HEADER PROTEIN TRANSPORT 09-NOV-06 2NUP
TITLE CRYSTAL STRUCTURE OF THE HUMAN SEC23A/24A HETERODIMER, COMPLEXED WITH
TITLE 2 THE SNARE PROTEIN SEC22B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC23A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SEC23-RELATED PROTEIN A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC24A;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: SEC24A FRAGMENT LACKING N-TERMINAL RESIDUES 1-340;
COMPND 10 SYNONYM: SEC24-RELATED PROTEIN A;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: VESICLE-TRAFFICKING PROTEIN SEC22B;
COMPND 14 CHAIN: C;
COMPND 15 FRAGMENT: SEC22B CYTOSOLIC DOMAIN, RESIDUES 1-195;
COMPND 16 SYNONYM: SEC22 VESICLE-TRAFFICKING PROTEIN HOMOLOG B, SEC22 VESICLE-
COMPND 17 TRAFFICKING PROTEIN-LIKE 1, ERS24, ERS-24;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SEC23A;
SOURCE 6 EXPRESSION_SYSTEM: HI5 INSECT CELLS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: SEC24A;
SOURCE 13 EXPRESSION_SYSTEM: HI5 INSECT CELLS;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: SEC22B, SEC22L1;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS HUMAN COPII SEC23-24 COMPLEXED WITH SEC22, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.MANCIAS,J.GOLDBERG
REVDAT 4 30-AUG-23 2NUP 1 REMARK SEQADV LINK
REVDAT 3 18-OCT-17 2NUP 1 REMARK
REVDAT 2 24-FEB-09 2NUP 1 VERSN
REVDAT 1 22-MAY-07 2NUP 0
JRNL AUTH J.D.MANCIAS,J.GOLDBERG
JRNL TITL THE TRANSPORT SIGNAL ON SEC22 FOR PACKAGING INTO
JRNL TITL 2 COPII-COATED VESICLES IS A CONFORMATIONAL EPITOPE
JRNL REF MOL.CELL V. 26 403 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17499046
JRNL DOI 10.1016/J.MOLCEL.2007.03.017
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 42329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2114
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 42
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 888
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE : 0.4770
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 51
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12419
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : 2.83600
REMARK 3 B33 (A**2) : -2.63600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 9.18300
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.428
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.533 ; 3.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.377 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.651 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.416 ; 4.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 31.70
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : ZINC.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : ZINC.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NUP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040323.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 WITH FIXED EXIT GEOMETRY
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.010
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 1M2V AND 1IFQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (W/V) PEG 4000, 0.5M SODIUM
REMARK 280 ACETATE AND 50 MM TRIS BUFFER, PH 7.9, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298.0K
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 74.10000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 74.10000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.70000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLY A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 LEU A 206
REMARK 465 SER A 207
REMARK 465 LYS A 208
REMARK 465 VAL A 209
REMARK 465 PRO A 210
REMARK 465 VAL A 211
REMARK 465 THR A 212
REMARK 465 GLN A 213
REMARK 465 ALA A 214
REMARK 465 THR A 215
REMARK 465 ARG A 216
REMARK 465 GLY A 217
REMARK 465 PRO A 218
REMARK 465 GLN A 219
REMARK 465 VAL A 220
REMARK 465 GLN A 221
REMARK 465 GLN A 222
REMARK 465 ASN A 465
REMARK 465 GLN A 466
REMARK 465 HIS A 467
REMARK 465 ASN A 468
REMARK 465 ALA A 469
REMARK 465 PRO A 470
REMARK 465 ILE A 471
REMARK 465 PRO A 472
REMARK 465 GLN A 473
REMARK 465 GLU A 538
REMARK 465 GLY A 539
REMARK 465 PRO A 540
REMARK 465 TRP A 667
REMARK 465 ARG A 668
REMARK 465 LYS A 669
REMARK 465 SER A 670
REMARK 465 GLY A 671
REMARK 465 TYR A 672
REMARK 465 GLN A 673
REMARK 465 ASP A 674
REMARK 465 MET A 675
REMARK 465 PRO A 676
REMARK 465 GLU A 677
REMARK 465 TYR A 678
REMARK 465 PRO A 724
REMARK 465 SER A 725
REMARK 465 GLN A 726
REMARK 465 THR A 727
REMARK 465 HIS A 728
REMARK 465 ASN A 729
REMARK 465 ASN A 730
REMARK 465 MET A 731
REMARK 465 TYR A 732
REMARK 465 ALA A 733
REMARK 465 TRP A 734
REMARK 465 GLY A 735
REMARK 465 GLN A 736
REMARK 465 GLU A 737
REMARK 465 SER A 738
REMARK 465 GLY A 739
REMARK 465 ALA A 740
REMARK 465 PRO A 741
REMARK 465 ILE A 742
REMARK 465 LEU A 743
REMARK 465 THR A 744
REMARK 465 ASP A 745
REMARK 465 ALA A 765
REMARK 465 LEU B 341
REMARK 465 SER B 342
REMARK 465 LEU B 343
REMARK 465 GLN B 344
REMARK 465 PRO B 345
REMARK 465 TYR B 467
REMARK 465 ASN B 468
REMARK 465 PRO B 469
REMARK 465 LEU B 470
REMARK 465 THR B 471
REMARK 465 ARG B 472
REMARK 465 VAL B 473
REMARK 465 TYR B 474
REMARK 465 GLY B 475
REMARK 465 ASP B 663
REMARK 465 ILE B 664
REMARK 465 HIS B 665
REMARK 465 LEU B 883
REMARK 465 SER B 884
REMARK 465 ASN B 885
REMARK 465 GLN B 886
REMARK 465 GLN B 887
REMARK 465 SER C 0
REMARK 465 GLU C 24
REMARK 465 GLN C 25
REMARK 465 SER C 26
REMARK 465 GLY C 27
REMARK 465 ARG C 28
REMARK 465 ARG C 133
REMARK 465 ASN C 134
REMARK 465 LEU C 135
REMARK 465 GLY C 136
REMARK 465 SER C 137
REMARK 465 ILE C 138
REMARK 465 ASN C 139
REMARK 465 THR C 140
REMARK 465 GLU C 141
REMARK 465 LEU C 142
REMARK 465 GLN C 143
REMARK 465 ASP C 144
REMARK 465 VAL C 145
REMARK 465 GLN C 146
REMARK 465 ARG C 147
REMARK 465 GLN C 158
REMARK 465 ARG C 159
REMARK 465 GLY C 160
REMARK 465 GLU C 161
REMARK 465 ALA C 162
REMARK 465 LEU C 163
REMARK 465 SER C 164
REMARK 465 ALA C 165
REMARK 465 LEU C 166
REMARK 465 ASP C 167
REMARK 465 SER C 168
REMARK 465 LYS C 169
REMARK 465 ALA C 170
REMARK 465 ASN C 171
REMARK 465 ASN C 172
REMARK 465 LEU C 173
REMARK 465 SER C 174
REMARK 465 SER C 175
REMARK 465 LEU C 176
REMARK 465 SER C 177
REMARK 465 LYS C 178
REMARK 465 LYS C 179
REMARK 465 TYR C 180
REMARK 465 ARG C 181
REMARK 465 GLN C 182
REMARK 465 ASP C 183
REMARK 465 ALA C 184
REMARK 465 LYS C 185
REMARK 465 TYR C 186
REMARK 465 LEU C 187
REMARK 465 ASN C 188
REMARK 465 MET C 189
REMARK 465 ARG C 190
REMARK 465 SER C 191
REMARK 465 THR C 192
REMARK 465 TYR C 193
REMARK 465 ALA C 194
REMARK 465 LYS C 195
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 B1056 CG CD NE CZ NH1 NH2
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 GLU A 181 N ILE A 183 2.16
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 SER A 115 N - CA - C ANGL. DEV. = -21.8 DEGREES
REMARK 500 PRO B 413 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO B1020 C - N - CA ANGL. DEV. = -9.7 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 43 79.60 -113.74
REMARK 500 PRO A 44 -38.74 -39.33
REMARK 500 ARG A 48 -141.12 -160.54
REMARK 500 VAL A 59 110.30 92.89
REMARK 500 ARG A 63 88.02 -174.42
REMARK 500 THR A 64 -61.68 -7.56
REMARK 500 CYS A 66 -85.53 -59.11
REMARK 500 ASP A 77 77.50 -150.73
REMARK 500 TYR A 78 -14.50 -49.84
REMARK 500 TYR A 89 -12.63 64.97
REMARK 500 LEU A 104 33.30 -86.99
REMARK 500 ASN A 105 80.30 171.08
REMARK 500 GLU A 109 -6.55 -51.44
REMARK 500 PHE A 114 30.97 -98.85
REMARK 500 SER A 116 89.86 62.41
REMARK 500 ARG A 123 -52.70 -168.31
REMARK 500 CYS A 138 79.96 -100.82
REMARK 500 GLU A 181 173.39 52.40
REMARK 500 SER A 184 97.93 63.00
REMARK 500 SER A 196 -86.55 -65.38
REMARK 500 ALA A 197 -28.12 177.12
REMARK 500 SER A 226 138.92 176.51
REMARK 500 ARG A 249 159.85 -48.94
REMARK 500 SER A 263 44.55 -88.47
REMARK 500 ASN A 281 48.54 73.97
REMARK 500 ALA A 321 75.78 -158.34
REMARK 500 MET A 394 17.88 -54.59
REMARK 500 ASN A 427 73.87 21.09
REMARK 500 PRO A 431 -16.83 -48.99
REMARK 500 ARG A 476 102.51 86.24
REMARK 500 ALA A 506 -38.48 -39.61
REMARK 500 THR A 508 24.99 -152.24
REMARK 500 TYR A 560 175.83 174.64
REMARK 500 LYS A 562 153.39 -45.13
REMARK 500 ASP A 563 20.67 48.11
REMARK 500 SER A 575 -39.04 -38.29
REMARK 500 SER A 587 173.69 -56.62
REMARK 500 LEU A 636 150.39 -49.27
REMARK 500 ASP A 645 42.43 -102.25
REMARK 500 PHE A 653 -38.03 -36.63
REMARK 500 ILE A 664 -9.08 -59.67
REMARK 500 LEU A 696 37.49 -66.80
REMARK 500 HIS A 697 -48.17 -154.48
REMARK 500 PHE A 700 -80.36 -64.71
REMARK 500 PRO A 701 109.53 -58.63
REMARK 500 VAL A 722 -163.48 -76.10
REMARK 500 VAL A 747 -114.52 -93.36
REMARK 500 SER A 762 -150.73 -89.37
REMARK 500 ASN B 358 31.71 -152.78
REMARK 500 CYS B 431 133.43 -28.91
REMARK 500
REMARK 500 THIS ENTRY HAS 116 RAMACHANDRAN OUTLIERS.
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 A 800 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 61 SG
REMARK 620 2 CYS A 66 SG 121.1
REMARK 620 3 CYS A 85 SG 108.5 97.9
REMARK 620 4 CYS A 88 SG 105.0 107.0 118.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1100 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 431 SG
REMARK 620 2 CYS B 434 SG 102.8
REMARK 620 3 CYS B 452 SG 114.7 93.9
REMARK 620 4 CYS B 455 SG 113.1 109.8 119.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M2V RELATED DB: PDB
REMARK 900 RELATED ID: 1IFQ RELATED DB: PDB
REMARK 900 RELATED ID: 2NUT RELATED DB: PDB
DBREF 2NUP A 1 765 UNP Q15436 SC23A_HUMAN 1 765
DBREF 2NUP B 341 1093 UNP O95486 SC24A_HUMAN 326 1078
DBREF 2NUP C 1 195 UNP O75396 SC22B_HUMAN 1 195
SEQADV 2NUP GLY A -3 UNP Q15436 CLONING ARTIFACT
SEQADV 2NUP ALA A -2 UNP Q15436 CLONING ARTIFACT
SEQADV 2NUP MET A -1 UNP Q15436 CLONING ARTIFACT
SEQADV 2NUP GLY A 0 UNP Q15436 CLONING ARTIFACT
SEQADV 2NUP SER C 0 UNP O75396 CLONING ARTIFACT
SEQRES 1 A 769 GLY ALA MET GLY MET THR THR TYR LEU GLU PHE ILE GLN
SEQRES 2 A 769 GLN ASN GLU GLU ARG ASP GLY VAL ARG PHE SER TRP ASN
SEQRES 3 A 769 VAL TRP PRO SER SER ARG LEU GLU ALA THR ARG MET VAL
SEQRES 4 A 769 VAL PRO VAL ALA ALA LEU PHE THR PRO LEU LYS GLU ARG
SEQRES 5 A 769 PRO ASP LEU PRO PRO ILE GLN TYR GLU PRO VAL LEU CYS
SEQRES 6 A 769 SER ARG THR THR CYS ARG ALA VAL LEU ASN PRO LEU CYS
SEQRES 7 A 769 GLN VAL ASP TYR ARG ALA LYS LEU TRP ALA CYS ASN PHE
SEQRES 8 A 769 CYS TYR GLN ARG ASN GLN PHE PRO PRO SER TYR ALA GLY
SEQRES 9 A 769 ILE SER GLU LEU ASN GLN PRO ALA GLU LEU LEU PRO GLN
SEQRES 10 A 769 PHE SER SER ILE GLU TYR VAL VAL LEU ARG GLY PRO GLN
SEQRES 11 A 769 MET PRO LEU ILE PHE LEU TYR VAL VAL ASP THR CYS MET
SEQRES 12 A 769 GLU ASP GLU ASP LEU GLN ALA LEU LYS GLU SER MET GLN
SEQRES 13 A 769 MET SER LEU SER LEU LEU PRO PRO THR ALA LEU VAL GLY
SEQRES 14 A 769 LEU ILE THR PHE GLY ARG MET VAL GLN VAL HIS GLU LEU
SEQRES 15 A 769 GLY CYS GLU GLY ILE SER LYS SER TYR VAL PHE ARG GLY
SEQRES 16 A 769 THR LYS ASP LEU SER ALA LYS GLN LEU GLN GLU MET LEU
SEQRES 17 A 769 GLY LEU SER LYS VAL PRO VAL THR GLN ALA THR ARG GLY
SEQRES 18 A 769 PRO GLN VAL GLN GLN PRO PRO PRO SER ASN ARG PHE LEU
SEQRES 19 A 769 GLN PRO VAL GLN LYS ILE ASP MET ASN LEU THR ASP LEU
SEQRES 20 A 769 LEU GLY GLU LEU GLN ARG ASP PRO TRP PRO VAL PRO GLN
SEQRES 21 A 769 GLY LYS ARG PRO LEU ARG SER SER GLY VAL ALA LEU SER
SEQRES 22 A 769 ILE ALA VAL GLY LEU LEU GLU CYS THR PHE PRO ASN THR
SEQRES 23 A 769 GLY ALA ARG ILE MET MET PHE ILE GLY GLY PRO ALA THR
SEQRES 24 A 769 GLN GLY PRO GLY MET VAL VAL GLY ASP GLU LEU LYS THR
SEQRES 25 A 769 PRO ILE ARG SER TRP HIS ASP ILE ASP LYS ASP ASN ALA
SEQRES 26 A 769 LYS TYR VAL LYS LYS GLY THR LYS HIS PHE GLU ALA LEU
SEQRES 27 A 769 ALA ASN ARG ALA ALA THR THR GLY HIS VAL ILE ASP ILE
SEQRES 28 A 769 TYR ALA CYS ALA LEU ASP GLN THR GLY LEU LEU GLU MET
SEQRES 29 A 769 LYS CYS CYS PRO ASN LEU THR GLY GLY TYR MET VAL MET
SEQRES 30 A 769 GLY ASP SER PHE ASN THR SER LEU PHE LYS GLN THR PHE
SEQRES 31 A 769 GLN ARG VAL PHE THR LYS ASP MET HIS GLY GLN PHE LYS
SEQRES 32 A 769 MET GLY PHE GLY GLY THR LEU GLU ILE LYS THR SER ARG
SEQRES 33 A 769 GLU ILE LYS ILE SER GLY ALA ILE GLY PRO CYS VAL SER
SEQRES 34 A 769 LEU ASN SER LYS GLY PRO CYS VAL SER GLU ASN GLU ILE
SEQRES 35 A 769 GLY THR GLY GLY THR CYS GLN TRP LYS ILE CYS GLY LEU
SEQRES 36 A 769 SER PRO THR THR THR LEU ALA ILE TYR PHE GLU VAL VAL
SEQRES 37 A 769 ASN GLN HIS ASN ALA PRO ILE PRO GLN GLY GLY ARG GLY
SEQRES 38 A 769 ALA ILE GLN PHE VAL THR GLN TYR GLN HIS SER SER GLY
SEQRES 39 A 769 GLN ARG ARG ILE ARG VAL THR THR ILE ALA ARG ASN TRP
SEQRES 40 A 769 ALA ASP ALA GLN THR GLN ILE GLN ASN ILE ALA ALA SER
SEQRES 41 A 769 PHE ASP GLN GLU ALA ALA ALA ILE LEU MET ALA ARG LEU
SEQRES 42 A 769 ALA ILE TYR ARG ALA GLU THR GLU GLU GLY PRO ASP VAL
SEQRES 43 A 769 LEU ARG TRP LEU ASP ARG GLN LEU ILE ARG LEU CYS GLN
SEQRES 44 A 769 LYS PHE GLY GLU TYR HIS LYS ASP ASP PRO SER SER PHE
SEQRES 45 A 769 ARG PHE SER GLU THR PHE SER LEU TYR PRO GLN PHE MET
SEQRES 46 A 769 PHE HIS LEU ARG ARG SER SER PHE LEU GLN VAL PHE ASN
SEQRES 47 A 769 ASN SER PRO ASP GLU SER SER TYR TYR ARG HIS HIS PHE
SEQRES 48 A 769 MET ARG GLN ASP LEU THR GLN SER LEU ILE MET ILE GLN
SEQRES 49 A 769 PRO ILE LEU TYR ALA TYR SER PHE SER GLY PRO PRO GLU
SEQRES 50 A 769 PRO VAL LEU LEU ASP SER SER SER ILE LEU ALA ASP ARG
SEQRES 51 A 769 ILE LEU LEU MET ASP THR PHE PHE GLN ILE LEU ILE TYR
SEQRES 52 A 769 HIS GLY GLU THR ILE ALA GLN TRP ARG LYS SER GLY TYR
SEQRES 53 A 769 GLN ASP MET PRO GLU TYR GLU ASN PHE ARG HIS LEU LEU
SEQRES 54 A 769 GLN ALA PRO VAL ASP ASP ALA GLN GLU ILE LEU HIS SER
SEQRES 55 A 769 ARG PHE PRO MET PRO ARG TYR ILE ASP THR GLU HIS GLY
SEQRES 56 A 769 GLY SER GLN ALA ARG PHE LEU LEU SER LYS VAL ASN PRO
SEQRES 57 A 769 SER GLN THR HIS ASN ASN MET TYR ALA TRP GLY GLN GLU
SEQRES 58 A 769 SER GLY ALA PRO ILE LEU THR ASP ASP VAL SER LEU GLN
SEQRES 59 A 769 VAL PHE MET ASP HIS LEU LYS LYS LEU ALA VAL SER SER
SEQRES 60 A 769 ALA ALA
SEQRES 1 B 753 LEU SER LEU GLN PRO GLU GLY LEU ARG VAL VAL ASN LEU
SEQRES 2 B 753 LEU GLN GLU ARG ASN MET LEU PRO SER THR PRO LEU LYS
SEQRES 3 B 753 PRO PRO VAL PRO ASN LEU HIS GLU ASP ILE GLN LYS LEU
SEQRES 4 B 753 ASN CYS ASN PRO GLU LEU PHE ARG CYS THR LEU THR SER
SEQRES 5 B 753 ILE PRO GLN THR GLN ALA LEU LEU ASN LYS ALA LYS LEU
SEQRES 6 B 753 PRO LEU GLY LEU LEU LEU HIS PRO PHE LYS ASP LEU VAL
SEQRES 7 B 753 GLN LEU PRO VAL VAL THR SER SER THR ILE VAL ARG CYS
SEQRES 8 B 753 ARG SER CYS ARG THR TYR ILE ASN PRO PHE VAL SER PHE
SEQRES 9 B 753 LEU ASP GLN ARG ARG TRP LYS CYS ASN LEU CYS TYR ARG
SEQRES 10 B 753 VAL ASN ASP VAL PRO GLU GLU PHE LEU TYR ASN PRO LEU
SEQRES 11 B 753 THR ARG VAL TYR GLY GLU PRO HIS ARG ARG PRO GLU VAL
SEQRES 12 B 753 GLN ASN ALA THR ILE GLU PHE MET ALA PRO SER GLU TYR
SEQRES 13 B 753 MET LEU ARG PRO PRO GLN PRO PRO VAL TYR LEU PHE VAL
SEQRES 14 B 753 PHE ASP VAL SER HIS ASN ALA VAL GLU THR GLY TYR LEU
SEQRES 15 B 753 ASN SER VAL CYS GLN SER LEU LEU ASP ASN LEU ASP LEU
SEQRES 16 B 753 LEU PRO GLY ASN THR ARG THR LYS ILE GLY PHE ILE THR
SEQRES 17 B 753 PHE ASP SER THR ILE HIS PHE TYR GLY LEU GLN GLU SER
SEQRES 18 B 753 LEU SER GLN PRO GLN MET LEU ILE VAL SER ASP ILE GLU
SEQRES 19 B 753 ASP VAL PHE ILE PRO MET PRO GLU ASN LEU LEU VAL ASN
SEQRES 20 B 753 LEU ASN GLU SER LYS GLU LEU VAL GLN ASP LEU LEU LYS
SEQRES 21 B 753 THR LEU PRO GLN MET PHE THR LYS THR LEU GLU THR GLN
SEQRES 22 B 753 SER ALA LEU GLY PRO ALA LEU GLN ALA ALA PHE LYS LEU
SEQRES 23 B 753 MET SER PRO THR GLY GLY ARG MET SER VAL PHE GLN THR
SEQRES 24 B 753 GLN LEU PRO THR LEU GLY VAL GLY ALA LEU LYS PRO ARG
SEQRES 25 B 753 GLU GLU PRO ASN HIS ARG SER SER ALA LYS ASP ILE HIS
SEQRES 26 B 753 MET THR PRO SER THR ASP PHE TYR LYS LYS LEU ALA LEU
SEQRES 27 B 753 ASP CYS SER GLY GLN GLN VAL ALA VAL ASP LEU PHE LEU
SEQRES 28 B 753 LEU SER GLY GLN TYR SER ASP LEU ALA SER LEU GLY CYS
SEQRES 29 B 753 ILE SER ARG TYR SER ALA GLY SER VAL TYR TYR TYR PRO
SEQRES 30 B 753 SER TYR HIS HIS GLN HIS ASN PRO VAL GLN VAL GLN LYS
SEQRES 31 B 753 LEU GLN LYS GLU LEU GLN ARG TYR LEU THR ARG LYS ILE
SEQRES 32 B 753 GLY PHE GLU ALA VAL MET ARG ILE ARG CYS THR LYS GLY
SEQRES 33 B 753 LEU SER ILE HIS THR PHE HIS GLY ASN PHE PHE VAL ARG
SEQRES 34 B 753 SER THR ASP LEU LEU SER LEU PRO ASN VAL ASN PRO ASP
SEQRES 35 B 753 ALA GLY TYR ALA VAL GLN MET SER VAL GLU GLU SER LEU
SEQRES 36 B 753 THR ASP THR GLN LEU VAL SER PHE GLN SER ALA LEU LEU
SEQRES 37 B 753 TYR THR SER SER LYS GLY GLU ARG ARG ILE ARG VAL HIS
SEQRES 38 B 753 THR LEU CYS LEU PRO VAL VAL SER THR LEU ASN ASP VAL
SEQRES 39 B 753 PHE LEU GLY ALA ASP VAL GLN ALA ILE SER GLY LEU LEU
SEQRES 40 B 753 ALA ASN MET ALA VAL ASP ARG SER MET THR ALA SER LEU
SEQRES 41 B 753 SER ASP ALA ARG ASP ALA LEU VAL ASN ALA VAL ILE ASP
SEQRES 42 B 753 SER LEU SER ALA TYR ARG SER SER VAL LEU SER ASN GLN
SEQRES 43 B 753 GLN PRO GLY LEU MET VAL PRO PHE SER LEU ARG LEU PHE
SEQRES 44 B 753 PRO LEU PHE VAL LEU ALA LEU LEU LYS GLN LYS SER PHE
SEQRES 45 B 753 GLN THR GLY THR ASN ALA ARG LEU ASP GLU ARG ILE PHE
SEQRES 46 B 753 ALA MET CYS GLN VAL LYS ASN GLN PRO LEU VAL TYR LEU
SEQRES 47 B 753 MET LEU THR THR HIS PRO SER LEU TYR ARG VAL ASP ASN
SEQRES 48 B 753 LEU SER ASP GLU GLY ALA LEU ASN ILE SER ASP ARG THR
SEQRES 49 B 753 ILE PRO GLN PRO PRO ILE LEU GLN LEU SER VAL GLU LYS
SEQRES 50 B 753 LEU SER ARG ASP GLY ALA PHE LEU MET ASP ALA GLY SER
SEQRES 51 B 753 VAL LEU MET LEU TRP VAL GLY LYS ASN CYS THR GLN ASN
SEQRES 52 B 753 PHE LEU SER GLN VAL LEU GLY VAL GLN ASN TYR ALA SER
SEQRES 53 B 753 ILE PRO GLN PRO MET THR ASP LEU PRO GLU LEU ASP THR
SEQRES 54 B 753 PRO GLU SER ALA ARG ILE ILE ALA PHE ILE SER TRP LEU
SEQRES 55 B 753 ARG GLU GLN ARG PRO PHE PHE PRO ILE LEU TYR VAL ILE
SEQRES 56 B 753 ARG ASP GLU SER PRO MET LYS ALA ASN PHE LEU GLN ASN
SEQRES 57 B 753 MET ILE GLU ASP ARG THR GLU SER ALA LEU SER TYR TYR
SEQRES 58 B 753 GLU PHE LEU LEU HIS ILE GLN GLN GLN VAL ASN LYS
SEQRES 1 C 196 SER MET VAL LEU LEU THR MET ILE ALA ARG VAL ALA ASP
SEQRES 2 C 196 GLY LEU PRO LEU ALA ALA SER MET GLN GLU ASP GLU GLN
SEQRES 3 C 196 SER GLY ARG ASP LEU GLN GLN TYR GLN SER GLN ALA LYS
SEQRES 4 C 196 GLN LEU PHE ARG LYS LEU ASN GLU GLN SER PRO THR ARG
SEQRES 5 C 196 CYS THR LEU GLU ALA GLY ALA MET THR PHE HIS TYR ILE
SEQRES 6 C 196 ILE GLU GLN GLY VAL CYS TYR LEU VAL LEU CYS GLU ALA
SEQRES 7 C 196 ALA PHE PRO LYS LYS LEU ALA PHE ALA TYR LEU GLU ASP
SEQRES 8 C 196 LEU HIS SER GLU PHE ASP GLU GLN HIS GLY LYS LYS VAL
SEQRES 9 C 196 PRO THR VAL SER ARG PRO TYR SER PHE ILE GLU PHE ASP
SEQRES 10 C 196 THR PHE ILE GLN LYS THR LYS LYS LEU TYR ILE ASP SER
SEQRES 11 C 196 ARG ALA ARG ARG ASN LEU GLY SER ILE ASN THR GLU LEU
SEQRES 12 C 196 GLN ASP VAL GLN ARG ILE MET VAL ALA ASN ILE GLU GLU
SEQRES 13 C 196 VAL LEU GLN ARG GLY GLU ALA LEU SER ALA LEU ASP SER
SEQRES 14 C 196 LYS ALA ASN ASN LEU SER SER LEU SER LYS LYS TYR ARG
SEQRES 15 C 196 GLN ASP ALA LYS TYR LEU ASN MET ARG SER THR TYR ALA
SEQRES 16 C 196 LYS
HET ZN A 800 1
HET ZN B1100 1
HETNAM ZN ZINC ION
FORMUL 4 ZN 2(ZN 2+)
FORMUL 6 HOH *220(H2 O)
HELIX 1 1 THR A 3 GLY A 16 1 14
HELIX 2 2 SER A 27 THR A 32 1 6
HELIX 3 3 PRO A 95 ALA A 99 5 5
HELIX 4 4 PRO A 107 SER A 115 5 9
HELIX 5 5 GLU A 140 LEU A 158 1 19
HELIX 6 6 ALA A 197 GLY A 205 1 9
HELIX 7 7 VAL A 233 LEU A 247 1 15
HELIX 8 8 SER A 263 PHE A 279 1 17
HELIX 9 9 SER A 312 LYS A 318 1 7
HELIX 10 10 TYR A 323 GLY A 342 1 20
HELIX 11 11 GLY A 356 LYS A 361 1 6
HELIX 12 12 LYS A 361 THR A 367 1 7
HELIX 13 13 THR A 379 VAL A 389 1 11
HELIX 14 14 ASP A 505 GLN A 507 5 3
HELIX 15 15 THR A 508 SER A 516 1 9
HELIX 16 16 ASP A 518 GLU A 535 1 18
HELIX 17 17 ASP A 541 GLY A 558 1 18
HELIX 18 18 LEU A 576 SER A 587 1 12
HELIX 19 19 SER A 596 MET A 608 1 13
HELIX 20 20 ASP A 611 GLN A 620 1 10
HELIX 21 21 ASP A 638 ILE A 642 5 5
HELIX 22 22 GLU A 679 GLN A 686 1 8
HELIX 23 23 GLN A 686 ARG A 699 1 14
HELIX 24 24 GLY A 712 GLN A 714 5 3
HELIX 25 25 ALA A 715 VAL A 722 1 8
HELIX 26 26 SER A 748 VAL A 761 1 14
HELIX 27 27 LEU B 353 ARG B 357 1 5
HELIX 28 28 HIS B 373 LYS B 378 1 6
HELIX 29 29 THR B 396 LYS B 404 1 9
HELIX 30 30 GLU B 476 GLN B 484 5 9
HELIX 31 31 SER B 513 GLY B 520 1 8
HELIX 32 32 GLY B 520 LEU B 533 1 14
HELIX 33 33 ASP B 534 LEU B 536 5 3
HELIX 34 34 LEU B 588 LEU B 602 1 15
HELIX 35 35 PRO B 603 PHE B 606 5 4
HELIX 36 36 ALA B 615 SER B 628 1 14
HELIX 37 37 ASP B 671 GLN B 683 1 13
HELIX 38 38 ASP B 698 GLY B 703 1 6
HELIX 39 39 GLY B 703 TYR B 708 1 6
HELIX 40 40 ASN B 724 ARG B 741 1 18
HELIX 41 41 THR B 830 GLY B 837 1 8
HELIX 42 42 ASP B 839 ALA B 858 1 20
HELIX 43 43 SER B 859 SER B 880 1 22
HELIX 44 44 SER B 895 ARG B 897 5 3
HELIX 45 45 LEU B 898 GLN B 909 1 12
HELIX 46 46 ARG B 919 GLN B 933 1 15
HELIX 47 47 PRO B 934 HIS B 943 1 10
HELIX 48 48 SER B 974 LEU B 978 5 5
HELIX 49 49 THR B 1001 VAL B 1008 1 8
HELIX 50 50 ASN B 1013 ILE B 1017 5 5
HELIX 51 51 THR B 1029 GLU B 1044 1 16
HELIX 52 52 PHE B 1065 MET B 1069 5 5
HELIX 53 53 SER B 1079 ASN B 1092 1 14
HELIX 54 54 ASP C 29 LEU C 44 1 16
HELIX 55 55 PRO C 80 GLY C 100 1 21
HELIX 56 56 PHE C 112 GLU C 114 5 3
HELIX 57 57 PHE C 115 LYS C 124 1 10
HELIX 58 58 LEU C 125 ILE C 127 5 3
SHEET 1 A 5 VAL A 17 PHE A 19 0
SHEET 2 A 5 ALA A 39 PHE A 42 -1 O LEU A 41 N ARG A 18
SHEET 3 A 5 LEU A 457 VAL A 463 -1 O ILE A 459 N ALA A 40
SHEET 4 A 5 ILE A 414 ILE A 420 -1 N GLY A 418 O TYR A 460
SHEET 5 A 5 VAL A 433 GLY A 439 1 O ILE A 438 N SER A 417
SHEET 1 B 3 VAL A 23 TRP A 24 0
SHEET 2 B 3 ARG A 492 TRP A 503 1 O ASN A 502 N TRP A 24
SHEET 3 B 3 ILE A 117 VAL A 121 -1 N ILE A 117 O VAL A 496
SHEET 1 C 6 VAL A 23 TRP A 24 0
SHEET 2 C 6 ARG A 492 TRP A 503 1 O ASN A 502 N TRP A 24
SHEET 3 C 6 GLY A 477 GLN A 486 -1 N GLY A 477 O ARG A 501
SHEET 4 C 6 GLY A 401 THR A 410 -1 N PHE A 402 O GLN A 486
SHEET 5 C 6 GLN A 445 LEU A 451 -1 O ILE A 448 N GLY A 404
SHEET 6 C 6 VAL A 424 SER A 425 -1 N VAL A 424 O LYS A 447
SHEET 1 D 3 GLN A 75 ASP A 77 0
SHEET 2 D 3 LEU A 82 ALA A 84 -1 O ALA A 84 N GLN A 75
SHEET 3 D 3 ARG A 91 GLN A 93 -1 O ASN A 92 N TRP A 83
SHEET 1 E 8 GLN A 231 PRO A 232 0
SHEET 2 E 8 LEU A 163 PHE A 169 -1 N VAL A 164 O GLN A 231
SHEET 3 E 8 MET A 172 GLU A 177 -1 O GLN A 174 N THR A 168
SHEET 4 E 8 LYS A 185 ARG A 190 -1 O PHE A 189 N VAL A 173
SHEET 5 E 8 GLN B 566 VAL B 570 1 O ILE B 569 N VAL A 188
SHEET 6 E 8 ILE B 553 GLY B 557 -1 N GLY B 557 O GLN B 566
SHEET 7 E 8 LYS B 543 PHE B 549 -1 N THR B 548 O HIS B 554
SHEET 8 E 8 VAL B 586 ASN B 587 -1 O VAL B 586 N ILE B 544
SHEET 1 F14 MET A 371 GLY A 374 0
SHEET 2 F14 VAL A 344 CYS A 350 1 N ALA A 349 O VAL A 372
SHEET 3 F14 ALA A 284 ILE A 290 1 N MET A 288 O TYR A 348
SHEET 4 F14 ILE A 130 ASP A 136 1 N ILE A 130 O ARG A 285
SHEET 5 F14 LEU A 163 PHE A 169 1 O ILE A 167 N VAL A 135
SHEET 6 F14 MET A 172 GLU A 177 -1 O GLN A 174 N THR A 168
SHEET 7 F14 LYS A 185 ARG A 190 -1 O PHE A 189 N VAL A 173
SHEET 8 F14 GLN B 566 VAL B 570 1 O ILE B 569 N VAL A 188
SHEET 9 F14 ILE B 553 GLY B 557 -1 N GLY B 557 O GLN B 566
SHEET 10 F14 LYS B 543 PHE B 549 -1 N THR B 548 O HIS B 554
SHEET 11 F14 VAL B 505 ASP B 511 1 N TYR B 506 O GLY B 545
SHEET 12 F14 GLY B 632 GLN B 638 1 O PHE B 637 N VAL B 509
SHEET 13 F14 VAL B 685 LEU B 691 1 O ASP B 688 N VAL B 636
SHEET 14 F14 SER B 712 TYR B 715 1 O TYR B 714 N LEU B 689
SHEET 1 G 2 GLU A 559 HIS A 561 0
SHEET 2 G 2 ASP A 564 ARG A 569 -1 O ARG A 569 N GLU A 559
SHEET 1 H 5 GLU A 633 PRO A 634 0
SHEET 2 H 5 ILE A 622 TYR A 626 -1 N ALA A 625 O GLU A 633
SHEET 3 H 5 ILE A 647 THR A 652 -1 O ILE A 647 N TYR A 626
SHEET 4 H 5 GLN A 655 HIS A 660 -1 O LEU A 657 N MET A 650
SHEET 5 H 5 ARG A 704 GLU A 709 1 O ILE A 706 N ILE A 658
SHEET 1 I 2 VAL B 350 ASN B 352 0
SHEET 2 I 2 MET B 891 PRO B 893 -1 O VAL B 892 N VAL B 351
SHEET 1 J 4 PHE B 386 CYS B 388 0
SHEET 2 J 4 GLY B 408 LEU B 411 -1 O LEU B 410 N ARG B 387
SHEET 3 J 4 TYR B 785 VAL B 791 -1 O VAL B 787 N LEU B 409
SHEET 4 J 4 LEU B 757 HIS B 763 -1 N HIS B 760 O GLN B 788
SHEET 1 K 4 ILE B 393 PRO B 394 0
SHEET 2 K 4 ARG B 816 VAL B 828 1 O VAL B 828 N ILE B 393
SHEET 3 K 4 THR B 487 MET B 491 -1 N PHE B 490 O ILE B 818
SHEET 4 K 4 VAL B 422 VAL B 423 1 N VAL B 423 O GLU B 489
SHEET 1 L 6 ILE B 393 PRO B 394 0
SHEET 2 L 6 ARG B 816 VAL B 828 1 O VAL B 828 N ILE B 393
SHEET 3 L 6 LEU B 800 SER B 811 -1 N PHE B 803 O LEU B 823
SHEET 4 L 6 GLY B 744 CYS B 753 -1 N PHE B 745 O THR B 810
SHEET 5 L 6 LEU B 774 VAL B 779 -1 O LEU B 774 N MET B 749
SHEET 6 L 6 PHE B 767 VAL B 768 -1 N PHE B 767 O SER B 775
SHEET 1 M 3 SER B 443 PHE B 444 0
SHEET 2 M 3 ARG B 449 LYS B 451 -1 O LYS B 451 N SER B 443
SHEET 3 M 3 VAL B 458 ASP B 460 -1 O ASN B 459 N TRP B 450
SHEET 1 N 3 SER B 945 ARG B 948 0
SHEET 2 N 3 ALA B 983 ASP B 987 -1 O ASP B 987 N SER B 945
SHEET 3 N 3 LEU B 994 VAL B 996 -1 O TRP B 995 N PHE B 984
SHEET 1 O 6 LEU C 14 SER C 19 0
SHEET 2 O 6 THR C 5 ARG C 9 -1 N ILE C 7 O LEU C 16
SHEET 3 O 6 VAL C 69 VAL C 73 -1 O CYS C 70 N ALA C 8
SHEET 4 O 6 MET C 59 GLU C 66 -1 N ILE C 64 O TYR C 71
SHEET 5 O 6 ARG C 51 ALA C 56 -1 N LEU C 54 O PHE C 61
SHEET 6 O 6 VAL C 150 ASN C 152 1 O ALA C 151 N THR C 53
LINK SG CYS A 61 ZN ZN A 800 1555 1555 2.49
LINK SG CYS A 66 ZN ZN A 800 1555 1555 2.29
LINK SG CYS A 85 ZN ZN A 800 1555 1555 2.45
LINK SG CYS A 88 ZN ZN A 800 1555 1555 2.60
LINK SG CYS B 431 ZN ZN B1100 1555 1555 2.36
LINK SG CYS B 434 ZN ZN B1100 1555 1555 2.42
LINK SG CYS B 452 ZN ZN B1100 1555 1555 2.39
LINK SG CYS B 455 ZN ZN B1100 1555 1555 2.40
CISPEP 1 GLY A 297 PRO A 298 0 -0.52
SITE 1 AC1 4 CYS A 61 CYS A 66 CYS A 85 CYS A 88
SITE 1 AC2 4 CYS B 431 CYS B 434 CYS B 452 CYS B 455
CRYST1 148.200 97.400 129.620 90.00 90.23 90.00 C 1 2 1 4
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 0.006748 0.000000 0.000027 0.00000
SCALE2 0.000000 0.010267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007715 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
