HEADER SIGNALING PROTEIN 22-OCT-16 5H3D
TITLE HELICAL STRUCTURE OF MEMBRANE TUBULES DECORATED BY ACAP1 (BARPH
TITLE 2 DOAMIN) PROTEIN BY CRYO-ELECTRON MICROSCOPY AND MD SIMULATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-
COMPND 3 CONTAINING PROTEIN 1;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: CENTAURIN-BETA-1,CNT-B1;
COMPND 6 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: ACAP1, CENTB1, KIAA0050;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACAP1 BARPH DOMAIN, MEMBRANE REMODELING, MOLECULAR DYNAMICS
KEYWDS 2 SIMULATION, SIGNALING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.CHAN,X.Y.PANG,Y.ZHANG,F.SUN,J.FAN
REVDAT 4 20-MAR-24 5H3D 1 REMARK
REVDAT 3 12-FEB-20 5H3D 1 JRNL
REVDAT 2 06-NOV-19 5H3D 1 CRYST1
REVDAT 1 16-JAN-19 5H3D 0
JRNL AUTH C.CHAN,X.PANG,Y.ZHANG,T.NIU,S.YANG,D.ZHAO,J.LI,L.LU,V.W.HSU,
JRNL AUTH 2 J.ZHOU,F.SUN,J.FAN
JRNL TITL ACAP1 ASSEMBLES INTO AN UNUSUAL PROTEIN LATTICE FOR MEMBRANE
JRNL TITL 2 DEFORMATION THROUGH MULTIPLE STAGES.
JRNL REF PLOS COMPUT.BIOL. V. 15 07081 2019
JRNL REFN ESSN 1553-7358
JRNL PMID 31291238
JRNL DOI 10.1371/JOURNAL.PCBI.1007081
REMARK 2
REMARK 2 RESOLUTION. 14.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SERIALEM
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : CROSS CORRELATION
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 14.00
REMARK 3 NUMBER OF PARTICLES : 304
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5H3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001720.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : HELICAL
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : HELICAL ARRAY
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : HELICAL STRUCTURE OF ACAP1
REMARK 245 BARPH DOMAIN ON MEMBRANE TUBULES
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN ULTRASCAN 4000 (4K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2000.00
REMARK 245 ILLUMINATION MODE : OTHER
REMARK 245 NOMINAL MAGNIFICATION : 75000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C3).
REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS:
REMARK 300 ROTATION PER SUBUNIT (TWIST) = 42.69 DEGREES
REMARK 300 RISE PER SUBUNIT (HEIGHT) = 23.20 ANGSTROMS
REMARK 300 IN ADDITION, THERE IS 3-FOLD CIRCULAR
REMARK 300 SYMMETRY AROUND THE HELIX AXIS
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 0.734997 0.678070 0.000000 0.00000
REMARK 350 BIOMT2 1 -0.678070 0.734997 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -23.19800
REMARK 350 BIOMT1 2 0.219727 -0.975561 0.000000 0.00000
REMARK 350 BIOMT2 2 0.975561 0.219727 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -23.19800
REMARK 350 BIOMT1 3 -0.954724 0.297492 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.297492 -0.954724 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -23.19800
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 5 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 7 0.734997 -0.678070 0.000000 0.00000
REMARK 350 BIOMT2 7 0.678070 0.734997 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 1.000000 23.19800
REMARK 350 BIOMT1 8 -0.954724 -0.297492 0.000000 0.00000
REMARK 350 BIOMT2 8 0.297492 -0.954724 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 1.000000 23.19800
REMARK 350 BIOMT1 9 0.219727 0.975561 0.000000 0.00000
REMARK 350 BIOMT2 9 -0.975561 0.219727 0.000000 0.00000
REMARK 350 BIOMT3 9 0.000000 0.000000 1.000000 23.19800
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 -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 GLN A 365
REMARK 465 ALA A 366
REMARK 465 ARG A 367
REMARK 465 LEU A 368
REMARK 465 ASP A 369
REMARK 465 ASP A 370
REMARK 465 SER A 371
REMARK 465 PRO A 372
REMARK 465 ARG A 373
REMARK 465 GLY A 374
REMARK 465 PRO A 375
REMARK 465 GLY A 376
REMARK 465 GLN A 377
REMARK 465 GLY B -4
REMARK 465 PRO B -3
REMARK 465 LEU B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ALA B 362
REMARK 465 PHE B 363
REMARK 465 SER B 364
REMARK 465 GLN B 365
REMARK 465 ALA B 366
REMARK 465 ARG B 367
REMARK 465 LEU B 368
REMARK 465 ASP B 369
REMARK 465 ASP B 370
REMARK 465 SER B 371
REMARK 465 PRO B 372
REMARK 465 ARG B 373
REMARK 465 GLY B 374
REMARK 465 PRO B 375
REMARK 465 GLY B 376
REMARK 465 GLN B 377
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 LEU C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 GLN C 365
REMARK 465 ALA C 366
REMARK 465 ARG C 367
REMARK 465 LEU C 368
REMARK 465 ASP C 369
REMARK 465 ASP C 370
REMARK 465 SER C 371
REMARK 465 PRO C 372
REMARK 465 ARG C 373
REMARK 465 GLY C 374
REMARK 465 PRO C 375
REMARK 465 GLY C 376
REMARK 465 GLN C 377
REMARK 465 GLY D -4
REMARK 465 PRO D -3
REMARK 465 LEU D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 ALA D 362
REMARK 465 PHE D 363
REMARK 465 SER D 364
REMARK 465 GLN D 365
REMARK 465 ALA D 366
REMARK 465 ARG D 367
REMARK 465 LEU D 368
REMARK 465 ASP D 369
REMARK 465 ASP D 370
REMARK 465 SER D 371
REMARK 465 PRO D 372
REMARK 465 ARG D 373
REMARK 465 GLY D 374
REMARK 465 PRO D 375
REMARK 465 GLY D 376
REMARK 465 GLN D 377
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 HZ3 LYS D 114 OE2 GLU D 115 1.50
REMARK 500 HH12 ARG C 160 OE2 GLU D 253 1.50
REMARK 500 OD2 ASP A 13 HE ARG A 18 1.51
REMARK 500 HZ1 LYS A 235 OD2 ASP B 182 1.51
REMARK 500 HH21 ARG B 260 OE2 GLU B 269 1.51
REMARK 500 OE2 GLU C 234 HZ3 LYS C 235 1.54
REMARK 500 OE2 GLU B 32 HH21 ARG B 121 1.55
REMARK 500 HG SER B 86 OE1 GLU B 209 1.55
REMARK 500 OE1 GLU A 208 HH21 ARG A 212 1.56
REMARK 500 HZ2 LYS D 90 OE1 GLU D 209 1.56
REMARK 500 O TYR C 52 HG SER C 56 1.57
REMARK 500 HZ3 LYS C 302 OE1 GLU D 22 1.57
REMARK 500 HH22 ARG A 325 OE2 GLU B 143 1.57
REMARK 500 HZ2 LYS C 318 OE2 GLU C 330 1.57
REMARK 500 OE1 GLU A 143 HH11 ARG B 325 1.57
REMARK 500 HE ARG A 194 OE2 GLU A 197 1.57
REMARK 500 OE1 GLU B 78 HZ3 LYS B 82 1.57
REMARK 500 OD1 ASP D 182 HZ3 LYS D 185 1.58
REMARK 500 OE1 GLU B 208 HH11 ARG B 212 1.58
REMARK 500 OD2 ASP D 126 HH22 ARG D 129 1.58
REMARK 500 HH11 ARG D 241 OE1 GLU D 249 1.58
REMARK 500 HH12 ARG C 50 OD1 ASP C 99 1.58
REMARK 500 OD2 ASP A 126 HE ARG A 169 1.58
REMARK 500 HG SER D 86 OE2 GLU D 209 1.59
REMARK 500 HH12 ARG A 147 OE2 GLU B 324 1.59
REMARK 500 HE ARG C 163 OE2 GLU D 254 1.59
REMARK 500 HH11 ARG A 275 OE2 GLU A 324 1.59
REMARK 500 HH11 ARG C 260 OE2 GLU C 269 1.59
REMARK 500 OE2 GLU D 32 HH21 ARG D 121 1.59
REMARK 500 OE2 GLU A 208 HH11 ARG A 212 1.59
REMARK 500 HH11 ARG C 236 OE1 GLU C 239 1.59
REMARK 500 HH12 ARG C 34 OD1 ASP D 65 1.59
REMARK 500 HZ1 LYS C 235 OD2 ASP D 182 1.59
REMARK 500 OE1 GLU C 253 HG SER C 344 1.60
REMARK 500 OD2 ASP B 13 HH TYR B 166 1.60
REMARK 500 HH11 ARG D 260 OE2 GLU D 269 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 166 CG TYR A 166 CD1 0.083
REMARK 500 GLU A 239 CD GLU A 239 OE1 0.074
REMARK 500 SER A 361 CA SER A 361 CB 0.093
REMARK 500 SER B 48 CA SER B 48 CB 0.098
REMARK 500 HIS B 51 CG HIS B 51 CD2 0.054
REMARK 500 GLU B 78 CB GLU B 78 CG 0.135
REMARK 500 GLU B 122 CB GLU B 122 CG 0.120
REMARK 500 TRP B 287 CE2 TRP B 287 CD2 0.098
REMARK 500 ARG B 326 CZ ARG B 326 NH1 -0.079
REMARK 500 GLU C 151 CB GLU C 151 CG 0.126
REMARK 500 ARG C 169 N ARG C 169 CA -0.120
REMARK 500 PHE C 191 CB PHE C 191 CG -0.105
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 A 6 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 GLU A 27 OE1 - CD - OE2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 HIS A 51 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 MET A 76 CG - SD - CE ANGL. DEV. = -13.8 DEGREES
REMARK 500 PHE A 83 CB - CG - CD2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 PHE A 83 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 PHE A 127 CB - CG - CD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 146 NH1 - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 160 NH1 - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 163 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 163 NE - CZ - NH2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 TYR A 166 CB - CG - CD2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 TYR A 166 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 167 NH1 - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG A 167 NE - CZ - NH2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 TYR A 173 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 184 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 187 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP A 187 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 212 NE - CZ - NH2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TYR A 216 CB - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TYR A 216 CB - CG - CD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 236 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 236 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 237 CB - CG - OD1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP A 237 CB - CG - OD2 ANGL. DEV. = -8.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 268 ANGLE DEVIATIONS.
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 13 53.78 71.41
REMARK 500 GLN A 108 -89.49 -97.08
REMARK 500 ARG A 148 55.20 -100.94
REMARK 500 LYS A 248 17.62 -160.79
REMARK 500 GLU A 249 11.38 -152.83
REMARK 500 GLU A 261 24.71 87.53
REMARK 500 LEU A 266 106.02 -8.84
REMARK 500 ASN A 293 23.24 85.98
REMARK 500 VAL A 308 -68.54 -108.12
REMARK 500 LYS B 4 77.63 42.12
REMARK 500 GLU B 115 20.76 -157.41
REMARK 500 PRO B 145 127.08 -34.20
REMARK 500 ALA B 149 -34.32 -130.71
REMARK 500 PRO B 255 133.51 -31.93
REMARK 500 PRO B 257 170.37 -43.42
REMARK 500 LYS B 281 35.21 80.79
REMARK 500 LYS B 302 -34.34 79.31
REMARK 500 GLN C 108 -90.10 -96.67
REMARK 500 ARG C 148 34.82 -86.50
REMARK 500 LYS C 248 8.58 -160.19
REMARK 500 GLU C 249 10.31 -151.96
REMARK 500 GLU C 261 26.60 83.92
REMARK 500 LEU C 266 73.62 18.80
REMARK 500 ASN C 293 34.67 70.88
REMARK 500 VAL C 308 -68.14 -94.45
REMARK 500 LEU C 314 56.96 -140.38
REMARK 500 CYS C 320 115.66 -36.27
REMARK 500 SER C 323 154.37 154.08
REMARK 500 LYS C 336 115.84 76.73
REMARK 500 PRO D 71 165.87 -47.38
REMARK 500 GLU D 115 21.88 -156.41
REMARK 500 ALA D 149 -33.04 -133.17
REMARK 500 PRO D 257 150.81 -34.94
REMARK 500 PRO D 263 106.10 -59.85
REMARK 500 ALA D 276 -147.52 -106.83
REMARK 500 ALA D 279 -138.85 39.22
REMARK 500 LYS D 299 -77.83 -106.57
REMARK 500 PRO D 304 131.85 -33.24
REMARK 500 PHE D 327 59.76 70.18
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 GLU A 115 GLY A 116 -147.16
REMARK 500 PHE C 280 LYS C 281 -148.75
REMARK 500 ASP D 6 PHE D 7 -147.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 17 0.08 SIDE CHAIN
REMARK 500 ARG A 34 0.16 SIDE CHAIN
REMARK 500 ARG A 125 0.11 SIDE CHAIN
REMARK 500 PHE A 127 0.07 SIDE CHAIN
REMARK 500 ARG A 129 0.13 SIDE CHAIN
REMARK 500 ARG A 169 0.10 SIDE CHAIN
REMARK 500 ARG A 236 0.20 SIDE CHAIN
REMARK 500 ARG A 260 0.15 SIDE CHAIN
REMARK 500 HIS A 271 0.08 SIDE CHAIN
REMARK 500 TYR A 297 0.09 SIDE CHAIN
REMARK 500 ARG A 313 0.10 SIDE CHAIN
REMARK 500 HIS B 51 0.12 SIDE CHAIN
REMARK 500 PHE B 120 0.08 SIDE CHAIN
REMARK 500 ARG B 121 0.09 SIDE CHAIN
REMARK 500 ARG B 124 0.10 SIDE CHAIN
REMARK 500 ARG B 160 0.12 SIDE CHAIN
REMARK 500 ARG B 169 0.16 SIDE CHAIN
REMARK 500 TYR B 216 0.07 SIDE CHAIN
REMARK 500 ARG B 241 0.14 SIDE CHAIN
REMARK 500 PHE B 273 0.07 SIDE CHAIN
REMARK 500 ARG B 346 0.15 SIDE CHAIN
REMARK 500 ARG C 34 0.23 SIDE CHAIN
REMARK 500 ARG C 57 0.11 SIDE CHAIN
REMARK 500 ARG C 68 0.16 SIDE CHAIN
REMARK 500 ARG C 118 0.16 SIDE CHAIN
REMARK 500 ARG C 125 0.11 SIDE CHAIN
REMARK 500 ARG C 160 0.21 SIDE CHAIN
REMARK 500 ARG C 169 0.08 SIDE CHAIN
REMARK 500 ARG C 184 0.14 SIDE CHAIN
REMARK 500 PHE C 186 0.08 SIDE CHAIN
REMARK 500 TYR C 216 0.16 SIDE CHAIN
REMARK 500 ARG C 285 0.12 SIDE CHAIN
REMARK 500 PHE D 7 0.08 SIDE CHAIN
REMARK 500 ARG D 57 0.15 SIDE CHAIN
REMARK 500 ARG D 68 0.07 SIDE CHAIN
REMARK 500 ARG D 129 0.12 SIDE CHAIN
REMARK 500 ARG D 148 0.09 SIDE CHAIN
REMARK 500 ARG D 167 0.07 SIDE CHAIN
REMARK 500 TYR D 173 0.12 SIDE CHAIN
REMARK 500 ARG D 184 0.12 SIDE CHAIN
REMARK 500 ARG D 233 0.08 SIDE CHAIN
REMARK 500 HIS D 271 0.09 SIDE CHAIN
REMARK 500 PHE D 273 0.09 SIDE CHAIN
REMARK 500 ARG D 275 0.10 SIDE CHAIN
REMARK 500 ARG D 285 0.15 SIDE CHAIN
REMARK 500 PHE D 288 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CKG RELATED DB: PDB
REMARK 900 RELATED ID: EMD-2546 RELATED DB: EMDB
DBREF 5H3D A 1 377 UNP Q15027 ACAP1_HUMAN 1 377
DBREF 5H3D B 1 377 UNP Q15027 ACAP1_HUMAN 1 377
DBREF 5H3D C 1 377 UNP Q15027 ACAP1_HUMAN 1 377
DBREF 5H3D D 1 377 UNP Q15027 ACAP1_HUMAN 1 377
SEQADV 5H3D GLY A -4 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D PRO A -3 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D LEU A -2 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY A -1 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D SER A 0 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY B -4 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D PRO B -3 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D LEU B -2 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY B -1 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D SER B 0 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY C -4 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D PRO C -3 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D LEU C -2 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY C -1 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D SER C 0 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY D -4 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D PRO D -3 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D LEU D -2 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D GLY D -1 UNP Q15027 EXPRESSION TAG
SEQADV 5H3D SER D 0 UNP Q15027 EXPRESSION TAG
SEQRES 1 A 382 GLY PRO LEU GLY SER MET THR VAL LYS LEU ASP PHE GLU
SEQRES 2 A 382 GLU CYS LEU LYS ASP SER PRO ARG PHE ARG ALA SER ILE
SEQRES 3 A 382 GLU LEU VAL GLU ALA GLU VAL SER GLU LEU GLU THR ARG
SEQRES 4 A 382 LEU GLU LYS LEU LEU LYS LEU GLY THR GLY LEU LEU GLU
SEQRES 5 A 382 SER GLY ARG HIS TYR LEU ALA ALA SER ARG ALA PHE VAL
SEQRES 6 A 382 VAL GLY ILE CYS ASP LEU ALA ARG LEU GLY PRO PRO GLU
SEQRES 7 A 382 PRO MET MET ALA GLU CYS LEU GLU LYS PHE THR VAL SER
SEQRES 8 A 382 LEU ASN HIS LYS LEU ASP SER HIS ALA GLU LEU LEU ASP
SEQRES 9 A 382 ALA THR GLN HIS THR LEU GLN GLN GLN ILE GLN THR LEU
SEQRES 10 A 382 VAL LYS GLU GLY LEU ARG GLY PHE ARG GLU ALA ARG ARG
SEQRES 11 A 382 ASP PHE TRP ARG GLY ALA GLU SER LEU GLU ALA ALA LEU
SEQRES 12 A 382 THR HIS ASN ALA GLU VAL PRO ARG ARG ARG ALA GLN GLU
SEQRES 13 A 382 ALA GLU GLU ALA GLY ALA ALA LEU ARG THR ALA ARG ALA
SEQRES 14 A 382 GLY TYR ARG GLY ARG ALA LEU ASP TYR ALA LEU GLN ILE
SEQRES 15 A 382 ASN VAL ILE GLU ASP LYS ARG LYS PHE ASP ILE MET GLU
SEQRES 16 A 382 PHE VAL LEU ARG LEU VAL GLU ALA GLN ALA THR HIS PHE
SEQRES 17 A 382 GLN GLN GLY HIS GLU GLU LEU SER ARG LEU SER GLN TYR
SEQRES 18 A 382 ARG LYS GLU LEU GLY ALA GLN LEU HIS GLN LEU VAL LEU
SEQRES 19 A 382 ASN SER ALA ARG GLU LYS ARG ASP MET GLU GLN ARG HIS
SEQRES 20 A 382 VAL LEU LEU LYS GLN LYS GLU LEU GLY GLY GLU GLU PRO
SEQRES 21 A 382 GLU PRO SER LEU ARG GLU GLY PRO GLY GLY LEU VAL MET
SEQRES 22 A 382 GLU GLY HIS LEU PHE LYS ARG ALA SER ASN ALA PHE LYS
SEQRES 23 A 382 THR TRP SER ARG ARG TRP PHE THR ILE GLN SER ASN GLN
SEQRES 24 A 382 LEU VAL TYR GLN LYS LYS TYR LYS ASP PRO VAL THR VAL
SEQRES 25 A 382 VAL VAL ASP ASP LEU ARG LEU CYS THR VAL LYS LEU CYS
SEQRES 26 A 382 PRO ASP SER GLU ARG ARG PHE CYS PHE GLU VAL VAL SER
SEQRES 27 A 382 THR SER LYS SER CYS LEU LEU GLN ALA ASP SER GLU ARG
SEQRES 28 A 382 LEU LEU GLN LEU TRP VAL SER ALA VAL GLN SER SER ILE
SEQRES 29 A 382 ALA SER ALA PHE SER GLN ALA ARG LEU ASP ASP SER PRO
SEQRES 30 A 382 ARG GLY PRO GLY GLN
SEQRES 1 B 382 GLY PRO LEU GLY SER MET THR VAL LYS LEU ASP PHE GLU
SEQRES 2 B 382 GLU CYS LEU LYS ASP SER PRO ARG PHE ARG ALA SER ILE
SEQRES 3 B 382 GLU LEU VAL GLU ALA GLU VAL SER GLU LEU GLU THR ARG
SEQRES 4 B 382 LEU GLU LYS LEU LEU LYS LEU GLY THR GLY LEU LEU GLU
SEQRES 5 B 382 SER GLY ARG HIS TYR LEU ALA ALA SER ARG ALA PHE VAL
SEQRES 6 B 382 VAL GLY ILE CYS ASP LEU ALA ARG LEU GLY PRO PRO GLU
SEQRES 7 B 382 PRO MET MET ALA GLU CYS LEU GLU LYS PHE THR VAL SER
SEQRES 8 B 382 LEU ASN HIS LYS LEU ASP SER HIS ALA GLU LEU LEU ASP
SEQRES 9 B 382 ALA THR GLN HIS THR LEU GLN GLN GLN ILE GLN THR LEU
SEQRES 10 B 382 VAL LYS GLU GLY LEU ARG GLY PHE ARG GLU ALA ARG ARG
SEQRES 11 B 382 ASP PHE TRP ARG GLY ALA GLU SER LEU GLU ALA ALA LEU
SEQRES 12 B 382 THR HIS ASN ALA GLU VAL PRO ARG ARG ARG ALA GLN GLU
SEQRES 13 B 382 ALA GLU GLU ALA GLY ALA ALA LEU ARG THR ALA ARG ALA
SEQRES 14 B 382 GLY TYR ARG GLY ARG ALA LEU ASP TYR ALA LEU GLN ILE
SEQRES 15 B 382 ASN VAL ILE GLU ASP LYS ARG LYS PHE ASP ILE MET GLU
SEQRES 16 B 382 PHE VAL LEU ARG LEU VAL GLU ALA GLN ALA THR HIS PHE
SEQRES 17 B 382 GLN GLN GLY HIS GLU GLU LEU SER ARG LEU SER GLN TYR
SEQRES 18 B 382 ARG LYS GLU LEU GLY ALA GLN LEU HIS GLN LEU VAL LEU
SEQRES 19 B 382 ASN SER ALA ARG GLU LYS ARG ASP MET GLU GLN ARG HIS
SEQRES 20 B 382 VAL LEU LEU LYS GLN LYS GLU LEU GLY GLY GLU GLU PRO
SEQRES 21 B 382 GLU PRO SER LEU ARG GLU GLY PRO GLY GLY LEU VAL MET
SEQRES 22 B 382 GLU GLY HIS LEU PHE LYS ARG ALA SER ASN ALA PHE LYS
SEQRES 23 B 382 THR TRP SER ARG ARG TRP PHE THR ILE GLN SER ASN GLN
SEQRES 24 B 382 LEU VAL TYR GLN LYS LYS TYR LYS ASP PRO VAL THR VAL
SEQRES 25 B 382 VAL VAL ASP ASP LEU ARG LEU CYS THR VAL LYS LEU CYS
SEQRES 26 B 382 PRO ASP SER GLU ARG ARG PHE CYS PHE GLU VAL VAL SER
SEQRES 27 B 382 THR SER LYS SER CYS LEU LEU GLN ALA ASP SER GLU ARG
SEQRES 28 B 382 LEU LEU GLN LEU TRP VAL SER ALA VAL GLN SER SER ILE
SEQRES 29 B 382 ALA SER ALA PHE SER GLN ALA ARG LEU ASP ASP SER PRO
SEQRES 30 B 382 ARG GLY PRO GLY GLN
SEQRES 1 C 382 GLY PRO LEU GLY SER MET THR VAL LYS LEU ASP PHE GLU
SEQRES 2 C 382 GLU CYS LEU LYS ASP SER PRO ARG PHE ARG ALA SER ILE
SEQRES 3 C 382 GLU LEU VAL GLU ALA GLU VAL SER GLU LEU GLU THR ARG
SEQRES 4 C 382 LEU GLU LYS LEU LEU LYS LEU GLY THR GLY LEU LEU GLU
SEQRES 5 C 382 SER GLY ARG HIS TYR LEU ALA ALA SER ARG ALA PHE VAL
SEQRES 6 C 382 VAL GLY ILE CYS ASP LEU ALA ARG LEU GLY PRO PRO GLU
SEQRES 7 C 382 PRO MET MET ALA GLU CYS LEU GLU LYS PHE THR VAL SER
SEQRES 8 C 382 LEU ASN HIS LYS LEU ASP SER HIS ALA GLU LEU LEU ASP
SEQRES 9 C 382 ALA THR GLN HIS THR LEU GLN GLN GLN ILE GLN THR LEU
SEQRES 10 C 382 VAL LYS GLU GLY LEU ARG GLY PHE ARG GLU ALA ARG ARG
SEQRES 11 C 382 ASP PHE TRP ARG GLY ALA GLU SER LEU GLU ALA ALA LEU
SEQRES 12 C 382 THR HIS ASN ALA GLU VAL PRO ARG ARG ARG ALA GLN GLU
SEQRES 13 C 382 ALA GLU GLU ALA GLY ALA ALA LEU ARG THR ALA ARG ALA
SEQRES 14 C 382 GLY TYR ARG GLY ARG ALA LEU ASP TYR ALA LEU GLN ILE
SEQRES 15 C 382 ASN VAL ILE GLU ASP LYS ARG LYS PHE ASP ILE MET GLU
SEQRES 16 C 382 PHE VAL LEU ARG LEU VAL GLU ALA GLN ALA THR HIS PHE
SEQRES 17 C 382 GLN GLN GLY HIS GLU GLU LEU SER ARG LEU SER GLN TYR
SEQRES 18 C 382 ARG LYS GLU LEU GLY ALA GLN LEU HIS GLN LEU VAL LEU
SEQRES 19 C 382 ASN SER ALA ARG GLU LYS ARG ASP MET GLU GLN ARG HIS
SEQRES 20 C 382 VAL LEU LEU LYS GLN LYS GLU LEU GLY GLY GLU GLU PRO
SEQRES 21 C 382 GLU PRO SER LEU ARG GLU GLY PRO GLY GLY LEU VAL MET
SEQRES 22 C 382 GLU GLY HIS LEU PHE LYS ARG ALA SER ASN ALA PHE LYS
SEQRES 23 C 382 THR TRP SER ARG ARG TRP PHE THR ILE GLN SER ASN GLN
SEQRES 24 C 382 LEU VAL TYR GLN LYS LYS TYR LYS ASP PRO VAL THR VAL
SEQRES 25 C 382 VAL VAL ASP ASP LEU ARG LEU CYS THR VAL LYS LEU CYS
SEQRES 26 C 382 PRO ASP SER GLU ARG ARG PHE CYS PHE GLU VAL VAL SER
SEQRES 27 C 382 THR SER LYS SER CYS LEU LEU GLN ALA ASP SER GLU ARG
SEQRES 28 C 382 LEU LEU GLN LEU TRP VAL SER ALA VAL GLN SER SER ILE
SEQRES 29 C 382 ALA SER ALA PHE SER GLN ALA ARG LEU ASP ASP SER PRO
SEQRES 30 C 382 ARG GLY PRO GLY GLN
SEQRES 1 D 382 GLY PRO LEU GLY SER MET THR VAL LYS LEU ASP PHE GLU
SEQRES 2 D 382 GLU CYS LEU LYS ASP SER PRO ARG PHE ARG ALA SER ILE
SEQRES 3 D 382 GLU LEU VAL GLU ALA GLU VAL SER GLU LEU GLU THR ARG
SEQRES 4 D 382 LEU GLU LYS LEU LEU LYS LEU GLY THR GLY LEU LEU GLU
SEQRES 5 D 382 SER GLY ARG HIS TYR LEU ALA ALA SER ARG ALA PHE VAL
SEQRES 6 D 382 VAL GLY ILE CYS ASP LEU ALA ARG LEU GLY PRO PRO GLU
SEQRES 7 D 382 PRO MET MET ALA GLU CYS LEU GLU LYS PHE THR VAL SER
SEQRES 8 D 382 LEU ASN HIS LYS LEU ASP SER HIS ALA GLU LEU LEU ASP
SEQRES 9 D 382 ALA THR GLN HIS THR LEU GLN GLN GLN ILE GLN THR LEU
SEQRES 10 D 382 VAL LYS GLU GLY LEU ARG GLY PHE ARG GLU ALA ARG ARG
SEQRES 11 D 382 ASP PHE TRP ARG GLY ALA GLU SER LEU GLU ALA ALA LEU
SEQRES 12 D 382 THR HIS ASN ALA GLU VAL PRO ARG ARG ARG ALA GLN GLU
SEQRES 13 D 382 ALA GLU GLU ALA GLY ALA ALA LEU ARG THR ALA ARG ALA
SEQRES 14 D 382 GLY TYR ARG GLY ARG ALA LEU ASP TYR ALA LEU GLN ILE
SEQRES 15 D 382 ASN VAL ILE GLU ASP LYS ARG LYS PHE ASP ILE MET GLU
SEQRES 16 D 382 PHE VAL LEU ARG LEU VAL GLU ALA GLN ALA THR HIS PHE
SEQRES 17 D 382 GLN GLN GLY HIS GLU GLU LEU SER ARG LEU SER GLN TYR
SEQRES 18 D 382 ARG LYS GLU LEU GLY ALA GLN LEU HIS GLN LEU VAL LEU
SEQRES 19 D 382 ASN SER ALA ARG GLU LYS ARG ASP MET GLU GLN ARG HIS
SEQRES 20 D 382 VAL LEU LEU LYS GLN LYS GLU LEU GLY GLY GLU GLU PRO
SEQRES 21 D 382 GLU PRO SER LEU ARG GLU GLY PRO GLY GLY LEU VAL MET
SEQRES 22 D 382 GLU GLY HIS LEU PHE LYS ARG ALA SER ASN ALA PHE LYS
SEQRES 23 D 382 THR TRP SER ARG ARG TRP PHE THR ILE GLN SER ASN GLN
SEQRES 24 D 382 LEU VAL TYR GLN LYS LYS TYR LYS ASP PRO VAL THR VAL
SEQRES 25 D 382 VAL VAL ASP ASP LEU ARG LEU CYS THR VAL LYS LEU CYS
SEQRES 26 D 382 PRO ASP SER GLU ARG ARG PHE CYS PHE GLU VAL VAL SER
SEQRES 27 D 382 THR SER LYS SER CYS LEU LEU GLN ALA ASP SER GLU ARG
SEQRES 28 D 382 LEU LEU GLN LEU TRP VAL SER ALA VAL GLN SER SER ILE
SEQRES 29 D 382 ALA SER ALA PHE SER GLN ALA ARG LEU ASP ASP SER PRO
SEQRES 30 D 382 ARG GLY PRO GLY GLN
HELIX 1 AA1 MET A 1 LEU A 5 5 5
HELIX 2 AA2 SER A 14 LEU A 69 1 56
HELIX 3 AA3 GLU A 73 GLN A 108 1 36
HELIX 4 AA4 GLN A 108 GLY A 116 1 9
HELIX 5 AA5 LEU A 117 VAL A 144 1 28
HELIX 6 AA6 ARG A 148 GLU A 209 1 62
HELIX 7 AA7 GLU A 209 GLU A 249 1 41
HELIX 8 AA8 SER A 344 SER A 364 1 21
HELIX 9 AA9 PHE B 7 ASP B 13 1 7
HELIX 10 AB1 SER B 14 ARG B 68 1 55
HELIX 11 AB2 GLU B 73 GLU B 78 1 6
HELIX 12 AB3 GLU B 78 GLY B 116 1 39
HELIX 13 AB4 LEU B 117 GLU B 143 1 27
HELIX 14 AB5 ALA B 149 GLU B 249 1 101
HELIX 15 AB6 ASP B 311 ARG B 313 5 3
HELIX 16 AB7 SER B 344 ALA B 360 1 17
HELIX 17 AB8 MET C 1 LEU C 5 5 5
HELIX 18 AB9 SER C 14 GLY C 70 1 57
HELIX 19 AC1 GLU C 73 GLN C 108 1 36
HELIX 20 AC2 GLN C 108 GLY C 116 1 9
HELIX 21 AC3 LEU C 117 GLU C 143 1 27
HELIX 22 AC4 ARG C 148 GLU C 209 1 62
HELIX 23 AC5 GLU C 209 GLU C 249 1 41
HELIX 24 AC6 GLU C 261 LEU C 266 1 6
HELIX 25 AC7 SER C 344 SER C 364 1 21
HELIX 26 AC8 ASP D 6 LYS D 12 1 7
HELIX 27 AC9 SER D 14 GLY D 70 1 57
HELIX 28 AD1 GLU D 73 GLU D 78 1 6
HELIX 29 AD2 GLU D 78 GLY D 116 1 39
HELIX 30 AD3 LEU D 117 ASN D 141 1 25
HELIX 31 AD4 ALA D 149 GLU D 249 1 101
HELIX 32 AD5 SER D 344 ALA D 360 1 17
SHEET 1 AA1 7 THR A 306 VAL A 309 0
SHEET 2 AA1 7 GLN A 294 GLN A 298 -1 N LEU A 295 O VAL A 308
SHEET 3 AA1 7 SER A 284 GLN A 291 -1 N THR A 289 O VAL A 296
SHEET 4 AA1 7 MET A 268 ARG A 275 -1 N MET A 268 O ILE A 290
SHEET 5 AA1 7 CYS A 338 GLN A 341 -1 O GLN A 341 N PHE A 273
SHEET 6 AA1 7 CYS A 328 VAL A 332 -1 N PHE A 329 O LEU A 340
SHEET 7 AA1 7 THR A 316 LEU A 319 -1 N LYS A 318 O GLU A 330
SHEET 1 AA2 5 ARG B 260 GLY B 262 0
SHEET 2 AA2 5 GLY B 265 ARG B 275 -1 O VAL B 267 N ARG B 260
SHEET 3 AA2 5 TRP B 283 ILE B 290 -1 O ARG B 286 N LEU B 272
SHEET 4 AA2 5 LEU B 295 TYR B 297 -1 O VAL B 296 N THR B 289
SHEET 5 AA2 5 THR B 306 VAL B 309 -1 O THR B 306 N TYR B 297
SHEET 1 AA3 3 CYS B 315 LYS B 318 0
SHEET 2 AA3 3 CYS B 328 SER B 333 -1 O GLU B 330 N LYS B 318
SHEET 3 AA3 3 SER B 337 GLN B 341 -1 O CYS B 338 N VAL B 331
SHEET 1 AA4 7 THR C 306 VAL C 309 0
SHEET 2 AA4 7 GLN C 294 GLN C 298 -1 N LEU C 295 O VAL C 308
SHEET 3 AA4 7 SER C 284 GLN C 291 -1 N TRP C 287 O GLN C 298
SHEET 4 AA4 7 MET C 268 ARG C 275 -1 N LYS C 274 O SER C 284
SHEET 5 AA4 7 CYS C 338 GLN C 341 -1 O GLN C 341 N PHE C 273
SHEET 6 AA4 7 CYS C 328 SER C 333 -1 N PHE C 329 O LEU C 340
SHEET 7 AA4 7 CYS C 315 LEU C 319 -1 N LYS C 318 O GLU C 330
SHEET 1 AA5 4 MET D 268 ARG D 275 0
SHEET 2 AA5 4 TRP D 283 GLN D 291 -1 O ILE D 290 N MET D 268
SHEET 3 AA5 4 GLN D 294 GLN D 298 -1 O GLN D 298 N TRP D 287
SHEET 4 AA5 4 VAL D 305 VAL D 309 -1 O VAL D 308 N LEU D 295
SHEET 1 AA6 3 THR D 316 LYS D 318 0
SHEET 2 AA6 3 CYS D 328 VAL D 332 -1 O GLU D 330 N LYS D 318
SHEET 3 AA6 3 SER D 337 GLN D 341 -1 O CYS D 338 N VAL D 331
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
