 3 GLY A 164 SER A 176 1 13
HELIX 4 4 CYS A 183 GLY A 190 1 8
HELIX 5 5 ARG A 211 SER A 223 1 13
HELIX 6 6 ASN A 232 ASN A 247 1 16
HELIX 7 7 ARG A 344 LEU A 352 1 9
HELIX 8 8 SER A 353 MET A 366 1 14
HELIX 9 9 MET A 387 GLU A 392 1 6
HELIX 10 10 LYS A 393 GLU A 395 5 3
HELIX 11 11 ASP A 398 LEU A 403 5 6
SHEET 1 A 7 MET A 145 PHE A 147 0
SHEET 2 A 7 PHE A 466 VAL A 473 -1 O MET A 470 N PHE A 147
SHEET 3 A 7 PHE A 455 ASP A 461 -1 N PHE A 455 O VAL A 473
SHEET 4 A 7 LEU A 331 PRO A 338 -1 N SER A 332 O TRP A 460
SHEET 5 A 7 ALA A 320 GLN A 326 -1 N LYS A 321 O VAL A 337
SHEET 6 A 7 ILE A 298 ASP A 315 -1 N PHE A 313 O VAL A 322
SHEET 7 A 7 ARG A 287 PHE A 291 -1 N GLU A 289 O VAL A 300
SHEET 1 B 7 MET A 145 PHE A 147 0
SHEET 2 B 7 PHE A 466 VAL A 473 -1 O MET A 470 N PHE A 147
SHEET 3 B 7 PHE A 455 ASP A 461 -1 N PHE A 455 O VAL A 473
SHEET 4 B 7 LEU A 331 PRO A 338 -1 N SER A 332 O TRP A 460
SHEET 5 B 7 ALA A 320 GLN A 326 -1 N LYS A 321 O VAL A 337
SHEET 6 B 7 ILE A 298 ASP A 315 -1 N PHE A 313 O VAL A 322
SHEET 7 B 7 PHE A 369 PRO A 377 -1 O LEU A 374 N SER A 305
SHEET 1 C 7 ARG A 227 VAL A 228 0
SHEET 2 C 7 VAL A 196 HIS A 204 1 N ILE A 202 O ARG A 227
SHEET 3 C 7 LEU A 265 LYS A 276 -1 O TYR A 272 N THR A 197
SHEET 4 C 7 GLY A 431 ILE A 440 -1 O ALA A 436 N ILE A 271
SHEET 5 C 7 MET A 419 LEU A 427 -1 N VAL A 424 O ALA A 435
SHEET 6 C 7 LYS A 380 ASP A 386 -1 N VAL A 381 O LEU A 425
SHEET 7 C 7 LEU A 446 VAL A 448 -1 O VAL A 448 N THR A 382
SSBOND 1 CYS A 101 CYS A 406 1555 1555 2.02
SSBOND 2 CYS A 108 CYS A 183 1555 1555 2.05
LINK ND2 ASN A 216 C1 NAG A 500 1555 1555 1.46
CRYST1 98.903 98.903 94.684 90.00 90.00 120.00 P 65 6
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 0.010111 0.005838 0.000000 0.00000
SCALE2 0.000000 0.011675 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010561 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
